|
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: 574.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVAT 80
Cdd:PRK09352 2 MYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 81 TSGTHAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGDG 160
Cdd:PRK09352 82 TTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 161 AGAVVLGASEEPGIISTHLHADGRYGELLTLPNADRVEPENPIYLTMAGNEVFKVAVTELAHIVDETLAANNLDRSALDW 240
Cdd:PRK09352 162 AGAVVLGASEEPGILSTHLGSDGSYGDLLYLPGGGSRGPASPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDIDW 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765315 241 LVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTWGSALVRF 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: 514.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVAT 80
Cdd:TIGR00747 1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 81 TSGTHAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGDG 160
Cdd:TIGR00747 81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 161 AGAVVLGASEEPG-IISTHLHADGRYGELLTLPNADRVEPENPIYLTMAGNEVFKVAVTELAHIVDETLAANNLDRSALD 239
Cdd:TIGR00747 161 AGAVVLGESEDPGgIISTHLGADGTQGEALYLPAGGRPTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDID 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765315 240 WLVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTWGSALVRF 317
Cdd:TIGR00747 241 WFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
1-317 |
2.17e-168 |
|
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: 470.36 E-value: 2.17e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVAT 80
Cdd:COG0332 1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 81 TSGTHAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGDG 160
Cdd:COG0332 81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 161 AGAVVLGASEE-PGIISTHLHADGRYGELLTLP-----NADRVEPENPIYLTMAGNEVFKVAVTELAHIVDETLAANNLD 234
Cdd:COG0332 161 AGAVVLEASEEgPGILGSVLGSDGSGADLLVVPaggsrNPPSPVDEGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 235 RSALDWLVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTWGSAL 314
Cdd:COG0332 241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320
|
...
gi 695765315 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 |
1.31e-156 |
|
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: 440.44 E-value: 1.31e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 2 YTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATT 81
Cdd:cd00830 1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 82 SGTHAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGDGA 161
Cdd:cd00830 81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 162 GAVVLGASEE-PGIISTHLHADGRYGELLTLP-----NADRVEPENPIYLTMAGNEVFKVAVTELAHIVDETLAANNLDR 235
Cdd:cd00830 161 GAVVLEATEEdPGILDSVLGSDGSGADLLTIPaggsrSPFEDAEGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 236 SALDWLVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTWGSALV 315
Cdd:cd00830 241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-316 |
1.34e-135 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 387.30 E-value: 1.34e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVAT 80
Cdd:PRK12879 3 SYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 81 TSGTHAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGDG 160
Cdd:PRK12879 83 TTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 161 AGAVVLGASE-EPGIISTHLHADGRYGELLTLPNA----DRVEPENPIYLTMAGNEVFKVAVTELAHIVDETLAANNLDR 235
Cdd:PRK12879 163 AGAVVLEATEnEPGFIDYVLGTDGDGGDILYRTGLgttmDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGLTK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 236 SALDWLVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTWGSALV 315
Cdd:PRK12879 243 DDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLV 322
|
.
gi 695765315 316 R 316
Cdd:PRK12879 323 K 323
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
3-317 |
1.65e-110 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 325.54 E-value: 1.65e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 3 TKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTS 82
Cdd:PLN02326 48 SKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 83 GTHAFpSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGDGAG 162
Cdd:PLN02326 128 PDDLF-GSAPQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGAG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 163 AVVLGASEEP--GIISTHLHADGR---------YGELLTLPNADR-----VEPENPIY--LTMAGNEVFKVAVTELAHIV 224
Cdd:PLN02326 207 AVVLQACDDDedGLLGFDMHSDGNghkhlhatfKGEDDDSSGGNTngvgdFPPKKASYscIQMNGKEVFKFAVRCVPQVI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 225 DETLAANNLDRSALDWLVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAF 304
Cdd:PLN02326 287 ESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAGF 366
|
330
....*....|...
gi 695765315 305 GGGFTWGSALVRF 317
Cdd:PLN02326 367 GAGLTWGSAIVRW 379
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
1-317 |
9.26e-94 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 281.06 E-value: 9.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVAT 80
Cdd:CHL00203 1 MGVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 81 TSGTHAFpSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGDG 160
Cdd:CHL00203 81 STPDDLF-GSASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 161 AGAVVLGASEEPGIISTHLHADGRYGELLTLPNAD---------RVEPENPIYLTMAGNEVFKVAVTELAHIVDETLAAN 231
Cdd:CHL00203 160 AGAAIIGASYENSILGFKLCTDGKLNSHLQLMNKPvnnqsfgttKLPQGQYQSISMNGKEVYKFAVFQVPAVIIKCLNAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 232 NLDRSALDWLVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTWG 311
Cdd:CHL00203 240 NISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTWG 319
|
....*.
