|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
1-317 |
0e+00 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 584.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 1 MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVAT 80
Cdd:PRK09352 2 MYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 81 TSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:PRK09352 82 TTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 161 AGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDW 240
Cdd:PRK09352 162 AGAVVLGASEEPGILSTHLGSDGSYGDLLYLPGGGSRGPASPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDIDW 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129054 241 LVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF 317
Cdd:PRK09352 242 LVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALVRW 318
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
1-317 |
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: 541.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 1 MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVAT 80
Cdd:TIGR00747 1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 81 TSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:TIGR00747 81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 161 AGAAVLAASEEPG-IISTHLHADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLD 239
Cdd:TIGR00747 161 AGAVVLGESEDPGgIISTHLGADGTQGEALYLPAGGRPTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDID 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129054 240 WLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF 317
Cdd:TIGR00747 241 WFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
1-317 |
1.65e-171 |
|
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: 478.06 E-value: 1.65e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 1 MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVAT 80
Cdd:COG0332 1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 81 TSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:COG0332 81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 161 AGAAVLAASEE-PGIISTHLHADGSYGELLTLPNADRVNP-----ENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLD 234
Cdd:COG0332 161 AGAVVLEASEEgPGILGSVLGSDGSGADLLVVPAGGSRNPpspvdEGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 235 RSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSAL 314
Cdd:COG0332 241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320
|
...
gi 16129054 315 VRF 317
Cdd:COG0332 321 LRW 323
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
2-315 |
5.17e-161 |
|
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: 451.61 E-value: 5.17e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 2 YTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATT 81
Cdd:cd00830 1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 82 SATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGA 161
Cdd:cd00830 81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 162 GAAVL-AASEEPGIISTHLHADGSYGELLTLPNADRVNP-----ENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDR 235
Cdd:cd00830 161 GAVVLeATEEDPGILDSVLGSDGSGADLLTIPAGGSRSPfedaeGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 236 SQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALV 315
Cdd:cd00830 241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-316 |
6.32e-141 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 400.78 E-value: 6.32e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 1 MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVAT 80
Cdd:PRK12879 3 SYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 81 TSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:PRK12879 83 TTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 161 AGAAVLAASE-EPGIISTHLHADGSYGELLTLPNA----DRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDR 235
Cdd:PRK12879 163 AGAVVLEATEnEPGFIDYVLGTDGDGGDILYRTGLgttmDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGLTK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 236 SQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALV 315
Cdd:PRK12879 243 DDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLV 322
|
.
gi 16129054 316 R 316
Cdd:PRK12879 323 K 323
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
3-317 |
7.66e-110 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 324.00 E-value: 7.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 3 TKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTS 82
Cdd:PLN02326 48 SKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 83 ATHAFPSAaCQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAG 162
Cdd:PLN02326 128 PDDLFGSA-PQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGAG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 163 AAVLAASEEP--GIISTHLHADGSYGELL--TLPNADRVNPENSIH--------------LTMAGNEVFKVAVTELAHIV 224
Cdd:PLN02326 207 AVVLQACDDDedGLLGFDMHSDGNGHKHLhaTFKGEDDDSSGGNTNgvgdfppkkasyscIQMNGKEVFKFAVRCVPQVI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 225 DETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAF 304
Cdd:PLN02326 287 ESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAGF 366
|
330
....*....|...
gi 16129054 305 GGGFTWGSALVRF 317
Cdd:PLN02326 367 GAGLTWGSAIVRW 379
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
1-317 |
8.93e-88 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 266.04 E-value: 8.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 1 MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVAT 80
Cdd:CHL00203 1 MGVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 81 TSATHAFPSAAcQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:CHL00203 81 STPDDLFGSAS-QLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 161 AGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPE---------NSIHLTMAGNEVFKVAVTELAHIVDETLAAN 231
Cdd:CHL00203 160 AGAAIIGASYENSILGFKLCTDGKLNSHLQLMNKPVNNQSfgttklpqgQYQSISMNGKEVYKFAVFQVPAVIIKCLNAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 232 NLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWG 311
Cdd:CHL00203 240 NISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTWG 319
|
....*.
