|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
1-397 |
0e+00 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 818.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 1 MSSAFYQQIQTQIEEVKEEGLYKSERIITSAQKAAVSISTGEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVR 80
Cdd:PRK06939 1 MSGAFYAQLREELEEIKAEGLYKEERVITSPQGADITVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 81 FICGTQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEE 160
Cdd:PRK06939 81 FICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 161 LEQQLIAAKEAGARHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITG 240
Cdd:PRK06939 161 LEAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 241 TLGKAMGGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTM 320
Cdd:PRK06939 241 TLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1596947121 321 GGADHAIIPIMLGDAKVAAEFAERALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVGKDMAII 397
Cdd:PRK06939 321 GPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
|
|
| 2am3keto_CoA |
TIGR01822 |
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ... |
5-397 |
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: 669.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 5 FYQQIQTQIEEVKEEGLYKSERIITSAQKAAVSISTGEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICG 84
Cdd:TIGR01822 1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVADGREVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFICG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 85 TQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQ 164
Cdd:TIGR01822 81 TQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 165 LIAAKEAGARHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITGTLGK 244
Cdd:TIGR01822 161 LKEARAAGARHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTLGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 245 AMGGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGAD 324
Cdd:TIGR01822 241 ALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKPAD 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1596947121 325 HAIIPIMLGDAKVAAEFAERALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVGKDMAII 397
Cdd:TIGR01822 321 HPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
5-393 |
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: 576.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 5 FYQQIQTQIEEVKEEGLYKSERIITSAQKAAVSIStGEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICG 84
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTID-GREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 85 TQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQ 164
Cdd:COG0156 80 TTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 165 LIAAKEagARHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITGTLGK 244
Cdd:COG0156 160 LKKARA--ARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 245 AMgGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGAD 324
Cdd:COG0156 238 AL-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1596947121 325 HAIIPIMLGDAKVAAEFAERALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVGKD 393
Cdd:COG0156 317 SPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
42-391 |
7.09e-166 |
|
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: 468.58 E-value: 7.09e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 42 EEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICGTQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFET 121
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 122 ILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQLIAAKEaGARHTLIVTDGVFSMDGVVANLPAICDLAD 201
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARR-PYGKKLIVTEGVYSMDGDIAPLPELVDLAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 202 KYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITGTLGKAmGGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAI 281
Cdd:cd06454 160 KYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKA-FGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 282 VSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGA-DHAIIPIMLGDAKVAAEFAERALEKGIYVVGFSFPVV 360
Cdd:cd06454 239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318
|
330 340 350
....*....|....*....|....*....|.
gi 1596947121 361 PKGQARIRTQMSAAHSREQLDRAIDAFVQVG 391
Cdd:cd06454 319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-387 |
5.07e-69 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 221.41 E-value: 5.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 42 EEVLNFCANNYLGLANhPDLIEAAKDgmdqhgFGMASVRFICGTQDSHKELEQKLSTFLG--------KEDTILYTSCFD 113
Cdd:pfam00155 1 TDKINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 114 ANAGLFETILG-KEDAIISDALNHASIIDGVRLCKAMRFRYA-------NNNMEELEQQLiaakeaGARHTLIVTDGVFS 185
Cdd:pfam00155 74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAAL------KEKPKVVLHTSPHN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 186 MDGVVANLPAICDLAD---KYGALVMVDDSHAVGFMGENGAGTHEFhNVVDRID-IITGTLGKAMG--GASGGYTSGKKE 259
Cdd:pfam00155 148 PTGTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVATRA-LLAEGPNlLVVGSFSKAFGlaGWRVGYILGNAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 260 VIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGADHAIIPIMLGDAKVAA 339
Cdd:pfam00155 227 VISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAK 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1596947121 340 EFAERAL-EKGIYVVGFSFPVVPkgqARIRTQMsAAHSREQLDRAIDAF 387
Cdd:pfam00155 307 ELAQVLLeEVGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
1-397 |
0e+00 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 818.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 1 MSSAFYQQIQTQIEEVKEEGLYKSERIITSAQKAAVSISTGEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVR 80
Cdd:PRK06939 1 MSGAFYAQLREELEEIKAEGLYKEERVITSPQGADITVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 81 FICGTQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEE 160
Cdd:PRK06939 81 FICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 161 LEQQLIAAKEAGARHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITG 240
Cdd:PRK06939 161 LEAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 241 TLGKAMGGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTM 320
Cdd:PRK06939 241 TLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1596947121 321 GGADHAIIPIMLGDAKVAAEFAERALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVGKDMAII 397
Cdd:PRK06939 321 GPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
|
|
| 2am3keto_CoA |
TIGR01822 |
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ... |
5-397 |
