|
Name |
Accession |
Description |
Interval |
E-value |
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
3-328 |
0e+00 |
|
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273249 [Multi-domain] Cd Length: 318 Bit Score: 523.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 3 FYASLKSIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVAT 82
Cdd:TIGR00747 1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 83 LSPDFlAMPSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCILFGD 162
Cdd:TIGR00747 81 TTPDH-AFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 163 GAGACVIGRTKCLKEsVLDVQISANGNFSNYLYTPRTLKPTPFNakeealEPFLCMKGNEVFKLAVKTLLKDVEMILEKN 242
Cdd:TIGR00747 160 GAGAVVLGESEDPGG-IISTHLGADGTQGEALYLPAGGRPTSGP------SPFITMEGNEVFKHAVRKMGDVVEETLEAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 243 ALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWG 322
Cdd:TIGR00747 233 GLDPEDIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWG 312
|
....*.
gi 446319982 323 SALVYF 328
Cdd:TIGR00747 313 AALVRF 318
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
4-329 |
1.16e-176 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 491.51 E-value: 1.16e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 4 YASLKSIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATL 83
Cdd:PRK09352 3 YAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVATT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 84 SPDFLaMPSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCILFGDG 163
Cdd:PRK09352 83 TPDYA-FPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 164 AGACVIGRTKclKESVLDVQISANGNFSNYLYTPRTLKPTPfnakeeALEPFLCMKGNEVFKLAVKTLLKDVEMILEKNA 243
Cdd:PRK09352 162 AGAVVLGASE--EPGILSTHLGSDGSYGDLLYLPGGGSRGP------ASPGYLRMEGREVFKFAVRELAKVAREALEAAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 244 LKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWGS 323
Cdd:PRK09352 234 LTPEDIDWLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGA 313
|
....*.
gi 446319982 324 ALVYFG 329
Cdd:PRK09352 314 ALVRWP 319
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
4-326 |
2.83e-158 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 445.06 E-value: 2.83e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 4 YASLKSIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATL 83
Cdd:cd00830 1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 84 SPDFLaMPSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCILFGDG 163
Cdd:cd00830 81 TPDYL-FPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 164 AGACVIGRTKClKESVLDVQISANGNFSNYLYTPRTLKPTPFNAKEEAlEPFLCMKGNEVFKLAVKTLLKDVEMILEKNA 243
Cdd:cd00830 160 AGAVVLEATEE-DPGILDSVLGSDGSGADLLTIPAGGSRSPFEDAEGG-DPYLVMDGREVFKFAVRLMPESIEEALEKAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 244 LKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWGS 323
Cdd:cd00830 238 LTPDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGA 317
|
...
gi 446319982 324 ALV 326
Cdd:cd00830 318 ALL 320
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
4-326 |
6.66e-157 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 441.86 E-value: 6.66e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 4 YASLKSIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATL 83
Cdd:COG0332 2 NVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVATV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 84 SPDFLaMPSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCILFGDG 163
Cdd:COG0332 82 TPDYL-FPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 164 AGACVIGRTKClKESVLDVQISANGNFSNYLYTPRTLKPTPFNAKEEAlEPFLCMKGNEVFKLAVKTLLKDVEMILEKNA 243
Cdd:COG0332 161 AGAVVLEASEE-GPGILGSVLGSDGSGADLLVVPAGGSRNPPSPVDEG-DHYLRMDGREVFKFAVRNLPEVIREALEKAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 244 LKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWGS 323
Cdd:COG0332 239 LTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGA 318
|
...
gi 446319982 324 ALV 326
Cdd:COG0332 319 AVL 321
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-326 |
6.79e-137 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 391.15 E-value: 6.79e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 1 MEFYASLKSIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVV 80
Cdd:PRK12879 1 MMSYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 81 ATLSPDFLaMPSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCILF 160
Cdd:PRK12879 81 ATTTPDYL-FPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 161 GDGAGACVIGRTKcLKESVLDVQISANGNFSNYLYTPrtlKP-TPFNAKEEALEPFLCMKGNEVFKLAVKTLLKDVEMIL 239
Cdd:PRK12879 160 GDGAGAVVLEATE-NEPGFIDYVLGTDGDGGDILYRT---GLgTTMDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 240 EKNALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGL 319
Cdd:PRK12879 236 EKAGLTKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGL 315
|
....*..
gi 446319982 320 TWGSALV 326
Cdd:PRK12879 316 TWAALLV 322
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
5-326 |
1.43e-95 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 288.17 E-value: 1.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 5 ASLKSIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATLS 84
Cdd:PLN02326 48 SKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 85 PDFLAmpSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCILFGDGA 164
Cdd:PLN02326 128 PDDLF--GSAPQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 165 GACVIGRTKCLKESVL--DVQISANGN------FSNYLYTPRTLKPTPFNAKEEALEPFLC--MKGNEVFKLAVKTLLKD 234
Cdd:PLN02326 206 GAVVLQACDDDEDGLLgfDMHSDGNGHkhlhatFKGEDDDSSGGNTNGVGDFPPKKASYSCiqMNGKEVFKFAVRCVPQV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 235 VEMILEKNALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDA 314
Cdd:PLN02326 286 IESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAG 365
|
330
....*....|..