gi 695765315 312 SALVRF 317
Cdd:CHL00203 320 AIVLKW 325
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
3-317 |
2.25e-77 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 239.24 E-value: 2.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 3 TKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTS 82
Cdd:PRK05963 4 SRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLATST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 83 GTHAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDyALVIGADVLARTCDPGDRGTIIIFGDGAG 162
Cdd:PRK05963 84 PDHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQGKP-VLVVAANILSRRINMAERASAVLFADAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 163 AVVLGASEEP--GIISTHLHADGRYGELLTLPNADRVEPENP------IYLTMA-GNEVFKVAVTELAHIVDETLAANNL 233
Cdd:PRK05963 163 AVVLAPSAKAnsGVLGSQLISDGSHYDLIKIPAGGSARPFAPerdaseFLMTMQdGRAVFTEAVRMMSGASQNVLASAAM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 234 DRSALDWLVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTWGSA 313
Cdd:PRK05963 243 TPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAV 322
|
....
gi 695765315 314 LVRF 317
Cdd:PRK05963 323 VMRV 326
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-315 |
6.51e-77 |
|
"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: 238.10 E-value: 6.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 5 IIGTGSYLPEQVRTNADLEKMVetSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGT 84
Cdd:cd00827 4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 85 HAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTiIIFGDGAGAV 164
Cdd:cd00827 82 DKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALE-PTLGDGAAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 165 VLGASEEP---GIISTHLHADGRYG----ELLTLPNADRVEPENPIYLTMA--GNEVFKVAVTELAHIVDETLAANNLDr 235
Cdd:cd00827 161 LVSRNPGIlaaGIVSTHSTSDPGYDfspyPVMDGGYPKPCKLAYAIRLTAEpaGRAVFEAAHKLIAKVVRKALDRAGLS- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 236 SALDWLVPHQAN-LRIISATARKLGMSMDNVVVT----LDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTW 310
Cdd:cd00827 240 EDIDYFVPHQPNgKKILEAVAKKLGGPPEKASQTrwilLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTA 319
|
....*
gi 695765315 311 GSALV 315
Cdd:cd00827 320 EAFVL 324
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
50-315 |
1.31e-59 |
|
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: 191.50 E-value: 1.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 50 TVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNG 129
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 130 AVDYALVIGADvlartcdpgdrgtIIIFGDGAGAVVLGASEE---------PGIISTHLHADGRYGElltlpnadrvepe 200
Cdd:cd00327 86 KADIVLAGGSE-------------EFVFGDGAAAAVVESEEHalrrgahpqAEIVSTAATFDGASMV------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 201 npiyltmagnevFKVAVTELAHIVDETLAANNLDRSALDWLVPHQANLRIISATARKLGMSMD-----NVVVTLDRHGNT 275
Cdd:cd00327 140 ------------PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDgvrspAVSATLIMTGHP 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 695765315 276 SAASVPCALDEAVRDGRI-------QRGQLILLEAFGGGFTWGSALV 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 |
7.51e-59 |
|
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: 192.08 E-value: 7.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 51 VATLGFEAAKNALDMAGVKPEQ----IGLIVVATTSGTHAF---------------------PSSACQIQSMLGINGcPA 105
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYqknpIVGVVVGTGGGSPRFqvfgadamravgpyvvtkamfPGASGQIATPLGIHG-PA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 106 FDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPG------------------DRGTIIIFGDGAGAVVLG 167
Cdd:cd00825 90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEfdamgalstpekasrtfdAAADGFVFGDGAGALVVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 168 ASEE---------PGIISTHLHADGrygelltlpnadrvepenpiyltmAGNEVFKVAVTELAHIVDETLAANNLDRSAL 238
Cdd:cd00825 170 ELEHalargahiyAEIVGTAATIDG------------------------AGMGAFAPSAEGLARAAKEALAVAGLTVWDI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 239 DWLVPHQANLRIISATARKLGMSMD-----NVVVTLDRHGNTSAASVPCALDEAVRDGRI-------------------- 293
Cdd:cd00825 226 DYLVAHGTGTPIGDVKELKLLRSEFgdkspAVSATKAMTGNLSSAAVVLAVDEAVLMLEHgfippsihieeldeaglniv 305
|
330 340
....*....|....*....|....*..