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: 669.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 5 FYQQIQTQIEEVKEEGLYKSERIITSAQKAAVSISTGEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICG 84
Cdd:TIGR01822 1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVADGREVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFICG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 85 TQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQ 164
Cdd:TIGR01822 81 TQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 165 LIAAKEAGARHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITGTLGK 244
Cdd:TIGR01822 161 LKEARAAGARHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTLGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 245 AMGGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGAD 324
Cdd:TIGR01822 241 ALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKPAD 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1596947121 325 HAIIPIMLGDAKVAAEFAERALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVGKDMAII 397
Cdd:TIGR01822 321 HPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
5-393 |
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: 576.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 5 FYQQIQTQIEEVKEEGLYKSERIITSAQKAAVSIStGEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICG 84
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTID-GREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 85 TQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQ 164
Cdd:COG0156 80 TTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 165 LIAAKEagARHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITGTLGK 244
Cdd:COG0156 160 LKKARA--ARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 245 AMgGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGAD 324
Cdd:COG0156 238 AL-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1596947121 325 HAIIPIMLGDAKVAAEFAERALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVGKD 393
Cdd:COG0156 317 SPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
42-391 |
7.09e-166 |
|
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: 468.58 E-value: 7.09e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 42 EEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICGTQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFET 121
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 122 ILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQLIAAKEaGARHTLIVTDGVFSMDGVVANLPAICDLAD 201
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARR-PYGKKLIVTEGVYSMDGDIAPLPELVDLAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 202 KYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITGTLGKAmGGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAI 281
Cdd:cd06454 160 KYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKA-FGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 282 VSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGA-DHAIIPIMLGDAKVAAEFAERALEKGIYVVGFSFPVV 360
Cdd:cd06454 239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318
|
330 340 350
....*....|....*....|....*....|.
gi 1596947121 361 PKGQARIRTQMSAAHSREQLDRAIDAFVQVG 391
Cdd:cd06454 319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
26-387 |
1.19e-127 |
|
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: 371.60 E-value: 1.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 26 RIITSAQKAAVSIStGEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICGTQDSHKELEQKLSTFLGKEDT 105
Cdd:TIGR00858 1 RPLDRGPGPEVVRD-GRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 106 ILYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQLiaAKEAGARHTLIVTDGVFS 185
Cdd:TIGR00858 80 LLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLL--EKNRGERRKLIVTDGVFS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 186 MDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNV-VDRIDIITGTLGKAMGGAsGGYTSGKKEVIDWL 264
Cdd:TIGR00858 158 MDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLkPEPVDIQVGTLSKALGSY-GAYVAGSQALIDYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 265 RQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGADHAIIPIMLGDAKVAAEFAER 344
Cdd:TIGR00858 237 INRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1596947121 345 ALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAF 387
Cdd:TIGR00858 317 LQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
4-391 |
3.08e-126 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 369.10 E-value: 3.08e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 4 AFYQQIQTQIEEVKEEGLYKSERIITSAQKAAVSIStGEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFIC 83
Cdd:PRK05958 2 SWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVD-GRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 84 GTQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQ 163
Cdd:PRK05958 81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 164 QLiaaKEAGARHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDII-TGTL 242
Cdd:PRK05958 161 LL---AKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVIlVGTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 243 GKAMgGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGG 322
Cdd:PRK05958 238 GKAL-GSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMD 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1596947121 323 ADHAIIPIMLGDAKVAAEFAERALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVG 391
Cdd:PRK05958 317 SQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
5-396 |
6.99e-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: 279.31 E-value: 6.99e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 5 FYQQIQTQIEEVKEEGLYKS----ERIITSAQKAAVSISTG-EEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASV 79
Cdd:TIGR01821 3 YDQFFNKEIDKLHLEGRYRVfadlERQAGEFPFAQWHRPDGaKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 80 RFICGTQDSHKELEQKLSTFLGKEDTILYTSCFDAN-AGLFetILGK---EDAIISDALNHASIIDGVRLCKAMRFRYAN 155
Cdd:TIGR01821 83 RNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLA--TLAKiipGCVIFSDELNHASMIEGIRHSGAEKFIFRH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 156 NNMEELEQQLIAAKEAgaRHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRI 235
Cdd:TIGR01821 161 NDVAHLEKLLQSVDPN--RPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 236 DIITGTLGKAMgGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEE 315
Cdd:TIGR01821 239 DIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 316 AGFTMGGADHAIIPIMLGDAKVAAEFAERALEK-GIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVGKDM 394
Cdd:TIGR01821 318 LGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKhGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRL 397
|
..