gi 446319982 315 FGGGLTWGSALV 326
Cdd:PLN02326 366 FGAGLTWGSAIV 377
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
9-326 |
6.92e-84 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 256.41 E-value: 6.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 9 SIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATLSPDFL 88
Cdd:CHL00203 7 STGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILATSTPDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 89 AmpSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCILFGDGAGACV 168
Cdd:CHL00203 87 F--GSASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDGAGAAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 169 IGrtKCLKESVLDVQISANGNFSNYLYTprTLKPTPfNAKEEALEPF------LCMKGNEVFKLAVKTLLKDVEMILEKN 242
Cdd:CHL00203 165 IG--ASYENSILGFKLCTDGKLNSHLQL--MNKPVN-NQSFGTTKLPqgqyqsISMNGKEVYKFAVFQVPAVIIKCLNAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 243 ALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWG 322
Cdd:CHL00203 240 NISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTWG 319
|
....
gi 446319982 323 SALV 326
Cdd:CHL00203 320 AIVL 323
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
13-326 |
2.37e-78 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 242.32 E-value: 2.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 13 HVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATLSPDFLaMPS 92
Cdd:PRK05963 12 AVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLATSTPDHL-LPP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 93 TACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESgMYENVLIVGAEKTSSVLDFKDRGTCILFGDGAGACVIGRT 172
Cdd:PRK05963 91 SAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRA-QGKPVLVVAANILSRRINMAERASAVLFADAAGAVVLAPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 173 KCLKESVLDVQISANGNFSNYLYTPRTLKPTPFNAKEEALEPFLCMK-GNEVFKLAVKTLLKDVEMILEKNALKPEDVRL 251
Cdd:PRK05963 170 AKANSGVLGSQLISDGSHYDLIKIPAGGSARPFAPERDASEFLMTMQdGRAVFTEAVRMMSGASQNVLASAAMTPQDIDR 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446319982 252 FIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWGSALV 326
Cdd:PRK05963 250 FFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAVVM 324
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
1-326 |
4.60e-66 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 210.85 E-value: 4.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 1 MEFYASLKSIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDkEKSSDLGVIAAKQAIERAHLTPKDIDLVVV 80
Cdd:PRK07204 1 MKRYISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVDG-ETSSYMGAEAAKKAVEDAKLTLDDIDCIIC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 81 ATLSPDfLAMPSTACVLSAKLGIENK--PAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCI 158
Cdd:PRK07204 80 ASGTIQ-QAIPCTASLIQEQLGLQHSgiPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 159 LFGDGAGACVIGRT-----------KCLKESVLDVQISANGnfsnylytprTLKPtPFNAKEEALEPFLC-MKGNEVFKL 226
Cdd:PRK07204 159 LFGDGAAAVVITKGdhssrilashmETYSSGAHLSEIRGGG----------TMIH-PREYSEERKEDFLFdMNGRAIFKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 227 AVKTLLKDVEMILEKNALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKK 306
Cdd:PRK07204 228 SSKYLMKFIDKLLMDAGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQR 307
|
330 340
....*....|....*....|
gi 446319982 307 GDLMLLDAFGGGLTWGSALV 326
Cdd:PRK07204 308 GNKILLLGTSAGLSIGGILL 327
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
7-326 |
2.33e-54 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 180.32 E-value: 2.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 7 LKSIAMHVPSERVKNAEFQQFLdtSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATLSPD 86
Cdd:cd00827 4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 87 FlAMPSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCIlFGDGAGA 166
Cdd:cd00827 82 D-KGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALEPT-LGDGAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 167 CVIGRTKCLKES-VLDVQISANGNFSNYLYTPRTLKPTPFNAKEEALEPFLCMKGNEVFKLAVKTLLKDVEMILEKNALK 245
Cdd:cd00827 160 MLVSRNPGILAAgIVSTHSTSDPGYDFSPYPVMDGGYPKPCKLAYAIRLTAEPAGRAVFEAAHKLIAKVVRKALDRAGLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 246 pEDVRLFIPHQAN-FRIIQAVREHLDFKDEQVVLTVHKY----GNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLT 320
Cdd:cd00827 240 -EDIDYFVPHQPNgKKILEAVAKKLGGPPEKASQTRWILlrrvGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFT 318
|
....*.