gi 695765315 294 -----QRGQLILLEAFGGGFTWGSALV 315
Cdd:cd00825 306 tettpRELRTALLNGFGLGGTNATLVL 332
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
2-317 |
1.29e-58 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 191.20 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 2 YTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAApNETVATLGFEAAKNALDMAGVKPEQIGLIVVATT 81
Cdd:PRK07204 4 YISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVD-GETSSYMGAEAAKKAVEDAKLTLDDIDCIICASG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 82 SGTHAFPSSACQIQSMLGI--NGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGD 159
Cdd:PRK07204 83 TIQQAIPCTASLIQEQLGLqhSGIPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILFGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 160 GAGAVVLGASEEPG-IISTHL--HADG------RYGELLTLPNADRVEPENPIYLTMAGNEVFKVAVTELAHIVDETLAA 230
Cdd:PRK07204 163 GAAAVVITKGDHSSrILASHMetYSSGahlseiRGGGTMIHPREYSEERKEDFLFDMNGRAIFKLSSKYLMKFIDKLLMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 231 NNLDRSALDWLVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTW 310
Cdd:PRK07204 243 AGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSI 322
|
....*..
gi 695765315 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 |
6.48e-43 |
|
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: 142.64 E-value: 6.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 228 LAANNLDRSALDWLVPHQANLRIISATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGG 307
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 695765315 308 FTWGSALVRF 317
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
5-316 |
7.00e-40 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 143.48 E-value: 7.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 5 IIGTGSYLPEQVRTNADL------------------------EKMVETSDEWIVTRTGIRER----------------RI 44
Cdd:PRK07515 5 ISGTGLYTPPESISNEELvasfnayverfnaenaaaiaagevEALQPSSSEFIEKASGIKSRyvmdkegildpdrmrpRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 45 AA-PNETV---ATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHAFPSSACQIQSMLGINGCpAFDVAAACAGFTYALS 120
Cdd:PRK07515 85 PErSNDELsiqAEMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIEGF-AFDMNVACSSATFGIQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 121 IADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGDGAGAVVLGASEEPG------IISTHLHAD------GRYGEL 188
Cdd:PRK07515 164 TAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATsaggfeILGTRLFTQfsnnirNNFGFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 189 ltlpnaDRVEPENP----IYLTMAGNEVFKVAVTELAHIVDETLAANNLDRSALD--WLvpHQANLRIISATARK-LG-- 259
Cdd:PRK07515 244 ------NRADPEGIgardKLFVQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKrfWL--HQANINMNQLIGKKvLGrd 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 695765315 260 MSMDNVVVTLDRHGNTSAASVPCALDEAVRDgrIQRGQLILLEAFGGGFTWGSALVR 316
Cdd:PRK07515 316 ATPEEAPVILDEYANTSSAGSIIAFHKHSDD--LAAGDLGVICSFGAGYSIGSVIVR 370
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
4-317 |
7.72e-34 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 127.01 E-value: 7.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 4 KIIGTGSYLPEQVRTNADLEKMVETSDEWIVTR----TGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVA 79
Cdd:PRK12880 9 KISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 80 TTSGTHAFPSSACQIQSMLGIN-GCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGaDVLARTCDPGDRGTIIIFG 158
Cdd:PRK12880 89 TQSPDFFMPSTACYLHQLLNLSsKTIAFDLGQACAGYLYGLFVAHSLIQSGLGKILLICG-DTLSKFIHPKNMNLAPIFG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 159 DGAGAVVLGASEEPGIIsTHLHADGRYGELLTLPNADRVEPENPIY----------------LTMAGNEVFKVAVTELAH 222
Cdd:PRK12880 168 DGVSATLIEKTDFNEAF-FELGSDGKYFDKLIIPKGAMRIPKADIFnddslmqteefrqlenLYMDGANIFNMALECEPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 223 IVDETLAANNLDRSALDWLVPHQANLRIISATARKLGMSMDNVV-VTLDRHGNTSAASVPCALDEAVRDGRIQrgqlILL 301
Cdd:PRK12880 247 SFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPnFIMEKYANLSACSLPALLCELDTPKEFK----ASL 322
|
330
....*....|....*.
gi 695765315 302 EAFGGGFTWGSALVRF 317
Cdd:PRK12880 323 SAFGAGLSWGSAVLNF 338
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
5-316 |
3.15e-33 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 125.12 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 5 IIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLiVVATTSGT 84
Cdd:PRK06840 7 IVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDV-VIYIGSEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 85 HAFP--SSACQIQSMLGINGCPAFDVAAACAGFTYALSIA-DQYVKNGAVDYALVIGAdvlARTCDPGDRGT-----III 156
Cdd:PRK06840 86 KDYPvwSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAkDLLYSDPSIENVLLVGG---YRNSDLVDYDNprtrfMFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 157 FGDGAGAVVLGasEEPG---IISTHLHADGRYGELLTLPNADRVEPENP-------IYLTMAGNEVFK-----VAVTELA 221
Cdd:PRK06840 163 FAAGGSAALLK--KDAGknrILGSAIITDGSFSEDVRVPAGGTKQPASPetvenrqHYLDVIDPESMKerldeVSIPNFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 222 HIVDETLAANNLDRSALDWLVP-------HQANLriisataRKLGMSMDNVVVtLDRHGNTSAASVPCALDEAVRDGRIQ 294
Cdd:PRK06840 241 KVIREALRKSGYTPKDIDYLAIlhmkrsaHIALL-------EGLGLTEEQAIY-LDEYGHLGQLDQILSLHLALEQGKLK 312
|
330 340
....*....|....*....|..