gi 16129054 312 SALVRF 317
Cdd:CHL00203 320 AIVLKW 325
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-315 |
1.98e-81 |
|
"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: 249.66 E-value: 1.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 5 IIGTGSYLPEQVRTNADLEKMVdtSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSAT 84
Cdd:cd00827 4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 85 HAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTiIIFGDGAGAA 164
Cdd:cd00827 82 DKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALE-PTLGDGAAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 165 VLAASEEP---GIISTHLHADGSYG----ELLTLPNADRVNPENSIHLTMA--GNEVFKVAVTELAHIVDETLAANNLDr 235
Cdd:cd00827 161 LVSRNPGIlaaGIVSTHSTSDPGYDfspyPVMDGGYPKPCKLAYAIRLTAEpaGRAVFEAAHKLIAKVVRKALDRAGLS- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 236 SQLDWLVPHQAN-LRIISATAKKLGMSMDNVVVT----LDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTW 310
Cdd:cd00827 240 EDIDYFVPHQPNgKKILEAVAKKLGGPPEKASQTrwilLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTA 319
|
....*
gi 16129054 311 GSALV 315
Cdd:cd00827 320 EAFVL 324
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
3-317 |
2.50e-78 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 241.93 E-value: 2.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 3 TKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTS 82
Cdd:PRK05963 4 SRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLATST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 83 ATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAvKYALVVGSDVLARTCDPTDRGTIIIFGDGAG 162
Cdd:PRK05963 84 PDHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQG-KPVLVVAANILSRRINMAERASAVLFADAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 163 AAVLAASEEP--GIISTHLHADGSYGELLTLPNADRVNPENS------IHLTMA-GNEVFKVAVTELAHIVDETLAANNL 233
Cdd:PRK05963 163 AVVLAPSAKAnsGVLGSQLISDGSHYDLIKIPAGGSARPFAPerdaseFLMTMQdGRAVFTEAVRMMSGASQNVLASAAM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 234 DRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSA 313
Cdd:PRK05963 243 TPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAV 322
|
....
gi 16129054 314 LVRF 317
Cdd:PRK05963 323 VMRV 326
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
50-315 |
8.34e-66 |
|
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: 207.30 E-value: 8.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 50 TVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSG 129
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 130 AVKYALVVGSDvlartcdptdrgtIIIFGDGAGAAVLAASEE---------PGIISTHLHADGSYGElltlpnadrvnpe 200
Cdd:cd00327 86 KADIVLAGGSE-------------EFVFGDGAAAAVVESEEHalrrgahpqAEIVSTAATFDGASMV------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 201 nsihltmagnevFKVAVTELAHIVDETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMD-----NVVVTLDRHGNT 275
Cdd:cd00327 140 ------------PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDgvrspAVSATLIMTGHP 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16129054 276 SAASVPCALDEAVRDGRIK-------PGQLVLLEAFGGGFTWGSALV 315
Cdd:cd00327 208 LGAAGLAILDELLLMLEHEfipptprEPRTVLLLGFGLGGTNAAVVL 254
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
51-315 |
1.82e-63 |
|
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: 204.02 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 51 VSTMGFEAATRAIEMAGIE----KDQIGLIVVATTSATHAF---------------------PSAACQIQSMLGIKGcPA 105
Cdd:cd00825 11 VSILGFEAAERAIADAGLSreyqKNPIVGVVVGTGGGSPRFqvfgadamravgpyvvtkamfPGASGQIATPLGIHG-PA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 106 FDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDP------------------TDRGTIIIFGDGAGAAVLA 167
Cdd:cd00825 90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCefdamgalstpekasrtfDAAADGFVFGDGAGALVVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 168 ASEE---------PGIISTHLHADGSYGELltlpnadrvnpensihltmagnevFKVAVTELAHIVDETLAANNLDRSQL 238
Cdd:cd00825 170 ELEHalargahiyAEIVGTAATIDGAGMGA------------------------FAPSAEGLARAAKEALAVAGLTVWDI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 239 DWLVPHQANLRIISATAKKLGMSMD-----NVVVTLDRHGNTSAASVPCALDEAVRDGRIK------------------- 294
Cdd:cd00825 226 DYLVAHGTGTPIGDVKELKLLRSEFgdkspAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGfippsihieeldeaglniv 305
|
330 340
....*....|....*....|....*..
gi 16129054 295 ------PGQLVLLEAFGGGFTWGSALV 315
Cdd:cd00825 306 tettprELRTALLNGFGLGGTNATLVL 332
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
2-317 |
1.13e-60 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 196.59 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 2 YTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAApNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATT 81
Cdd:PRK07204 4 YISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVD-GETSSYMGAEAAKKAVEDAKLTLDDIDCIICASG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 82 SATHAFPSAACQIQSMLGIK--GCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGD 159
Cdd:PRK07204 83 TIQQAIPCTASLIQEQLGLQhsGIPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILFGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 160 GAGAAVLAASEEPG-IISTHL--HADGSY------GELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAA 230
Cdd:PRK07204 163 GAAAVVITKGDHSSrILASHMetYSSGAHlseirgGGTMIHPREYSEERKEDFLFDMNGRAIFKLSSKYLMKFIDKLLMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 231 NNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTW 310
Cdd:PRK07204 243 AGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSI 322
|
....*..