gi 446319982 321 WGSALV 326
Cdd:cd00827 319 AEAFVL 324
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
239-328 |
7.04e-46 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 150.73 E-value: 7.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 239 LEKNALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGG 318
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 446319982 319 LTWGSALVYF 328
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
5-328 |
1.35e-42 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 150.50 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 5 ASLKSIAMHVPSERVKNAEFQQFLDTSDEWIEKR----TGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVV 80
Cdd:PRK12880 8 AKISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 81 ATLSPDFLaMPSTACVLSAKLGIENKP-AFDISAACTGFIYLLSVAKAYVESGMYENVLIVGaEKTSSVLDFKDRGTCIL 159
Cdd:PRK12880 88 VTQSPDFF-MPSTACYLHQLLNLSSKTiAFDLGQACAGYLYGLFVAHSLIQSGLGKILLICG-DTLSKFIHPKNMNLAPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 160 FGDGAGACVIGRTKcLKESVLdvQISANGNFSNYLYTP----RTLKPTPFNAKE-EALEPF-----LCMKGNEVFKLAVK 229
Cdd:PRK12880 166 FGDGVSATLIEKTD-FNEAFF--ELGSDGKYFDKLIIPkgamRIPKADIFNDDSlMQTEEFrqlenLYMDGANIFNMALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 230 TLLKDVEMILEKNALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVV-LTVHKYGNTSAASIPMAMCEAYEEGRLKKgd 308
Cdd:PRK12880 243 CEPKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPnFIMEKYANLSACSLPALLCELDTPKEFKA-- 320
|
330 340
....*....|....*....|
gi 446319982 309 lmLLDAFGGGLTWGSALVYF 328
Cdd:PRK12880 321 --SLSAFGAGLSWGSAVLNF 338
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
31-326 |
5.86e-35 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 130.77 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 31 SDEWIEKRTGIKeRRFANDK--------------EKSSD-------LGVIAAKQAIERAHLTPKDIDLVVVATlSPDFLA 89
Cdd:PRK07515 53 SSEFIEKASGIK-SRYVMDKegildpdrmrpripERSNDelsiqaeMGVAAARQALARAGRTAEDIDAVIVAC-SNMQRA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 90 MPSTACVLSAKLGIENKpAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCILFGDGAGACVI 169
Cdd:PRK07515 131 YPAMAIEIQQALGIEGF-AFDMNVACSSATFGIQTAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 170 GRT-KCLKESVLDV-------QISANGNfSNYLYTPRTLKPTPFNAkeealEPFLCMKGNEVFKlavktllkDV-----E 236
Cdd:PRK07515 210 ERAdTATSAGGFEIlgtrlftQFSNNIR-NNFGFLNRADPEGIGAR-----DKLFVQEGRKVFK--------EVcpmvaE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 237 MI---LEKNALKPEDVRLFIPHQANFRIIQAVREHL---DFKDEQVVLTVHKYGNTSAASIPMAMCEAYEEgrLKKGDLM 310
Cdd:PRK07515 276 HIvehLAENGLTPADVKRFWLHQANINMNQLIGKKVlgrDATPEEAPVILDEYANTSSAGSIIAFHKHSDD--LAAGDLG 353
|
330
....*....|....*.
gi 446319982 311 LLDAFGGGLTWGSALV 326
Cdd:PRK07515 354 VICSFGAGYSIGSVIV 369
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
109-188 |
8.25e-35 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 121.85 E-value: 8.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 109 FDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLDFKDRGTCILFGDGAGACVIGRTKCLKESVLDVQISANG 188
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEPGARILDSVLGSDG 80
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
5-319 |
5.16e-29 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 113.82 E-value: 5.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 5 ASLKSIAMHVPSERVKNAEFQQFL-DTSDEW------IEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDL 77
Cdd:PRK09258 6 VAILSLAYELAPVVVTSSEIEERLaPLYERLrlppgqLEALTGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 78 VVVATLSPDFLAmPSTACVLSAKLGIENKPA-FDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVL------- 149
Cdd:PRK09258 86 LINTSVCRDYLE-PATACRVHHNLGLPKSCAnFDVSNACLGFLNGMLDAANMIELGQIDYALVVSGESAREIVeatidrl 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 150 --------DFKDRGTCILFGDGAGACVIGRTKC------LKESVldvqisangnfsnylytprTLKPTPFNAkeealepf 215
Cdd:PRK09258 165 lapettreDFAQSFATLTLGSGAAAAVLTRGSLhprghrLLGGV-------------------TRAATEHHE-------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 216 LCMKGNEVFKLAVKTLLKD-VEMI-------LEKNALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHKYGNTS 287
Cdd:PRK09258 218 LCQGGRDGMRTDAVGLLKEgVELAvdtweafLAQLGWAVEQVDRVICHQVGAAHTRAILKALGIDPEKVFTTFPTLGNMG 297
|
330 340 350
....*....|....*....|....*....|..
gi 446319982 288 AASIPMAMCEAYEEGRLKKGDLMLLDAFGGGL 319
Cdd:PRK09258 298 PASLPITLAMAAEEGFLKPGDRVALLGIGSGL 329
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
56-326 |
1.28e-28 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 112.73 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 56 LGVIAAKQAIERAHLTPKD----IDLVVVATLSPDFLA--------------------MPSTACVLSAKLGIeNKPAFDI 111
Cdd:cd00825 14 LGFEAAERAIADAGLSREYqknpIVGVVVGTGGGSPRFqvfgadamravgpyvvtkamFPGASGQIATPLGI-HGPAYDV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 112 SAACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVLD------------------FKDRGTCILFGDGAGACVIGRTK 173
Cdd:cd00825 93 SAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDcefdamgalstpekasrtFDAAADGFVFGDGAGALVVEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 174 CLKESVLDVQISANGnfsnylyTPRTLKPTpfnakeealepflcmkGNEVFKLAVKTLLKDVEMILEKNALKPEDVRLFI 253
Cdd:cd00825 173 HALARGAHIYAEIVG-------TAATIDGA----------------GMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 254 PHQANFRIIQAVREHL---DFKDEQVVLTVHK--YGNTSAASIPMAMCEA-------------------------YEEGR 303
Cdd:cd00825 230 AHGTGTPIGDVKELKLlrsEFGDKSPAVSATKamTGNLSSAAVVLAVDEAvlmlehgfippsihieeldeaglniVTETT 309
|
330 340
....*....|....*....|...