gi 695765315 295 RGQLILLEAFGGGFTWGSALVR 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 |
1.31e-32 |
|
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: 115.69 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 106 FDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTIIIFGDGAGAVVLGASEEPG--IISTHLHADG 183
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEPGarILDSVLGSDG 80
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
37-307 |
7.62e-28 |
|
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: 111.04 E-value: 7.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 37 TGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHAFPSSACQIQSMLGIN-GCPAFDVAAACAGF 115
Cdd:COG3425 37 LGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGTESGPDASKPIATYVHGALGLPpNCRAFELKFACYAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 116 TYALSIADQYVKNGAVDYALVIGADVlARTcDPGDRGTiIIFGDGAGAVVLGasEEPGIISTHLHA-------------- 181
Cdd:COG3425 117 TAALQAALGWVASGPNKKALVIASDI-ARY-GPGSAGE-YTQGAGAVAMLVG--ADPRIAEIEGGSgsyttdvmdfwrpn 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 182 -------DGRYGelltlpnadrvepeNPIYLTMagnevfkvavteLAHIVDETLAANNLDRSALDWLVPHQANLRIISAT 254
Cdd:COG3425 192 gsdyplvDGRFS--------------EPAYLDH------------LEEAVKDYKEKTGLKPDDFDYFVFHQPFGKMPKKA 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765315 255 ARKLGMSM---------DNVVVTLD---RHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGG 307
Cdd:COG3425 246 AKKLGRKAgreiqedfeEQVEPSLIysrRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSG 310
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
5-307 |
1.78e-25 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 104.22 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 5 IIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGT 84
Cdd:PRK04262 5 IVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGSESHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 85 HAFPSSACQIQSMLGI-NGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVlARTcDPGDrgtIIIFGDGAGA 163
Cdd:PRK04262 85 YAVKPTATIVAEALGAtPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADT-AQG-APGD---ALEYTAAAGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 164 V--VLGASEEPGIIsthlhaDGRYGelLTLPNADRVEPENPIYlTMAGNEV------FKvavtelaHI---VDETLAANN 232
Cdd:PRK04262 160 AafIIGKEEVIAEI------EATYS--YTTDTPDFWRREGEPY-PRHGGRFtgepayFK-------HIisaAKGLMEKLG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765315 233 LDRSALDWLVPHQANLRIISATARKLGMSMDNVVVTL--DRHGNTSAASVPCALdEAVRDgRIQRGQLILLEAFGGG 307
Cdd:PRK04262 224 LKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLltPYIGNTYSGSALLGL-AAVLD-VAKPGDRILVVSFGSG 298
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
3-317 |
3.31e-24 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 100.60 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 3 TKIIGTGSYLPEQVRTNADLEKMVETSDEW----------IVTRTGIRERRIAAPNETVAT-----------------LG 55
Cdd:COG3424 2 ARILSIATAVPPHRYTQEEIAEFAAELFGLderdrrrlrrLFENSGIETRHSVLPLEWYLEppsfgernalyieealeLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 56 FEAAKNALDMAGVKPEQIGLIVVATTSGTHAfPSSACQIQSMLGIN-----------GCpafdvAAACAGftyaLSIADQ 124
Cdd:COG3424 82 EEAARRALDKAGLDPEDIDHLVTVSCTGFAA-PGLDARLINRLGLRpdvrrlpvggmGC-----AAGAAG----LRRAAD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 125 YVKNGAVDYALVIGADVLARTCDPGD--RGTII---IFGDGAGAVVLGASEEPG----IISTHLHadgrygellTLPNAD 195
Cdd:COG3424 152 FLRADPDAVVLVVCVELCSLTFQRDDdsKDNLVanaLFGDGAAAVVVSGDPRPGpgprILAFRSY---------LIPDTE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 196 RVepenpiyltMA---GNEVFKV--------AVTE-LAHIVDETLAANNLDRSALDWLVPHQANLRIISATARKLGMSMD 263
Cdd:COG3424 223 DV---------MGwdvGDTGFRMvlspevpdLIAEhLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPE 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 695765315 264 NVVVT---LDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTWGSALVRF 317
Cdd:COG3424 294 ALAHSrevLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGFTAELVLLRW 350