gi 16129054 311 GSALVRF 317
Cdd:PRK07204 323 GGILLEY 329
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
228-317 |
4.68e-45 |
|
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: 148.42 E-value: 4.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 228 LAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGG 307
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 16129054 308 FTWGSALVRF 317
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
5-316 |
1.89e-40 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 145.02 E-value: 1.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 5 IIGTGSYLPEQVRTNADL------------------------EKMVDTSDEWIVTRTGIRERHI---------------- 44
Cdd:PRK07515 5 ISGTGLYTPPESISNEELvasfnayverfnaenaaaiaagevEALQPSSSEFIEKASGIKSRYVmdkegildpdrmrpri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 45 -AAPNETVST---MGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCpAFDVAAACAGFTYALS 120
Cdd:PRK07515 85 pERSNDELSIqaeMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIEGF-AFDMNVACSSATFGIQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 121 VADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPG------IISTHLHADGS------YGEL 188
Cdd:PRK07515 164 TAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATsaggfeILGTRLFTQFSnnirnnFGFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 189 ltlpnaDRVNPENS----IHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLD--WLvpHQANLRIISATAKK-LG-- 259
Cdd:PRK07515 244 ------NRADPEGIgardKLFVQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKrfWL--HQANINMNQLIGKKvLGrd 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129054 260 MSMDNVVVTLDRHGNTSAASVPCALDEAVRDgrIKPGQLVLLEAFGGGFTWGSALVR 316
Cdd:PRK07515 316 ATPEEAPVILDEYANTSSAGSIIAFHKHSDD--LAAGDLGVICSFGAGYSIGSVIVR 370
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
4-317 |
9.32e-39 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 140.10 E-value: 9.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 4 KIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTR----TGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVA 79
Cdd:PRK12880 9 KISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 80 TTSATHAFPSAACQIQSMLGIK-GCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGsDVLARTCDPTDRGTIIIFG 158
Cdd:PRK12880 89 TQSPDFFMPSTACYLHQLLNLSsKTIAFDLGQACAGYLYGLFVAHSLIQSGLGKILLICG-DTLSKFIHPKNMNLAPIFG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 159 DGAGAAVLAASEEPGIIsTHLHADGSYGELLTLPN-------ADRVNPE---------NSIHLTMAGNEVFKVAVTELAH 222
Cdd:PRK12880 168 DGVSATLIEKTDFNEAF-FELGSDGKYFDKLIIPKgamripkADIFNDDslmqteefrQLENLYMDGANIFNMALECEPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 223 IVDETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVV-VTLDRHGNTSAASVPCALDEAVRDGRIKpgqlVLL 301
Cdd:PRK12880 247 SFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPnFIMEKYANLSACSLPALLCELDTPKEFK----ASL 322
|
330
....*....|....*.
gi 16129054 302 EAFGGGFTWGSALVRF 317
Cdd:PRK12880 323 SAFGAGLSWGSAVLNF 338
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
5-316 |
5.28e-37 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 135.13 E-value: 5.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 5 IIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLiVVATTSAT 84
Cdd:PRK06840 7 IVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDV-VIYIGSEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 85 HAFP--SAACQIQSMLGIKGCPAFDVAAACAGFTYALSVA-DQYVKSGAVKYALVVGSdvlARTCDPTDRGT-----III 156
Cdd:PRK06840 86 KDYPvwSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAkDLLYSDPSIENVLLVGG---YRNSDLVDYDNprtrfMFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 157 FGDGAGAAVLAasEEPG---IISTHLHADGSYGELLTLPNADRVNP------ENSIH-LTMAGNEVFK-----VAVTELA 221
Cdd:PRK06840 163 FAAGGSAALLK--KDAGknrILGSAIITDGSFSEDVRVPAGGTKQPaspetvENRQHyLDVIDPESMKerldeVSIPNFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 222 HIVDETLAANNLDRSQLDWLVP-------HQANLRiisatakKLGMSMDNVVVtLDRHGNTSAASVPCALDEAVRDGRIK 294
Cdd:PRK06840 241 KVIREALRKSGYTPKDIDYLAIlhmkrsaHIALLE-------GLGLTEEQAIY-LDEYGHLGQLDQILSLHLALEQGKLK 312
|
330 340
....*....|....*....|..