gi 446319982 304 LKKGDLMLLDAFGGGLTWGSALV 326
Cdd:cd00825 310 PRELRTALLNGFGLGGTNATLVL 332
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
1-330 |
3.85e-28 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 111.64 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 1 MEFYASLKSIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVV- 79
Cdd:PRK06840 1 MEMNVGIVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVIy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 80 ---------VATLSPDflampstacvLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVES-GMYENVLIVGAEKTSSVL 149
Cdd:PRK06840 81 igsehkdypVWSSAPK----------IQHEIGAKNAWAFDIMAVCASFPIALKVAKDLLYSdPSIENVLLVGGYRNSDLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 150 DFKDRGTCILF--GDGAGACVIGRTKClKESVLDVQISANGNFSNYLYTPR--TLKPtPFNAKEEALEPFLCMKGNEVFK 225
Cdd:PRK06840 151 DYDNPRTRFMFnfAAGGSAALLKKDAG-KNRILGSAIITDGSFSEDVRVPAggTKQP-ASPETVENRQHYLDVIDPESMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 226 --LAVKTLLKDVEMI---LEKNALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVVLTVHkYGNTSAASIPMAMCEAYE 300
Cdd:PRK06840 229 erLDEVSIPNFLKVIreaLRKSGYTPKDIDYLAILHMKRSAHIALLEGLGLTEEQAIYLDE-YGHLGQLDQILSLHLALE 307
|
330 340 350
....*....|....*....|....*....|
gi 446319982 301 EGRLKKGDLMLLDAFGGGLTWGSALVYFGG 330
Cdd:PRK06840 308 QGKLKDGDLVVLVSAGTGYTWAATVIRWGP 337
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
54-326 |
8.39e-26 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 103.29 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 54 SDLGVIAAKQAIERAHLTPKDIDLVVVATLSPDFlAMPSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGM 133
Cdd:cd00327 8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSG-EFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 134 YENVLIVGAEKtssvldfkdrgtcILFGDGAGACVIGRTKCLKESVLDVQISANGnfsnylyTPRTLKPTpfnakeeale 213
Cdd:cd00327 87 ADIVLAGGSEE-------------FVFGDGAAAAVVESEEHALRRGAHPQAEIVS-------TAATFDGA---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 214 pflcmkgNEVFKLAVKTLLKDVEMILEKNALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQ-----VVLTVHKYGNTSA 288
Cdd:cd00327 137 -------SMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGvrspaVSATLIMTGHPLG 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446319982 289 ASIPMAMCEAYEEGRLKKG-------DLMLLDAFGGGLTWGSALV 326
Cdd:cd00327 210 AAGLAILDELLLMLEHEFIpptprepRTVLLLGFGLGGTNAAVVL 254
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
5-320 |
2.30e-25 |
|
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.
Pssm-ID: 238427 [Multi-domain] Cd Length: 361 Bit Score: 104.23 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 5 ASLKSIAMHVPSERVKNAEFQQF--LDTSDE----------WIEKRTGIKERRFA---------------------ND-- 49
Cdd:cd00831 2 ATILAIGTAVPPHRVPQSELVDFyrRLFSSDhlpelkeklkRLCAKTGIETRYLVlpggeetyaprpemspslderNDia 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 50 KEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATLSpdFLAMPSTACVLSAKLGI-ENKPAFDI-----SAACTGfiylLS 123
Cdd:cd00831 82 LEEARELAEEAARGALDEAGLRPSDIDHLVVNTST--GNPTPSLDAMLINRLGLrPDVKRYNLggmgcSAGAIA----LD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 124 VAKAYVESGMYENVLIVGAEKTSSVLDFKDR-----GTCiLFGDGAGACVIG--------RTKCLK------------ES 178
Cdd:cd00831 156 LAKDLLEANPGARVLVVSTELCSLWYRGPDHrsmlvGNA-LFGDGAAAVLLSndprdrrrERPLFElvraastllpdsED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 179 VLDVQISANGnfsnylYTPRTLKPTPFNAkEEALEPFlcmkgnevfklaVKTLLKDVEMILEKnalkpEDVRLFIPHQAN 258
Cdd:cd00831 235 AMGWHLGEEG------LTFVLSRDVPRLV-EKNLERV------------LRKLLARLGIGLFK-----LAFDHWCVHPGG 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446319982 259 FRIIQAVREHLDFKDEQVVL---TVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLT 320