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
41-309 |
3.81e-24 |
|
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: 100.76 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 41 ERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHAfPSSACQI-----------QSMLGINGCpafdvA 109
Cdd:cd00831 75 DERNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPT-PSLDAMLinrlglrpdvkRYNLGGMGC-----S 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 110 AACAgftyALSIADQYVKNGAVDYALVIGADVLART-CDPGDRGTII---IFGDGAGAVVLGASEEPGIISTH---LHAD 182
Cdd:cd00831 149 AGAI----ALDLAKDLLEANPGARVLVVSTELCSLWyRGPDHRSMLVgnaLFGDGAAAVLLSNDPRDRRRERPlfeLVRA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 183 GRYgellTLPNADRVEPenpIYLTMAGNEV-FKVAVTELAH-----IVDETLAANNLDRSALD---WLVpHQANLRIISA 253
Cdd:cd00831 225 AST----LLPDSEDAMG---WHLGEEGLTFvLSRDVPRLVEknlerVLRKLLARLGIGLFKLAfdhWCV-HPGGRAVLDA 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 695765315 254 TARKLGMSMDNVVV---TLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFT 309
Cdd:cd00831 297 VEKALGLSPEDLEAsrmVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFT 355
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
37-307 |
4.00e-23 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 97.64 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 37 TGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHAFPSSACQIQSMLGING-CPAFDVAAACAGF 115
Cdd:PRK09258 47 TGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGLLINTSVCRDYLEPATACRVHHNLGLPKsCANFDVSNACLGF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 116 TYALSIADQYVKNGAVDYALVIGA----DVLARTCD-----PGDRGTIIIF------GDGAGAVVLGASEepgiisthLH 180
Cdd:PRK09258 127 LNGMLDAANMIELGQIDYALVVSGesarEIVEATIDrllapETTREDFAQSfatltlGSGAAAAVLTRGS--------LH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 181 ADG-RYgelltLPNADRVEPE-------NPIYLTMAGNEVFKVAVtELAHIV-DETLAANNLDRSALDWLVPHQANLRII 251
Cdd:PRK09258 199 PRGhRL-----LGGVTRAATEhhelcqgGRDGMRTDAVGLLKEGV-ELAVDTwEAFLAQLGWAVEQVDRVICHQVGAAHT 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 695765315 252 SATARKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGG 307
Cdd:PRK09258 273 RAILKALGIDPEKVFTTFPTLGNMGPASLPITLAMAAEEGFLKPGDRVALLGIGSG 328
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
5-301 |
8.18e-16 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 77.26 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 5 IIGTGSYLPEQVRTNADLE-------KMVETSDEWIVTRTGIRERRIA-----APNETVATLGFEAAKNALDMAGVKPEQ 72
Cdd:PRK06816 5 ITSTGAFLPGEPVSNDEMEaylglinGKPSRARRIILRNNGIKTRHYAldpegRPTHSNAQMAAEAIRDLLDDAGFSLGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 73 IGLIVVATTSGTHAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVL-----ARTCD 147
Cdd:PRK06816 85 IELLACGTSQPDQLMPGHASMVHGELGAPPIEVVSSAGVCAAGMMALKYAYLSVKAGESRNAVATASELAsrwfrASRFE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 148 PG-------DRGTIIIF---------GDGAGAVVLGASEEPGIIS-----THL--HAD------------GRYGELLTLP 192
Cdd:PRK06816 165 AEeeklaelEENPEIAFekdflrwmlSDGAGAVLLENKPRPDGLSlridwIDLrsYAGelpvcmyagaekNEDGSLKGWS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 193 NADRVEPENpiyltmAG-----------NEVFKVAVTE-LAHIVDEtlaaNNLDRSALDWLVPHQANLRIISATARKL-- 258
Cdd:PRK06816 245 DYPPEEAEA------ASalslkqdvrllNENIVVYTIKpLLELVDK----RNLDPDDIDYFLPHYSSEYFREKIVELLak 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 695765315 259 ---GMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILL 301
Cdd:PRK06816 315 agfMIPEEKWFTNLATVGNTGSASIYIMLDELLNSGRLKPGQKILC 360
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
47-140 |
1.99e-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: 64.21 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 47 PNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHAFPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYV 126
Cdd:cd00829 12 SDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPATRVEAAGASGSAAVRAAAAAI 91
|
90
....*....|....