gi 16129054 295 PGQLVLLEAFGGGFTWGSALVR 316
Cdd:PRK06840 313 DGDLVVLVSAGTGYTWAATVIR 334
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
106-183 |
1.48e-33 |
|
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: 118.00 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 106 FDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPG--IISTHLHADG 183
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEPGarILDSVLGSDG 80
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
37-307 |
8.81e-27 |
|
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: 108.34 E-value: 8.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 37 TGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGI-KGCPAFDVAAACAGF 115
Cdd:COG3425 37 LGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGTESGPDASKPIATYVHGALGLpPNCRAFELKFACYAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 116 TYALSVADQYVKSGAVKYALVVGSDVlARtcdpTDRGTiiiFGD---GAGAAVLAASEEPGIISTHLHAdGSY------- 185
Cdd:COG3425 117 TAALQAALGWVASGPNKKALVIASDI-AR----YGPGS---AGEytqGAGAVAMLVGADPRIAEIEGGS-GSYttdvmdf 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 186 ----GELLTLPNADRVNPENSIHLTMAGNEVFKVAvtelahivdetlaanNLDRSQLDWLVPHQANLRIISATAKKLGMS 261
Cdd:COG3425 188 wrpnGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKT---------------GLKPDDFDYFVFHQPFGKMPKKAAKKLGRK 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129054 262 M---------DNVVVTLD---RHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGG 307
Cdd:COG3425 253 AgreiqedfeEQVEPSLIysrRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSG 310
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
3-317 |
1.34e-25 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 104.45 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 3 TKIIGTGSYLPEQVRTNADLEKMVDTSDEW----------IVTRTGIRERHIAAPNETVST-----------------MG 55
Cdd:COG3424 2 ARILSIATAVPPHRYTQEEIAEFAAELFGLderdrrrlrrLFENSGIETRHSVLPLEWYLEppsfgernalyieealeLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 56 FEAATRAIEMAGIEKDQIGLIVVATTSATHAfPSAACQIQSMLGIK-----------GCpafdvAAACAGftyaLSVADQ 124
Cdd:COG3424 82 EEAARRALDKAGLDPEDIDHLVTVSCTGFAA-PGLDARLINRLGLRpdvrrlpvggmGC-----AAGAAG----LRRAAD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 125 YVKSGAVKYALVVGSDVlartC------DPTDRGTII---IFGDGAGAAVLAASEEPGIiSTHLHADGSYgellTLPNAD 195
Cdd:COG3424 152 FLRADPDAVVLVVCVEL----CsltfqrDDDSKDNLVanaLFGDGAAAVVVSGDPRPGP-GPRILAFRSY----LIPDTE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 196 RVnpensihltMA---GNEVFKV--------AVTE-LAHIVDETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMD 263
Cdd:COG3424 223 DV---------MGwdvGDTGFRMvlspevpdLIAEhLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPE 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129054 264 NVVVT---LDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF 317
Cdd:COG3424 294 ALAHSrevLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGFTAELVLLRW 350
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
37-307 |
3.45e-25 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 103.04 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 37 TGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGI-KGCPAFDVAAACAGF 115
Cdd:PRK09258 47 TGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGLLINTSVCRDYLEPATACRVHHNLGLpKSCANFDVSNACLGF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 116 TYALSVADQYVKSGAVKYALVVG----SDVLARTCD-----PTDRGTIIIF------GDGAGAAVLA-ASEEPG---IIS 176
Cdd:PRK09258 127 LNGMLDAANMIELGQIDYALVVSgesaREIVEATIDrllapETTREDFAQSfatltlGSGAAAAVLTrGSLHPRghrLLG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 177 THLHADGSYGElLTLPNADRVNpENSIHLTMAGnevfkvavTELAHIV-DETLAANNLDRSQLDWLVPHQANLRIISATA 255
Cdd:PRK09258 207 GVTRAATEHHE-LCQGGRDGMR-TDAVGLLKEG--------VELAVDTwEAFLAQLGWAVEQVDRVICHQVGAAHTRAIL 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16129054 256 KKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGG 307
Cdd:PRK09258 277 KALGIDPEKVFTTFPTLGNMGPASLPITLAMAAEEGFLKPGDRVALLGIGSG 328
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
10-309 |
5.25e-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: 103.07 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 10 SYLPEQVRTNADLEKMVDTSD--EWIVTRTGIRERHIAAP-----------------------NETVSTMGFEAATRAIE 64
Cdd:cd00831 19 SELVDFYRRLFSSDHLPELKEklKRLCAKTGIETRYLVLPggeetyaprpemspslderndiaLEEARELAEEAARGALD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 65 MAGIEKDQIGLIVVATTSATHAfPSAACQIQSMLGIKGcpafDVAA------ACAGFTYALSVADQYVKSGAVKYALVVG 138
Cdd:cd00831 99 EAGLRPSDIDHLVVNTSTGNPT-PSLDAMLINRLGLRP----DVKRynlggmGCSAGAIALDLAKDLLEANPGARVLVVS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 139 SDVLARTCDPTD-RGTII---IFGDGAGAAVLAASEEPGIISTHL-HADGSYGELLtlPNADRVNpenSIHLTMAGNEV- 212
Cdd:cd00831 174 TELCSLWYRGPDhRSMLVgnaLFGDGAAAVLLSNDPRDRRRERPLfELVRAASTLL--PDSEDAM---GWHLGEEGLTFv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 213 FKVAVTELAH-----IVDETLAANNLDRSQLD---WLVpHQANLRIISATAKKLGMSMDNVVV---TLDRHGNTSAASVP 281
Cdd:cd00831 249 LSRDVPRLVEknlerVLRKLLARLGIGLFKLAfdhWCV-HPGGRAVLDAVEKALGLSPEDLEAsrmVLRRYGNMSSSSVL 327
|
330 340
....*....|....*....|....*...