Cdd:cd00831 291 RAVLDAVEKALGLSPEDLEAsrmVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFT 355
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
13-318 |
1.34e-21 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 93.82 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 13 HVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATLSPDFlAMPS 92
Cdd:PRK04262 11 YIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGSESHPY-AVKP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 93 TACVLSAKLGIENK-PAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAEkTSS-----VLDFKDrgtcilfGDGAGA 166
Cdd:PRK04262 90 TATIVAEALGATPDlTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGAD-TAQgapgdALEYTA-------AAGGAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 167 CVIGRTKCLKEsvldvqisANGNFSNYLYTP----RTLKPTPFNAKEEALEP--FlcmkgnevfklavKTLLKDVEMILE 240
Cdd:PRK04262 162 FIIGKEEVIAE--------IEATYSYTTDTPdfwrREGEPYPRHGGRFTGEPayF-------------KHIISAAKGLME 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 241 KNALKPEDVRLFIPHQANFRIIQAVREHLDFKDEQVV--LTVHKYGNTSAASIPMAMCEAYEEGrlKKGDLMLLDAFGGG 318
Cdd:PRK04262 221 KLGLKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKpgLLTPYIGNTYSGSALLGLAAVLDVA--KPGDRILVVSFGSG 298
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
5-320 |
7.09e-21 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 91.74 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 5 ASLKSIAMHVPSERVKNAE----FQQFLDTSDEWIEK------RTGIKERRFA---------------ND--KEKSSDLG 57
Cdd:COG3424 2 ARILSIATAVPPHRYTQEEiaefAAELFGLDERDRRRlrrlfeNSGIETRHSVlplewyleppsfgerNAlyIEEALELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 58 VIAAKQAIERAHLTPKDIDLVVVATLSPdfLAMPSTACVLSAKLGIENkpafDIS----------AACTGfiylLSVAKA 127
Cdd:COG3424 82 EEAARRALDKAGLDPEDIDHLVTVSCTG--FAAPGLDARLINRLGLRP----DVRrlpvggmgcaAGAAG----LRRAAD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 128 YVESGMYENVLIVGAEKTSSVLDFKDR------GTCiLFGDGAGACVIG--------------RTKCLKESvLDV---QI 184
Cdd:COG3424 152 FLRADPDAVVLVVCVELCSLTFQRDDDskdnlvANA-LFGDGAAAVVVSgdprpgpgprilafRSYLIPDT-EDVmgwDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 185 SANGnFSNYL--YTPRTLkptpfnakEEALEPflcmkgnevfklavktllkDVEMILEKNALKPEDVRLFIPHQANFRII 262
Cdd:COG3424 230 GDTG-FRMVLspEVPDLI--------AEHLAP-------------------AVEPLLARHGLTIEDIDHWAVHPGGPKVL 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446319982 263 QAVREHLDFKDEQVVLTVH---KYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLT 320
Cdd:COG3424 282 DAVEEALGLPPEALAHSREvlrEYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGFT 342
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
9-318 |
2.22e-17 |
|
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 442651 [Multi-domain] Cd Length: 382 Bit Score: 81.76 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 9 SIAMHVPSERVKNAEFQQFLDTSDEWIEKRTGIKERRFANDKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVATLS-PDF 87
Cdd:COG3425 7 AIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGTESgPDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 88 lAMPSTACVLSAkLGI-ENKPAFDISAACTGFIYLLSVAKAYVESGMYENVLIVGAE----KTSSVLDFkdrgTcilFGD 162
Cdd:COG3425 87 -SKPIATYVHGA-LGLpPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDiaryGPGSAGEY----T---QGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 163 GAGACVIGRtkclKESVLDVqisaNGNFSNYLY-TPRTLKPTPfnakeealEPFLCMKG---NEVFKLAVKTLLKDVemi 238
Cdd:COG3425 158 GAVAMLVGA----DPRIAEI----EGGSGSYTTdVMDFWRPNG--------SDYPLVDGrfsEPAYLDHLEEAVKDY--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 239 LEKNALKPEDVRLFIPHQAN-------FR--IIQAVREHLDFKDEQVV--LTVHKY-GNTSAASIPMAMCEAYEEGRLKK 306
Cdd:COG3425 219 KEKTGLKPDDFDYFVFHQPFgkmpkkaAKklGRKAGREIQEDFEEQVEpsLIYSRRiGNTYTGSLYLGLASLLDNAKDLP 298
|
330
....*....|..