gi 695765315 127 KNGAVDYALVIGAD 140
Cdd:cd00829 92 ASGLADVVLVVGAE 105
|
|
| PLN03171 |
PLN03171 |
chalcone synthase-like protein; Provisional |
23-309 |
2.55e-08 |
|
chalcone synthase-like protein; Provisional
Pssm-ID: 178715 [Multi-domain] Cd Length: 399 Bit Score: 54.62 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 23 EKMVETSDEWIVTRTGIRERRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHaFPSSACQI-------- 94
Cdd:PLN03171 80 EELLSAHPEFLDHDAPSLDARLDIAADAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSGAH-IPGVDFRLvpllglrp 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 95 ---QSMLGINGCpafdvAAACAgftyALSIADQYVKNGAVDYALVIGADVLARTCDPGDRG---TII---IFGDGAGAVV 165
Cdd:PLN03171 159 svrRTMLHLNGC-----FAGAA----ALRLAKDLAENNRGARVLVVAAEITLLLFNGPDEGcfqTLLnqgLFGDGAAAVI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 166 LGASEepgiisthLHADGRYGELLTLpnADRVEPENPIYLTMAGNEVFKVAVTELAHIvdETLAANNLDRSALDWLVP-- 243
Cdd:PLN03171 230 VGADA--------DAAERPLFEIVSA--AQAIIPESDDAINMHFTEGGLDGNIGTRQV--PGLIGDNIERCLLDAFAPll 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 244 ---------------HQANLRIISATARKLGMSMDNVVVT---LDRHGNTSAASVPCALDEAVRdgRIQRG-------QL 298
Cdd:PLN03171 298 ggdggaewndlfwavHPGSSAILDQVDAALGLEPEKLAASrrvLSDYGNMFGATVIFALDELRR--QMEEAaaagawpEL 375
|
330
....*....|.
gi 695765315 299 ILLEAFGGGFT 309
Cdd:PLN03171 376 GVMMAFGPGLT 386
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
50-140 |
7.09e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 50.23 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 50 TVATLGFEAAKNALDMAGVKPEQIGLIVVATTS--GTHAFPssACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVK 127
Cdd:PRK12578 20 SVQELAWESIKEALNDAGVSQTDIELVVVGSTAyrGIELYP--APIVAEYSGLTGKVPLRVEAMCATGLAASLTAYTAVA 97
|
90
....*....|...
gi 695765315 128 NGAVDYALVIGAD 140
Cdd:PRK12578 98 SGLVDMAIAVGVD 110
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
49-140 |
1.38e-06 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 49.38 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 49 ETVATLGFEAAKNALDMAGVKPEQIGLIVVATT--SGTHAFPSSACQIQSmLGINGCPAFDVAAACAGFTYALSIADQYV 126
Cdd:PRK06059 21 RDFVEYGVVAARAALADAGLDWRDVQLVVGADTirNGYPGFVAGATFAQA-LGWNGAPVSSSYAACASGSQALQSARAQI 99
|
90
....*....|....
gi 695765315 127 KNGAVDYALVIGAD 140
Cdd:PRK06059 100 LAGLCDVALVVGAD 113
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
54-189 |
5.93e-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: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 54 LGFEAAKNALDMAG-----VKPEQIGLIVVATTSGTHAF--------------------PSS-----ACQIQSMLGINGc 103
Cdd:COG0304 74 YALAAAREALADAGldldeVDPDRTGVIIGSGIGGLDTLeeayrallekgprrvspffvPMMmpnmaAGHVSIRFGLKG- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 104 PAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGAD---------------VLARTCD-------PGDR---GTIIifG 158
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEaaitplglagfdalgALSTRNDdpekasrPFDKdrdGFVL--G 230
|
170 180 190
....*....|....*....|....*....|....*
gi 695765315 159 DGAGAVVLgasEEPGiisthlHADGR----YGELL 189
Cdd:COG0304 231 EGAGVLVL---EELE------HAKARgakiYAEVV 256
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
51-311 |
9.87e-05 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 43.49 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 51 VATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHaFPSSACQIQSMLGINgcPAFDVA----AACAGFTYALSIADQYV 126
Cdd:PLN03168 101 VPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVN-MPGADHALAKLLGLK--PTVKRVmmyqTGCFGGASVLRVAKDLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 127 KNGAVDYALVIGADVLARTCDPGDRGTI------IIFGDGAGAVVLGASEEPGiISTHLHADGRYGELLtLPNADrvepe 200
Cdd:PLN03168 178 ENNKGARVLAVASEVTAVTYRAPSENHLdglvgsALFGDGAGVYVVGSDPKPE-VEKALFEVHWAGETI-LPESD----- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 201 NPI--YLTMAG------NEVFKVAVTELAHIVDETL-AANNLDRSALDWLVpHQANLRIISATARKLGMSMDNVVVTLD- 270
Cdd:PLN03168 251 GAIdgHLTEAGlifhlmKDVPGLISKNIEKFLNEARkCVGSPDWNEMFWAV-HPGGPAILDQVEAKLKLTKDKMQGSRDi 329
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 695765315 271 --RHGNTSAASVPCALDEaVRDGRIQRGQLILLEAFGGGFTWG 311
Cdd:PLN03168 330 lsEFGNMSSASVLFVLDQ-IRQRSVKMGASTLGEGSEFGFFIG 371
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
54-189 |
1.35e-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: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 54 LGFEAAKNALDMAG-----VKPEQIGLIVVATTSGTHAF------------------------PSSAC-QIQSMLGINGc 103
Cdd:cd00834 74 FALAAAEEALADAGldpeeLDPERIGVVIGSGIGGLATIeeayrallekgprrvspffvpmalPNMAAgQVAIRLGLRG- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 104 PAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVL----------------ARTCDPG--------DRGTIIIfGD 159
Cdd:cd00834 153 PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALitpltlagfaalralsTRNDDPEkasrpfdkDRDGFVL-GE 231
|
170 180 190
....*....|....*....|....*....|....