gi 1596947121 395 AI 396
Cdd:TIGR01821 398 GL 399
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
13-390 |
1.89e-83 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 260.56 E-value: 1.89e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 13 IEEVKEEGLYKS----ERIITSAQKAAVSISTGE-EVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICGTQD 87
Cdd:PRK13392 12 LAQLHQEGRYRVfadlEREAGRFPRARDHGPDGPrRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 88 SHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILGKEDA--IISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQL 165
Cdd:PRK13392 92 PHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGcvILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 166 iaAKEAGARHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITGTLGKA 245
Cdd:PRK13392 172 --ASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 246 MgGASGGYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGADH 325
Cdd:PRK13392 250 F-GCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPS 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1596947121 326 AIIPIMLGDAKVAAEFAERAL-EKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQV 390
Cdd:PRK13392 329 HIVPVMVGDPTLCKAISDRLMsEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAI 394
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
25-396 |
3.14e-71 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 231.19 E-value: 3.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 25 ERIITSAQKAAVSISTGEEVLNFCANNYLGLANH-----PDLIEAakdgMDQHGFGMASVRFICGTQDSHKELEQKLSTF 99
Cdd:PLN02483 83 ERVSNDNNKTLKRTTKTRRCLNLGSYNYLGFAAAdeyctPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 100 LGKEDTILYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQLIAAKEAGARHT--- 176
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRThrp 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 177 ----LIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDR-IDIITGTLGKAMgGASG 251
Cdd:PLN02483 239 wkkiIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSF-GSCG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 252 GYTSGKKEVIDWLRQRSRPYLFSNSVAPAIVS---ASIRVldLLAESGDLR-----TQLWENSAHFRTRMEEAGF-TMGG 322
Cdd:PLN02483 318 GYIAGSKELIQYLKRTCPAHLYATSMSPPAVQqviSAIKV--ILGEDGTNRgaqklAQIRENSNFFRSELQKMGFeVLGD 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1596947121 323 ADHAIIPIML-GDAKVAAeFAERALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVGKDMAI 396
Cdd:PLN02483 396 NDSPVMPIMLyNPAKIPA-FSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGI 469
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-387 |
5.07e-69 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 221.41 E-value: 5.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 42 EEVLNFCANNYLGLANhPDLIEAAKDgmdqhgFGMASVRFICGTQDSHKELEQKLSTFLG--------KEDTILYTSCFD 113
Cdd:pfam00155 1 TDKINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 114 ANAGLFETILG-KEDAIISDALNHASIIDGVRLCKAMRFRYA-------NNNMEELEQQLiaakeaGARHTLIVTDGVFS 185
Cdd:pfam00155 74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAAL------KEKPKVVLHTSPHN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 186 MDGVVANLPAICDLAD---KYGALVMVDDSHAVGFMGENGAGTHEFhNVVDRID-IITGTLGKAMG--GASGGYTSGKKE 259
Cdd:pfam00155 148 PTGTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVATRA-LLAEGPNlLVVGSFSKAFGlaGWRVGYILGNAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 260 VIDWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGADHAIIPIMLGDAKVAA 339
Cdd:pfam00155 227 VISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAK 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1596947121 340 EFAERAL-EKGIYVVGFSFPVVPkgqARIRTQMsAAHSREQLDRAIDAF 387