gi 16129054 282 CALDEAVRDGRIKPGQLVLLEAFGGGFT 309
Cdd:cd00831 328 YVLAYMEAKGRVKRGDRGLLIAFGPGFT 355
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
5-307 |
3.15e-23 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 98.05 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 5 IIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSAT 84
Cdd:PRK04262 5 IVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGSESHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 85 HAFPSAACQIQSMLGI-KGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVL-ARTCDPTDrgtiiiFGDGAG 162
Cdd:PRK04262 85 YAVKPTATIVAEALGAtPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADTAqGAPGDALE------YTAAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 163 AA--VLAASEEPGIIsthlhaDGSYGelLTLPNADRVNPENSiHLTMAGNEV------FKvavtelaHI---VDETLAAN 231
Cdd:PRK04262 159 GAafIIGKEEVIAEI------EATYS--YTTDTPDFWRREGE-PYPRHGGRFtgepayFK-------HIisaAKGLMEKL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129054 232 NLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTL--DRHGNTSAASVPCALdEAVRDgRIKPGQLVLLEAFGGG 307
Cdd:PRK04262 223 GLKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLltPYIGNTYSGSALLGL-AAVLD-VAKPGDRILVVSFGSG 298
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
5-301 |
3.53e-17 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 81.11 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 5 IIGTGSYLPEQVRTNADLEK---MVD----TSDEWIVTRTGIRERHIA-----APNETVSTMGFEAATRAIEMAGIEKDQ 72
Cdd:PRK06816 5 ITSTGAFLPGEPVSNDEMEAylgLINgkpsRARRIILRNNGIKTRHYAldpegRPTHSNAQMAAEAIRDLLDDAGFSLGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 73 IGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVL-----ARTCD 147
Cdd:PRK06816 85 IELLACGTSQPDQLMPGHASMVHGELGAPPIEVVSSAGVCAAGMMALKYAYLSVKAGESRNAVATASELAsrwfrASRFE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 148 P-------TDRGTIIIF---------GDGAGAAVLAASEEPGIIS-----THL-----------------HADGSYGELL 189
Cdd:PRK06816 165 AeeeklaeLEENPEIAFekdflrwmlSDGAGAVLLENKPRPDGLSlridwIDLrsyagelpvcmyagaekNEDGSLKGWS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 190 TLPNADRVNpensihltmAG-----------NEVFKVAVTE-LAHIVDEtlaaNNLDRSQLDWLVPHQANLRIISATAKK 257
Cdd:PRK06816 245 DYPPEEAEA---------ASalslkqdvrllNENIVVYTIKpLLELVDK----RNLDPDDIDYFLPHYSSEYFREKIVEL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 16129054 258 L-----GMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLL 301
Cdd:PRK06816 312 LakagfMIPEEKWFTNLATVGNTGSASIYIMLDELLNSGRLKPGQKILC 360
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
54-178 |
2.93e-11 |
|
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: 63.44 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 54 MGFEAATRAIEMAGIEKDQIGLIVVATTSA--THAFPSAacQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAV 131
Cdd:cd00829 19 LAAEAARAALDDAGLEPADIDAVVVGNAAGgrFQSFPGA--LIAEYLGLLGKPATRVEAAGASGSAAVRAAAAAIASGLA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 16129054 132 KYALVVGSDVlartcdPTDRGTIIIFGDGAGAAVLAASEEPGIISTH 178
Cdd:cd00829 97 DVVLVVGAEK------MSDVPTGDEAGGRASDLEWEGPEPPGGLTPP 137
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
18-311 |
6.30e-08 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 53.50 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 18 TNADLEKMVDTSDEWIVTRTGIRERHIAAPNET-------------------------VSTMGFEAATRAIEMAGIEKDQ 72
Cdd:PLN03168 43 TNCGEKEALKAKFKRICDKSGIRKRHMFLTEEVlkanpgictymepslnvrhdivvvqVPKLAAEAAQKAIKEWGGRKSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 73 IGLIVVATTSATHaFPSAACQIQSMLGIKgcPAFDVA----AACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDP 148
Cdd:PLN03168 123 ITHIVFATTSGVN-MPGADHALAKLLGLK--PTVKRVmmyqTGCFGGASVLRVAKDLAENNKGARVLAVASEVTAVTYRA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 149 TDRGTI------IIFGDGAGAAVLAASEEPGiISTHLHADGSYGELLtLPNADrvnpeNSI--HLTMAG------NEVFK 214
Cdd:PLN03168 200 PSENHLdglvgsALFGDGAGVYVVGSDPKPE-VEKALFEVHWAGETI-LPESD-----GAIdgHLTEAGlifhlmKDVPG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 215 VAVTELAHIVDETL-AANNLDRSQLDWLVpHQANLRIISATAKKLGMSMDNVVVTLD---RHGNTSAASVPCALDEaVRD 290
Cdd:PLN03168 273 LISKNIEKFLNEARkCVGSPDWNEMFWAV-HPGGPAILDQVEAKLKLTKDKMQGSRDilsEFGNMSSASVLFVLDQ-IRQ 350
|
330 340
....*....|....*....|.