gi 695765315 160 GAGAVVLgASEEpgiisthlHADGR----YGELL 189
Cdd:cd00834 232 GAGVLVL-ESLE--------HAKARgakiYAEIL 256
|
|
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
51-311 |
6.71e-04 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 41.19 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 51 VATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHaFPSSACQIQSMLGINGCPA--FDVAAACAGFTYALSIADQYVKN 128
Cdd:PLN03172 102 VPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLKPSVKrfMMYQQGCFAGGTVLRLAKDLAEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 129 GAVDYALVIGADVLARTC-DPGDR--GTII---IFGDGAGAVVLGASEEPGIisthlhaDGRYGELLTLPNADRVEPENP 202
Cdd:PLN03172 181 NAGSRVLVVCSEITAVTFrGPSDThlDSLVgqaLFGDGAAAVIIGADPDTKI-------ERPLFEIVSAAQTILPDSDGA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 203 IyltmaGNEVFKVAVTelAHIVDET--LAANNLDRSALDWLVP-------------HQANLRIISATARKLGMSMDNVVV 267
Cdd:PLN03172 254 I-----DGHLREVGLT--FHLLKDVpgLISKNIEKSLVEAFAPigindwnsifwiaHPGGPAILDQVEIKLDLKEEKLRA 326
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 695765315 268 T---LDRHGNTSAASVPCALDEaVRDGRIQRGQlillEAFGGGFTWG 311
Cdd:PLN03172 327 TrhvLSDYGNMSSACVLFILDE-MRKKSIEEGK----GSTGEGLEWG 368
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
57-166 |
8.65e-04 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 40.62 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 57 EAAKNALDMAGVKPEQ-----IGLIVVATTSGTHAFPSSACQIQSMLGINGC-----------------PAFDVAAACAG 114
Cdd:cd00833 93 EVAWEALEDAGYSPESlagsrTGVFVGASSSDYLELLARDPDEIDAYAATGTsraflanrisyffdlrgPSLTVDTACSS 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765315 115 FTYALSIADQYVKNGAVDYALVIGADV---------------LART--CDPGDR---GTiiIFGDGAGAVVL 166
Cdd:cd00833 173 SLVALHLACQSLRSGECDLALVGGVNLilspdmfvgfskagmLSPDgrCRPFDAdadGY--VRGEGVGVVVL 242
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
189-316 |
1.23e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 40.34 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 189 LTLPNADRVEpenpIYLTMAGNEVFKVAVTelAHIVDETLAANNL-----DRSALDWLvphQANLRIISatarklgMSMD 263
Cdd:PLN02192 364 LVLPMSEQLL----FFATLVGKKLFKMKLK--PYIPDFKLAFEHFcihagGRAVLDEL---EKNLQLSD-------WHME 427
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 695765315 264 NVVVTLDRHGNTSAASVPCALDEAVRDGRIQRGQLILLEAFGGGFTWGSALVR 316
Cdd:PLN02192 428 PSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRTWQIAFGSGFKCNSAVWK 480
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
42-153 |
1.80e-03 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 39.67 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 42 RRIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTH--------AFPSSACQiqsmlGINGCPAFDVAAACA 113
Cdd:PRK06289 17 RNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGELfagqghlgAMPATVHP-----ALWGVPASRHEAACA 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 695765315 114 GFTYALSIADQYVKNGAVDYALVIGADVLaRTCdPGDRGT 153
Cdd:PRK06289 92 SGSVATLAAMADLRAGRYDVALVVGVELM-KTV-PGDVAA 129
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
51-311 |
2.03e-03 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 39.67 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 51 VATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHaFPSSACQIQSMLGINGCPA--FDVAAACAGFTYALSIADQYVKN 128
Cdd:PLN03173 102 VPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLRSSVKrfMMYQQGCFAGGTVLRLAKDLAEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 129 GAVDYALVIGADVLARTC-DPGDR--GTII---IFGDGAGAVVLGASEEPGIISTHLhadgrygELLT-----LPNADRV 197
Cdd:PLN03173 181 NKGARVLVVCSEITAVTFrGPSDThlDSLVgqaLFGDGAAAIIIGSDPVLGVEKPLF-------ELVSaaqtiLPDSDGA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 198 epenpiyltmAGNEVFKVAVTelAHIVDET--LAANNLDRSAL---------DW----LVPHQANLRIISATARKLGMSM 262