Cdd:pfam00155 307 ELAQVLLeEVGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
42-387 |
3.30e-55 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 189.12 E-value: 3.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 42 EEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICGTQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFET 121
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 122 I-------------LGKED-AIISDALNHASIIDGVRLCK----AMRFRYANNNMEELEQQLIAAKeagARHTLIVTDGV 183
Cdd:PLN02955 182 IgsvasllaasgkpLKNEKvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCK---MKRKVVVTDSL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 184 FSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNVVDRIDIITGTLGKAmGGASGGYTSGKKEVIDW 263
Cdd:PLN02955 259 FSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 264 LRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRtrmEEAGFTMGGadhAIIPIMLGDAKVAAEFAE 343
Cdd:PLN02955 338 IQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK---ALSGVDISS---PIISLVVGNQEKALKASR 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1596947121 344 RALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAF 387
Cdd:PLN02955 412 YLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
27-393 |
7.66e-53 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 182.63 E-value: 7.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 27 IITSAQKAAVSIStGEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICGTQDSHKELEQKLSTFLGKEDTI 106
Cdd:PLN02822 95 VLESAAGPHTIIN-GKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 107 LYTSCFDANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQL--IAAKEAGAR--HTLIVTDG 182
Cdd:PLN02822 174 LYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLekLTAENKRKKklRRYIVVEA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 183 VFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENGAGTHEFHNV-VDRIDIITGTLGKAMGGAsGGYTSGKKEVI 261
Cdd:PLN02822 254 IYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATE-GGFCTGSARVV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 262 DWLRQRSRPYLFSNSVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEE-AGFTMGGadHAIIPIML-------- 332
Cdd:PLN02822 333 DHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDiPGLSIGS--NTLSPIVFlhlekstg 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1596947121 333 ---GDAKVAAEFAERAL-EKGIYVVGFSFPVVPKGQ--ARIRTQMSAAHSREQLDRAIDAFVQVGKD 393
Cdd:PLN02822 411 sakEDLSLLEHIADRMLkEDSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESLKRVAAS 477
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
41-384 |
3.56e-52 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 179.05 E-value: 3.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 41 GEEVLNFCANNYLGLANHPDLIEAAKDGMDQHGFG--MASVrFICGTQDSHKeLEQKLSTFLGKEDTILYTSCFDANAGL 118
Cdd:PRK07179 53 GPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSlvMSAV-FLHDDSPKPQ-FEKKLAAFTGFESCLLCQSGWAANVGL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 119 FETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQLiaakeagARHT--LIVTDGVFSMDGVVANLPAI 196
Cdd:PRK07179 131 LQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQI-------ERHGpgIIVVDSVYSTTGTIAPLADI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 197 CDLADKYGALVMVDDSHAVGFMGENGAG-THEFhNVVDRIDIITGTLGKAMGGaSGGYTSGKKEVIDWLRQRSRPYLFSN 275
Cdd:PRK07179 204 VDIAEEFGCVLVVDESHSLGTHGPQGAGlVAEL-GLTSRVHFITASLAKAFAG-RAGIITCPRELAEYVPFVSYPAIFSS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 276 SVAPAIVSASIRVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGADHaIIPIMLG---DAKVAAEFAEralEKGIYV 352
Cdd:PRK07179 282 TLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ-IIALETGserNTEVLRDALE---ERNVFG 357
|
330 340 350
....*....|....*....|....*....|..