gi 446319982 307 GDLMLLDAFGGG 318
Cdd:COG3425 299 GDRIGLFSYGSG 310
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
40-148 |
1.22e-15 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 76.92 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 40 GIKERRFANDKEKSS-DLGVIAAKQAIERAHLTPKDIDLVVVATLSPDFLAMPSTACVLSAkLGIENKPAFDISAACTGF 118
Cdd:cd00829 2 GVGMTPFGRRSDRSPlELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEY-LGLLGKPATRVEAAGASG 80
|
90 100 110
....*....|....*....|....*....|
gi 446319982 119 IYLLSVAKAYVESGMYENVLIVGAEKTSSV 148
Cdd:cd00829 81 SAAVRAAAAAIASGLADVVLVVGAEKMSDV 110
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
9-312 |
1.18e-11 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 64.93 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 9 SIAMHVPSERVKNAEFQQFL-------DTSDEWIEKRTGIKERRFANDKE-----KSSDLGVIAAKQAIERAHLTPKDID 76
Cdd:PRK06816 7 STGAFLPGEPVSNDEMEAYLglingkpSRARRIILRNNGIKTRHYALDPEgrpthSNAQMAAEAIRDLLDDAGFSLGDIE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 77 LVVVATLSPDFLaMPSTACVLSAKLGIenkPAFDISAA---CTGFIYLLSVAKAYVESGMYENVLIVGAEKTSSVL---- 149
Cdd:PRK06816 87 LLACGTSQPDQL-MPGHASMVHGELGA---PPIEVVSSagvCAAGMMALKYAYLSVKAGESRNAVATASELASRWFrasr 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 150 --------DFKDRGTCILF---------GDGAGAcVIGRTK------CLKESVLDVQ---------------ISANGNFS 191
Cdd:PRK06816 163 feaeeeklAELEENPEIAFekdflrwmlSDGAGA-VLLENKprpdglSLRIDWIDLRsyagelpvcmyagaeKNEDGSLK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 192 NYL-YTPrtlkptpfnakEEAL-EPFLCMKG-----NEVFKLA-VKTLLKdvemILEKNALKPEDVRLFIPHQANFRIIQ 263
Cdd:PRK06816 242 GWSdYPP-----------EEAEaASALSLKQdvrllNENIVVYtIKPLLE----LVDKRNLDPDDIDYFLPHYSSEYFRE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446319982 264 AVREHLdfKDEQVVLTVHK-------YGNTSAASIPMAMCEAYEEGRLKKGDLMLL 312
Cdd:PRK06816 307 KIVELL--AKAGFMIPEEKwftnlatVGNTGSASIYIMLDELLNSGRLKPGQKILC 360
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
40-148 |
4.88e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 59.91 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 40 GIKERRFANDKEKS-SDLGVIAAKQAIERAHLTPKDIDLVVVATLSPD-FLAMPSTACVLSAKLGIENKPAFDISAAC-T 116
Cdd:PRK06064 8 GVGQTKFGELWDVSlRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGlFVSQEHIAALIADYAGLAPIPATRVEAACaS 87
|
90 100 110
....*....|....*....|....*....|....
gi 446319982 117 GfiyLLSVAKAY--VESGMYENVLIVGAEKTSSV 148
Cdd:PRK06064 88 G---GAALRQAYlaVASGEADVVLAAGVEKMTDV 118
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
199-325 |
1.16e-06 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 49.97 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 199 TLKPTPFNAKEEALEpFLCMKGNEVFKLAVKTLLKDVEMILEKnalkpedvrlFIPHQANFRIIQAVREHLDFKD---EQ 275
Cdd:PLN02192 360 TLGPLVLPMSEQLLF-FATLVGKKLFKMKLKPYIPDFKLAFEH----------FCIHAGGRAVLDELEKNLQLSDwhmEP 428
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446319982 276 VVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWGSAL 325
Cdd:PLN02192 429 SRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRTWQIAFGSGFKCNSAV 478
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
199-325 |
5.24e-06 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 48.03 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 199 TLKPT--PFNakeEALEPFLCMKGNEVFKLAVKTLLKDVEMILEKnalkpedvrlFIPHQANFRIIQAVREHLDFKD--- 273
Cdd:PLN02854 372 TLGPLvlPLS---EQFMFFVTLVRRKLLKAKVKPYIPDFKLAFEH----------FCIHAGGRAVLDELQKNLQLSDwhm 438
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446319982 274 EQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWGSAL 325
Cdd:PLN02854 439 EPSRMTLHRFGNTSSSSLWYELAYTEAKGRVSAGDRVWQIAFGSGFKCNSAV 490
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
55-148 |
9.30e-06 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 46.98 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 55 DLGVIAAKQAIERAHLTPKDIDLVVVATLSPDFLAM-PSTACVLSAKLGIEnKPAFDISAAC-TGFIYLLSVAKAyVESG 132
Cdd:COG0183 28 DLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQnPARQAALLAGLPES-VPAVTVNRVCgSGLQAVALAAQA-IAAG 105
|
90
....*....|....*.
gi 446319982 133 MYENVLIVGAEKTSSV 148
Cdd:COG0183 106 DADVVIAGGVESMSRA 121
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
55-145 |
1.02e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 46.68 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 55 DLGVIAAKQAIERAHLTPKDIDLVVVA-TLS---PDFLAmpstACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVE 130
Cdd:PRK06059 25 EYGVVAARAALADAGLDWRDVQLVVGAdTIRngyPGFVA----GATFAQALGWNGAPVSSSYAACASGSQALQSARAQIL 100
|
90
....*....|....*
gi 446319982 131 SGMYENVLIVGAEKT 145
Cdd:PRK06059 101 AGLCDVALVVGADTT 115
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
49-144 |
1.21e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 46.48 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 49 DKEKSSDLGVIAAKQAIERAHLTPKDIDLVVVAT----LSP-DFLAmpstACVLSAKLGIENKPAFDISAAC-TGFIYLL 122
Cdd:PRK07516 18 DAETLESLIVRVAREALAHAGIAAGDVDGIFLGHfnagFSPqDFPA----SLVLQADPALRFKPATRVENACaTGSAAVY 93
|
90 100
....*....|....*....|..