Cdd:PLN03173 254 ----------IDGHLREVGLT--FHLLKDVpgLISKNVEKSLTeafkplgisDWnslfWIAHPGGPAILDQVEAKLALKP 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 695765315 263 DNVVVT---LDRHGNTSAASVPCALDEaVRDGRIQRGqlilLEAFGGGFTWG 311
Cdd:PLN03173 322 EKLRATrhvLSEYGNMSSACVLFILDE-MRKKSAEDG----LKSTGEGLEWG 368
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
42-166 |
2.95e-03 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 38.86 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 42 RRIAAPNETVATLGFEAAKNALdMAGVKPEQIGLIV-----------------------VATTSGTHAFPSSACQIQS-M 97
Cdd:PRK07103 75 RRASLSAQAALAAAREAWRDAA-LGPVDPDRIGLVVggsnlqqreqalvhetyrdrpafLRPSYGLSFMDTDLVGLCSeQ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 98 LGINGcPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGA------------------------DVLARTCDPGDRGT 153
Cdd:PRK07103 154 FGIRG-EGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGAlmdlsywecqalrslgamgsdrfaDEPEAACRPFDQDR 232
|
170
....*....|....
gi 695765315 154 I-IIFGDGAGAVVL 166
Cdd:PRK07103 233 DgFIYGEACGAVVL 246
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
30-140 |
3.31e-03 |
|
"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: 38.96 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 30 DEWIVTRTGIRERriaapnetVATLGFEAAKNALDMAGVKPEQI------GLIVVATTSGTHA----------------- 86
Cdd:cd00828 59 PGWDAKRTGIVDR--------TTLLALVATEEALADAGITDPYEvhpsevGVVVGSGMGGLRFlrrggkldaravnpyvs 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 87 ------FPSSACQIQSMLGINGCPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGAD 140
Cdd:cd00828 131 pkwmlsPNTVAGWVNILLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVE 190
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
43-168 |
4.38e-03 |
|
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: 37.91 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 43 RIAAPNETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSGTHaFPSSACQIQSMLGINGcpafDVA------AACAGFT 116
Cdd:pfam00195 91 RLEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVR-MPGADYQLAKLLGLRP----SVKrvmlyfQGCYGGA 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 695765315 117 YALSIADQYVKNGAVDYALVIGADVLARTCDPGDRGTI------IIFGDGAGAVVLGA 168
Cdd:pfam00195 166 TVLRTAKDIAENNPGARVLVVCSEITVLGFRGPSKDRLdslvgaALFGDGAAAVIIGA 223
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
91-166 |
4.81e-03 |
|
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: 38.00 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 91 ACQIQSMLGINGcPAFDVAAACAGFTYALSIADQYVKNGAVDYALVIGADVLA--------------------RTCDPGD 150
Cdd:pfam00109 153 AGRISYFLGLRG-PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLtplgfagfsaagmlspdgpcKAFDPFA 231
|
90
....*....|....*.
gi 695765315 151 RGTiiIFGDGAGAVVL 166
Cdd:pfam00109 232 DGF--VRGEGVGAVVL 245
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
49-172 |
6.26e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 38.00 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 49 ETVATLGFEAAKNALDMAGVKPEQIGLIVVATTSG---THAFPSS-ACQIQSMLgiNGCPAFDVAAACAGFTYALSIADQ 124
Cdd:PRK07516 20 ETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAgfsPQDFPASlVLQADPAL--RFKPATRVENACATGSAAVYAALD 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 695765315 125 YVKNGAVDYALVIGADVLARTcdPGDRgtiiifgdgAGAVVLGASEEP 172
Cdd:PRK07516 98 AIEAGRARIVLVVGAEKMTAT--PTAE---------VGDILLGASYLK 134
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
54-138 |
7.55e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 37.57 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765315 54 LGFEAAKNALDMAGVKPEQI-----GLIVVATTSGTHAFPSsacqiqsmLGINGCPAFDVAAACAGFTYALSIADQYVKN 128
Cdd:PRK08256 25 MAAEAGRAALADAGIDYDAVqqayvGYVYGDSTSGQRALYE--------VGMTGIPIVNVNNNCSTGSTALFLARQAVRS 96
|
90
....*....|
gi 695765315 129 GAVDYALVIG 138
Cdd:PRK08256 97 GAADCALALG 106
|
|
| |