gi 1596947121 353 VGFSFPVVPKGQARIRTQMSAAHSREQLDRAI 384
Cdd:PRK07179 358 AVFCAPATPKNRNLIRLSLNADLTASDLDRVL 389
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
28-393 |
5.96e-44 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 157.06 E-value: 5.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 28 ITSAQKAAVSIST--GEEVLNFCANNYLGLANHPDLIEAAKDGMDQHG-FGMASVRFICGTQdSHKELEQKLSTFLGKEd 104
Cdd:PRK07505 30 LTVGEREGILITLadGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGsLHLSSSRTRVRSQ-ILKDLEEALSELFGAS- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 105 TILYTSCFDANAGLFETIL------GKEDAIISDALNHASIIDGVRLCK--AMRFRYANNNMEELEQqliAAKeaGARHT 176
Cdd:PRK07505 108 VLTFTSCSAAHLGILPLLAsghltgGVPPHMVFDKNAHASLNILKGICAdeTEVETIDHNDLDALED---ICK--TNKTV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 177 LIVTDGVFSMDGVvANLPAICDLADKYGALVMVDDSHAVGFMGENGAG---THEFHNVVDRIdIITGTLGKAMGGASGGY 253
Cdd:PRK07505 183 AYVADGVYSMGGI-APVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvrSELDYRLNERT-IIAASLGKAFGASGGVI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 254 TSGKKEVIDWLRQRSRPYLFSNSV-APAI--VSASIRvLDLLAESGDLRTQLWENSAHFRTRM--EEAGFTMggadhAII 328
Cdd:PRK07505 261 MLGDAEQIELILRYAGPLAFSQSLnVAALgaILASAE-IHLSEELDQLQQKLQNNIALFDSLIptEQSGSFL-----PIR 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1596947121 329 PIMLGDAKVAAEFAERALEKGIYVVGFSFPVVPKGQARIRTQMSAAHSREQLDRAIDAFVQVGKD 393
Cdd:PRK07505 335 LIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDE 399
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
45-386 |
4.96e-39 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 143.89 E-value: 4.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 45 LNFCANNYLGLANHPDLIEAAKDGMDQHGFGMASVRFICGTQDSHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILG 124
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 125 KEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEEL--------EQQLIAAKEAGARHTLIVTDGVFSMDGVVANLPAI 196
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvrAQDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 197 CDLADKYGALVMVDDSHAVGFMGENGAGT--HEFHNVVDRIDIITGTLGKAMGGAsGGYTSGKKEVIDWLRQRSRPYLFS 274
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSleHAGLKPMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 275 NSVAPAIVSASIRVL-------DLLAESGDLRTQLWE---NSAH-FRTRMEEAGFTMGGADHAIIPIMLGDAKVAA---- 339
Cdd:PLN03227 240 ASAPPFLAKADATATagelagpQLLNRLHDSIANLYStltNSSHpYALKLRNRLVITSDPISPIIYLRLSDQEATRrtde 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1596947121 340 -----EFAERALEKGIYVVGFSFPVVPKGQAR----IRTQMSAAHSREQLDRAIDA 386
Cdd:PLN03227 320 tlildQIAHHSLSEGVAVVSTGGHVKKFLQLVpppcLRVVANASHTREDIDKLLTV 375
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
89-257 |
4.22e-28 |
|
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: 108.62 E-value: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 89 HKELEQKLSTFL--GKEDTILYTSCFDANAGLFETILGKEDAIISDALNHAS---IIDGVRLCKAMRFRYANNNMEELEQ 163
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 164 QLIAAKEAGARHTLIVTDGVFSMDGVVANLPAICDLADKYGALVMVDDSHAVGFMGENgagthEFHNVVDRIDIITGTLG 243
Cdd:cd01494 82 AILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAP-----GVLIPEGGADVVTFSLH 156
|
170
....*....|....