gi 16129054 291 GRIKPGQLVLLEAFGGGFTWG 311
Cdd:PLN03168 351 RSVKMGASTLGEGSEFGFFIG 371
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
50-149 |
3.52e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 44.84 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 50 TVSTMGFEAATRAIEMAGIEKDQIGLIVVATTS--ATHAFPsaACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVK 127
Cdd:PRK12578 20 SVQELAWESIKEALNDAGVSQTDIELVVVGSTAyrGIELYP--APIVAEYSGLTGKVPLRVEAMCATGLAASLTAYTAVA 97
|
90 100
....*....|....*....|..
gi 16129054 128 SGAVKYALVVGSDVLARTCDPT 149
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTEVDTST 119
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
54-166 |
6.09e-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: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 54 MGFEAATRAIEMAGIEKDQ-----IGLIVVATTSATHAF----------------P---------SAACQIQSMLGIKGc 103
Cdd:COG0304 74 YALAAAREALADAGLDLDEvdpdrTGVIIGSGIGGLDTLeeayrallekgprrvsPffvpmmmpnMAAGHVSIRFGLKG- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 104 PAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSD---------------VLA-RTCDPT--------DR-GTIIifG 158
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEaaitplglagfdalgALStRNDDPEkasrpfdkDRdGFVL--G 230
|
....*...
gi 16129054 159 DGAGAAVL 166
Cdd:COG0304 231 EGAGVLVL 238
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
51-311 |
9.56e-05 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 43.53 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 51 VSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHaFPSAACQIQSMLGIKGCPA--FDVAAACAGFTYALSVADQYVKS 128
Cdd:PLN03173 102 VPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLRSSVKrfMMYQQGCFAGGTVLRLAKDLAEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 129 GAVKYALVVGSDVLARTC-DPTDR--GTII---IFGDGAGAAVLAASEEPGI---------------------ISTHLHA 181
Cdd:PLN03173 181 NKGARVLVVCSEITAVTFrGPSDThlDSLVgqaLFGDGAAAIIIGSDPVLGVekplfelvsaaqtilpdsdgaIDGHLRE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 182 DGSYGELLT-LPNADRVNPENSIhltmagNEVFKVAVTElahivdetlaannlDRSQLDWlVPHQANLRIISATAKKLGM 260
Cdd:PLN03173 261 VGLTFHLLKdVPGLISKNVEKSL------TEAFKPLGIS--------------DWNSLFW-IAHPGGPAILDQVEAKLAL 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16129054 261 SMDNVVVT---LDRHGNTSAASVPCALDEaVRDGRIKPGqlvlLEAFGGGFTWG 311
Cdd:PLN03173 320 KPEKLRATrhvLSEYGNMSSACVLFILDE-MRKKSAEDG----LKSTGEGLEWG 368
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
54-166 |
1.16e-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: 43.30 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 54 MGFEAATRAIEMAGIEKDQ-----IGLIVVATTSATHAFP-------------------------SAACQIQSMLGIKGc 103
Cdd:cd00834 74 FALAAAEEALADAGLDPEEldperIGVVIGSGIGGLATIEeayrallekgprrvspffvpmalpnMAAGQVAIRLGLRG- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 104 PAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVL----------------ARTCDPT--------DRGTIIIfGD 159
Cdd:cd00834 153 PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALitpltlagfaalralsTRNDDPEkasrpfdkDRDGFVL-GE 231
|
....*..
gi 16129054 160 GAGAAVL 166
Cdd:cd00834 232 GAGVLVL 238
|
|
| PLN03171 |
PLN03171 |
chalcone synthase-like protein; Provisional |
49-309 |
1.26e-04 |
|
chalcone synthase-like protein; Provisional
Pssm-ID: 178715 [Multi-domain] Cd Length: 399 Bit Score: 43.45 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 49 ETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHaFPSAACQIQSMLGIK-----------GCpafdvAAACAGFTY 117
Cdd:PLN03171 106 DAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSGAH-IPGVDFRLVPLLGLRpsvrrtmlhlnGC-----FAGAAALRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 118 ALSVADQyvKSGAvkYALVVGSDVLARTCDPTDRG---TII---IFGDGAGAAVLAASEepgiisthLHADGSYGELLTL 191
Cdd:PLN03171 180 AKDLAEN--NRGA--RVLVVAAEITLLLFNGPDEGcfqTLLnqgLFGDGAAAVIVGADA--------DAAERPLFEIVSA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 192 pnADRVNPENSIHLTMAGNEVFKVAVTELAHIvdETLAANNLDRSQLDWLVP-----------------HQANLRIISAT 254
Cdd:PLN03171 248 --AQAIIPESDDAINMHFTEGGLDGNIGTRQV--PGLIGDNIERCLLDAFAPllggdggaewndlfwavHPGSSAILDQV 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129054 255 AKKLGMSMDNVVVT---LDRHGNTSAASVPCALDEAVRdgRIKPG-------QLVLLEAFGGGFT 309
Cdd:PLN03171 324 DAALGLEPEKLAASrrvLSDYGNMFGATVIFALDELRR--QMEEAaaagawpELGVMMAFGPGLT 386
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
57-138 |
2.30e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 42.58 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 57 EAATRAIEMAGIEKDQIGLIVVATTSA----THAFPSAAcqIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVK 132
Cdd:PRK06064 28 EAGLEALEDAGIDGKDIDAMYVGNMSAglfvSQEHIAAL--IADYAGLAPIPATRVEAACASGGAALRQAYLAVASGEAD 105
|
....*.