gi 446319982 123 SVAKAyVESGMYENVLIVGAEK 144
Cdd:PRK07516 94 AALDA-IEAGRARIVLVVGAEK 114
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
60-146 |
1.43e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 46.26 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 60 AAKQAIERAHLTPKDIDLVVVATlSPDF---LAMPSTacVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYVESGMYEN 136
Cdd:PRK08313 31 AIDRALADAGLTWDDIDAVVVGK-APDFfegVMMPEL--FLADALGATGKPLIRVHTAGSVGGSTAVVAASLVQSGVYRR 107
|
90
....*....|
gi 446319982 137 VLIVGAEKTS 146
Cdd:PRK08313 108 VLAVAWEKQS 117
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
55-148 |
2.24e-05 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 45.55 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 55 DLGVIAAKQAIERAHLTPKDIDLVVV-ATLSPDFLAMPSTACVLSAKLGIEnKPAFDISAAC-TGfiyLLSVAKAY--VE 130
Cdd:cd00751 24 DLGAAVIKALLERAGLDPEEVDDVIMgNVLQAGEGQNPARQAALLAGLPES-VPATTVNRVCgSG---LQAVALAAqsIA 99
|
90
....*....|....*...
gi 446319982 131 SGMYENVLIVGAEKTSSV 148
Cdd:cd00751 100 AGEADVVVAGGVESMSRA 117
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
32-169 |
6.77e-05 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 44.32 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 32 DEWIEKrtgiKERRFANdkeKSSDLGVIAAKQAIERAHLTPKDIDL----VVVAT----------------------LSP 85
Cdd:COG0304 57 EEYLDR----KELRRMD---RFTQYALAAAREALADAGLDLDEVDPdrtgVIIGSgiggldtleeayrallekgprrVSP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 86 DFL--AMPST-ACVLSAKLGIENkPAFDISAAC-TGfiyLLSVAKAY--VESGMYENVLIVGAEKTSSVLDF-------- 151
Cdd:COG0304 130 FFVpmMMPNMaAGHVSIRFGLKG-PNYTVSTACaSG---AHAIGEAYrlIRRGRADVMIAGGAEAAITPLGLagfdalga 205
|
170 180 190
....*....|....*....|....*....|....
gi 446319982 152 ----------------KDRgTCILFGDGAGACVI 169
Cdd:COG0304 206 lstrnddpekasrpfdKDR-DGFVLGEGAGVLVL 238
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
60-165 |
1.65e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 42.91 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 60 AAKQAIERAHLTPKDIDLVVV-ATLSPDFLAMPstACVLSAKLGIENKPAFDISAAC-TGfiyLLSVAKAY--VESGMYE 135
Cdd:PRK12578 28 SIKEALNDAGVSQTDIELVVVgSTAYRGIELYP--APIVAEYSGLTGKVPLRVEAMCaTG---LAASLTAYtaVASGLVD 102
|
90 100 110
....*....|....*....|....*....|
gi 446319982 136 NVLIVGAEKTSSVldfkDRGTCILFGDGAG 165
Cdd:PRK12578 103 MAIAVGVDKMTEV----DTSTSLAIGGRGG 128
|
|
| PLN02932 |
PLN02932 |
3-ketoacyl-CoA synthase |
70-325 |
2.45e-04 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 178520 Cd Length: 478 Bit Score: 42.71 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 70 LTPKDIDLVVVAtlSPDFLAMPSTACVLSAKLGI-ENKPAFDISA-ACTGFIYLLSVAKAYVESGMYENVLIVGAEKTSS 147
Cdd:PLN02932 165 ISPSDIGILVVN--SSTFNPTPSLSSILVNKFKLrDNIKSLNLGGmGCSAGVIAIDAAKSLLQVHRNTYALVVSTENITQ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 148 VLDFKDRGTCI----LFGDGAGACV-----IGRTKCLKESVLDVQISANGNfsnylytPRTLKPTPFNAKEE-----ALE 213
Cdd:PLN02932 243 NLYLGNNKSMLvtncLFRIGGAAILlsnrsRDRKRAKYELVHTVRVHTGAD-------DRSYECATQEEDEDgivgvSLS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 214 PFLCMKGNEVFKLAVKTLLKDVEMILEKNA----------LKPEdVRLFIP-----------HQANFRIIQAVREHLDFK 272
Cdd:PLN02932 316 KNLPMVAARTLKINIATLGPLVLPLSEKFHffvrfvkkkfFNPK-LKHYIPdfklafehfciHAGGRALIDEMEKNLHLT 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446319982 273 D---EQVVLTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWGSAL 325
Cdd:PLN02932 395 PldvEASRMTLHRFGNTSSSSIWYELAYTEAKGRMKKGDRIWQIALGSGFKCNSSV 450
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
56-170 |
2.47e-04 |
|
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.
Pssm-ID: 395142 Cd Length: 225 Bit Score: 41.76 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 56 LGVIAAKQAIERAHLTPKDIDLVVVATLSPdfLAMPSTACVLSAKLGIEN--KPAFDISAACTGFIYLLSVAKAYVESGM 133
Cdd:pfam00195 102 LGAEAALKAIKEWGQPKSKITHLVFCTTSG--VRMPGADYQLAKLLGLRPsvKRVMLYFQGCYGGATVLRTAKDIAENNP 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446319982 134 YENVLIVGAEKTssVLDFkdRGTC----------ILFGDGAGACVIG 170
Cdd:pfam00195 180 GARVLVVCSEIT--VLGF--RGPSkdrldslvgaALFGDGAAAVIIG 222
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
51-148 |
2.91e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 42.12 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 51 EKSSDLGVIAAKQAIERAHLTPKDIDLVVVATlSPD-FLAMPSTACVLSAKLGIENKPAFDISAACTGFIYLLSVAKAYV 129
Cdd:PRK06065 27 ETPQELAWEAASKALDEAGLELKDIDCVVIGS-APDaFDGVHMKGEYLSHGSGGIRKPVSRVYVGGATGVMTAIAGWYHV 105
|
90
....*....|....*....