gi 1596947121 244 KAMGGASGGYTSGK 257
Cdd:cd01494 157 KNLGGEGGGVVIVK 170
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
40-309 |
6.68e-22 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 96.00 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 40 TGEEVLNFCANNYLGLANHPDLIEAAKDGMDQH-------GFGMASVRFICGTQDSHKELEQKLSTFLGKEDTILYTSCF 112
Cdd:PRK05937 2 KESLSIDFVTNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 113 DANAGLFETILGKEDAIISDALNHASIIDGVRLCKAMRFRYANNNMEELEQQLIAAKEAGARHTLIVTDGVFSMDGVVAN 192
Cdd:PRK05937 82 MANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGRIFIFVCSVYSFKGTLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 193 LPAICDLADKYGALVMVDDSHAVGFMGENGA------GTHEFHNVVdridiitGTLGKAMGGASGGYTSgKKEVIDWLRQ 266
Cdd:PRK05937 162 LEQIIALSKKYHAHLIVDEAHAMGIFGDDGKgfchslGYENFYAVL-------VTYSKALGSMGAALLS-SSEVKQDLML 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1596947121 267 RSRPYLFSNSVAP-AIVSASIrVLDLLAESGDL-RTQLWENSAHF 309
Cdd:PRK05937 234 NSPPLRYSTGLPPhLLISIQV-AYDFLSQEGELaRKQLFRLKEYF 277
|
|
| OAT_like |
cd00610 |
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ... |
193-390 |
1.71e-14 |
|
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: 74.53 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 193 LPAICDLADKYGALVMVDDShAVGF--MGENGAgtHEFHNVVdrIDIITgtLGKAMGGAS--GGYTsGKKEVIDWLrqRS 268
Cdd:cd00610 214 LKALRELCRKHGILLIADEV-QTGFgrTGKMFA--FEHFGVE--PDIVT--LGKGLGGGLplGAVL-GREEIMDAF--PA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 269 RPYLFS-----NSVAPAIVSASIRVLdllaESGDLRTQLWENSAHFRTRMEEA-------------GFtMGGADHAIIPI 330
Cdd:cd00610 284 GPGLHGgtfggNPLACAAALAVLEVL----EEEGLLENAAELGEYLRERLRELaekhplvgdvrgrGL-MIGIELVKDRA 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1596947121 331 MLG-DAKVAAEFAERALEKGIYvvgfsfpVVPKGQARIRTQMSAAHSREQLDRAIDAFVQV 390
Cdd:cd00610 359 TKPpDKELAAKIIKAALERGLL-------LRPSGGNVIRLLPPLIITEEEIDEGLDALDEA 412
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
45-389 |
1.31e-10 |
|
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: 62.36 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 45 LNFCANNYLgLANHPDLIEAAKDGMDQHGFgmasvrFICGTQDSHKELEQKLSTFLG-------KEDTILYTS-CFDANA 116
Cdd:cd00609 1 IDLSIGEPD-FPPPPEVLEALAAAALRAGL------LGYYPDPGLPELREAIAEWLGrrggvdvPPEEIVVTNgAQEALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 117 GLFETILGKEDAIISDALNHASIIDGVRLCKAmRFRY----ANNNMEELEQQLIAAKEAGARhtLIV-------TDGVFS 185
Cdd:cd00609 74 LLLRALLNPGDEVLVPDPTYPGYEAAARLAGA-EVVPvpldEEGGFLLDLELLEAAKTPKTK--LLYlnnpnnpTGAVLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 186 MDgvvaNLPAICDLADKYGALVMVDDSHavGFMGENGAGTHEFHNVVDRIDIIT-GTLGKAMGGAS--GGYTSG-KKEVI 261
Cdd:cd00609 151 EE----ELEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLDAYERVIVlRSFSKTFGLPGlrIGYLIApPEELL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596947121 262 DWLRQRSRPYLFSNSVAPAIVsasirVLDLLAESGDLRTQLWENSAHFRTRMEEAGFTMGGaDHAIIP-----IMLG--D 334
Cdd:cd00609 225 ERLKKLLPYTTSGPSTLSQAA-----AAAALDDGEEHLEELRERYRRRRDALLEALKELGP-LVVVKPsggffLWLDlpE 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1596947121 335 AKVAAEFAERALEKGIYVV-GFSFPVVPKGQARIrtqmSAAHSREQLDRAIDAFVQ 389
Cdd:cd00609 299 GDDEEFLERLLLEAGVVVRpGSAFGEGGEGFVRL----SFATPEEELEEALERLAE 350
|
|
| |