gi 16129054 133 YALVVG 138
Cdd:PRK06064 106 VVLAAG 111
|
|
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
51-311 |
3.70e-04 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 41.96 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 51 VSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHaFPSAACQIQSMLGIKGCPA--FDVAAACAGFTYALSVADQYVKS 128
Cdd:PLN03172 102 VPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLKPSVKrfMMYQQGCFAGGTVLRLAKDLAEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 129 GAVKYALVVGSDVLARTC-DPTDR--GTII---IFGDGAGAAVLAASEEPGIisthlhaDGSYGELLTLPNADRVNPENS 202
Cdd:PLN03172 181 NAGSRVLVVCSEITAVTFrGPSDThlDSLVgqaLFGDGAAAVIIGADPDTKI-------ERPLFEIVSAAQTILPDSDGA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 203 I--HLTMAGNEVfkvavtelaHIVDET--LAANNLDRSQLDWLVP-------------HQANLRIISATAKKLGMSMDNV 265
Cdd:PLN03172 254 IdgHLREVGLTF---------HLLKDVpgLISKNIEKSLVEAFAPigindwnsifwiaHPGGPAILDQVEIKLDLKEEKL 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 16129054 266 VVT---LDRHGNTSAASVPCALDEaVRDGRIKPGQlvllEAFGGGFTWG 311
Cdd:PLN03172 325 RATrhvLSDYGNMSSACVLFILDE-MRKKSIEEGK----GSTGEGLEWG 368
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
52-166 |
7.11e-04 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 40.31 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 52 STMGFEAATRAIEMAGIEKDQIGLIVVATTSAthafpsAACQIQSMLGIKGcPAFDVAAACAGFTYALSVADQYVKSGAV 131
Cdd:pfam00109 120 SGIGDYAALLLLDEDGGPRRGSPFAVGTMPSV------IAGRISYFLGLRG-PSVTVDTACSSSLVAIHAAVQSIRSGEA 192
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 16129054 132 KYALVVGSDVLA--------------------RTCDPTDRGTiiIFGDGAGAAVL 166
Cdd:pfam00109 193 DVALAGGVNLLLtplgfagfsaagmlspdgpcKAFDPFADGF--VRGEGVGAVVL 245
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
30-140 |
7.20e-04 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 40.89 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 30 DEWIVTRTGIRERhiaapnetVSTMGFEAATRAIEMAGIEKDQI------GLIV-----------------------VAT 80
Cdd:cd00828 59 PGWDAKRTGIVDR--------TTLLALVATEEALADAGITDPYEvhpsevGVVVgsgmgglrflrrggkldaravnpYVS 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 81 TSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSD 140
Cdd:cd00828 131 PKWMLSPNTVAGWVNILLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVE 190
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
49-138 |
1.32e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 39.93 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 49 ETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSA---THAFPSA-ACQIQSMLGIKgcPAFDVAAACAGFTYALSVADQ 124
Cdd:PRK07516 20 ETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAgfsPQDFPASlVLQADPALRFK--PATRVENACATGSAAVYAALD 97
|
90
....*....|....
gi 16129054 125 YVKSGAVKYALVVG 138
Cdd:PRK07516 98 AIEAGRARIVLVVG 111
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
49-140 |
2.19e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 39.36 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 49 ETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTsATHAFPS--AACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYV 126
Cdd:PRK06059 21 RDFVEYGVVAARAALADAGLDWRDVQLVVGADT-IRNGYPGfvAGATFAQALGWNGAPVSSSYAACASGSQALQSARAQI 99
|
90
....*....|....
gi 16129054 127 KSGAVKYALVVGSD 140
Cdd:PRK06059 100 LAGLCDVALVVGAD 113
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
206-316 |
2.35e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 39.57 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 206 TMAGNEVFKVAVTelAHIVDETLAannldrsqLDWLVPHQANLRIISATAKKLGMS---MDNVVVTLDRHGNTSAASVPC 282
Cdd:PLN02192 377 TLVGKKLFKMKLK--PYIPDFKLA--------FEHFCIHAGGRAVLDELEKNLQLSdwhMEPSRMTLYRFGNTSSSSLWY 446
|
90 100 110
....*....|....*....|....*....|....