gi 446319982 130 ESGMYENVLIVGAEKTSSV 148
Cdd:PRK06065 106 ASGLCQKVLAVAEEKMSPA 124
|
|
| PRK08304 |
PRK08304 |
stage V sporulation protein AD; Validated |
60-147 |
3.41e-04 |
|
stage V sporulation protein AD; Validated
Pssm-ID: 236230 Cd Length: 337 Bit Score: 41.75 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 60 AAKQAIERAHLTPKDIDLVvvatLSPDFLAMPSTACVLSAKLGIenkPAFDISAACTGFIYLLSVAKAYVESGMYENVLI 139
Cdd:PRK08304 63 AIQQALQKANLKKSDIDYL----LAGDLLNQIISANFAARELGI---PFLGLYGACSTMMESLALGSMLIDGGFADRVLA 135
|
....*...
gi 446319982 140 VgaekTSS 147
Cdd:PRK08304 136 A----TSS 139
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
55-139 |
4.65e-04 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 41.55 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 55 DLGVIAAKQAIERAHLTPKDIDLVVVATLSPDFLAMPstacvLSAKLGIenKPAFdISAACTG---FIYLLSVAKAYVES 131
Cdd:PRK06158 30 ELLAQAAHRALADAGLTMADVDGLFTASPDDALWGLS-----VAEYLGI--RPRF-VDGTMIGgssFLAHLLPAALALEA 101
|
....*...
gi 446319982 132 GMYENVLI 139
Cdd:PRK06158 102 GLCDVALI 109
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
42-143 |
9.77e-04 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 40.60 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 42 KERRFANdkeKSSDLGVIAAKQAIERAHLTPKDIDL----VVVAT----------------------LSPDFL--AMPST 93
Cdd:cd00834 63 KELRRMD---RFAQFALAAAEEALADAGLDPEELDPerigVVIGSgigglatieeayrallekgprrVSPFFVpmALPNM 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446319982 94 AC-VLSAKLGIENkPAFDISAAC-TGfiyLLSVAKAY--VESGMYENVLIVGAE 143
Cdd:cd00834 140 AAgQVAIRLGLRG-PNYTVSTACaSG---AHAIGDAArlIRLGRADVVIAGGAE 189
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
55-170 |
1.34e-03 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 40.07 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 55 DLGVIAAKQAIERAHLTPKDIDLVVVATLSPdfLAMPSTACVLSAKLGIENkpafDIS------AACTGFIYLLSVAKAY 128
Cdd:PLN03169 108 QMAVEASLACIKEWGRPVSDITHLVYVSSSE--ARLPGGDLYLAKQLGLSP----DVQrvmlyfLGCSGGVAGLRVAKDI 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446319982 129 VESGMYENVLIVGAEKTssVLDFK----DR-----GTCiLFGDGAGACVIG 170
Cdd:PLN03169 182 AENNPGSRVLLTTSETT--ILGFRppspDRpydlvGAA-LFGDGAAAVIIG 229
|
|
| PLN00415 |
PLN00415 |
3-ketoacyl-CoA synthase |
210-323 |
1.41e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 177808 Cd Length: 466 Bit Score: 40.06 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 210 EALEPFLCMKGNEVFKLAVKTLLKDVEMILEKnalkpedvrlFIPHQANFRIIQAVREHL---DFKDEQVVLTVHKYGNT 286
Cdd:PLN00415 328 EKLRFILFLVKSKLFRLKVSPYVPDFKLCFKH----------FCIHAGGRALLDAVEKGLglsEFDLEPSRMTLHRFGNT 397
|
90 100 110
....*....|....*....|....*....|....*..
gi 446319982 287 SAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWGS 323
Cdd:PLN00415 398 SSSSLWYELAYVEAKCRVKRGDRVWQLAFGSGFKCNS 434
|
|
| PLN02377 |
PLN02377 |
3-ketoacyl-CoA synthase |
278-325 |
3.46e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 166018 Cd Length: 502 Bit Score: 38.85 E-value: 3.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446319982 278 LTVHKYGNTSAASIPMAMCEAYEEGRLKKGDLMLLDAFGGGLTWGSAL 325
Cdd:PLN02377 427 MTLHRFGNTSSSSIWYELAYIEAKGRMRKGNRVWQIAFGSGFKCNSAV 474
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
53-148 |
7.46e-03 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 37.28 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319982 53 SSDLGVIAAKQAIERAHLTPKDIDLVVVATLSPDFL-AMPSTACVLsaKLGIENK-PAFDISAAC-TGFIYLLSVAKAyV 129
Cdd:pfam00108 23 AVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEgQNPARQAAL--KAGIPDSaPAVTINKVCgSGLKAVYLAAQS-I 99
|
90
....*....|....*....
gi 446319982 130 ESGMYENVLIVGAEKTSSV 148
Cdd:pfam00108 100 ASGDADVVLAGGVESMSHA 118
|
|
| |