gi 16129054 283 ALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVR 316
Cdd:PLN02192 447 ELAYSEAKGRIKKGDRTWQIAFGSGFKCNSAVWK 480
|
|
| PLN02377 |
PLN02377 |
3-ketoacyl-CoA synthase |
44-314 |
3.91e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 166018 Cd Length: 502 Bit Score: 38.85 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 44 IAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVaTTSATHAFPSAACQIQSMLGIKG-CPAFDVAA-ACAGFTYALSV 121
Cdd:PLN02377 165 MAAAREEAEQVMFGALDNLFANTNVNPKDIGILVV-NCSLFNPTPSLSAMIVNKYKLRGnIRSFNLGGmGCSAGVIAVDL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 122 ADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIII----FGDGaGAAVLAASEEPG----------IISTHLHADGS--- 184
Cdd:PLN02377 244 AKDMLQVHRNTYAVVVSTENITQNWYFGNKKSMLIpnclFRVG-GSAVLLSNKSRDkrrskyklvhVVRTHRGADDKafr 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 185 --YGELltlPNADRVNPENSIHLTMAGNEVFKVAVTELAHIV---------DETLAANNLDRSQLDWLVP---------- 243
Cdd:PLN02377 323 cvYQEQ---DDAGKTGVSLSKDLMAIAGEALKTNITTLGPLVlpiseqllfFATLVVKKLFNKKMKPYIPdfklafdhfc 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129054 244 -HQANLRIISATAKKLGMSMDNVV---VTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSAL 314
Cdd:PLN02377 400 iHAGGRAVIDELEKNLQLLPVHVEasrMTLHRFGNTSSSSIWYELAYIEAKGRMRKGNRVWQIAFGSGFKCNSAV 474
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
51-311 |
4.34e-03 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 38.54 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 51 VSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHaFPSAACQIQSMLGIKgcPAFD----VAAACAGFTYALSVADQYV 126
Cdd:PLN03170 106 VPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKMLGLR--PSVNrlmmYQQGCFAGGTVLRVAKDLA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 127 KSGAVKYALVVGSDVLARTCDPTDRGTI------IIFGDGAGAAVLAAS-----EEP----------------GIISTHL 179
Cdd:PLN03170 183 ENNRGARVLVVCSEITAVTFRGPSESHLdsmvgqALFGDGAAAVIVGADpdervERPlfqlvsasqtilpdseGAIDGHL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 180 HADGSYGELLT-LPNADRVNPENSIhltmagNEVFK-VAVTelahivdetlaannlDRSQLDWlVPHQANLRIISATAKK 257
Cdd:PLN03170 263 REVGLTFHLLKdVPGLISKNIERSL------EEAFKpLGIT---------------DYNSIFW-VAHPGGPAILDQVEAK 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129054 258 LGMSMDNVVVT---LDRHGNTSAASVPCALDEaVRDGRIKPGQLVLleafGGGFTWG 311
Cdd:PLN03170 321 VGLEKERMRATrhvLSEYGNMSSACVLFILDE-MRKRSAEDGQATT----GEGFDWG 372
|
|
| PRK12404 |
PRK12404 |
stage V sporulation protein AD; Provisional |
57-171 |
4.50e-03 |
|
stage V sporulation protein AD; Provisional
Pssm-ID: 183504 Cd Length: 334 Bit Score: 38.44 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 57 EAATRAIEMAGIEKDQIGLIVVA------TTSathafpSAACqiqSMLGIkgcPAFDVAAACAGFTYALSVADQYVKSGA 130
Cdd:PRK12404 60 EACSRAIEKAKLRKEDIQFFLAGdlmnqiTPT------SFAA---RTLGI---PYLGLFGACSTSMEGLALAALIVNSGG 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129054 131 VKYalvvgsdVLARTCD-----------PTDRG---------TIIifgdGAGAAVLAASEE 171
Cdd:PRK12404 128 AKY-------VLTGASShnaavekqfryPTEYGgqkpptaqwTVT----GAGAAILSKTGD 177
|
|
| HMG_CoA_synt_N |
pfam01154 |
Hydroxymethylglutaryl-coenzyme A synthase N terminal; |
5-141 |
7.38e-03 |
|
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
Pssm-ID: 307348 [Multi-domain] Cd Length: 173 Bit Score: 36.83 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129054 5 IIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSAT 84
Cdd:pfam01154 6 ILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMERYNLPWDKIGRLEVGTETII 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129054 85 HAFPSAACQIQSMLGIKG---CPAFDVAAACAGFTYALSVADQYVKSGAV--KYALVVGSDV 141
Cdd:pfam01154 86 DKSKSVKSVLMQLFQESGntdIEGIDTTNACYGGTAALFNAANWIESSSWdgRYALVVCGDI 147
|
|
|