|
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: 583.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVAT 80
Cdd:PRK09352 2 MYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 81 TSSTHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:PRK09352 82 TTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 161 AGAVVLSASEEPGILSTHLHADGRYGELLTLPNADRVNPENPIHLTMAGNEVFKVAVTELAHIVDETLEANNLDRSALDW 240
Cdd:PRK09352 162 AGAVVLGASEEPGILSTHLGSDGSYGDLLYLPGGGSRGPASPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDIDW 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489928855 241 LVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTWGSALVRF 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: 527.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVAT 80
Cdd:TIGR00747 1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 81 TSSTHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:TIGR00747 81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 161 AGAVVLSASEEPG-ILSTHLHADGRYGELLTLPNADRVNPENPIHLTMAGNEVFKVAVTELAHIVDETLEANNLDRSALD 239
Cdd:TIGR00747 161 AGAVVLGESEDPGgIISTHLGADGTQGEALYLPAGGRPTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDID 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489928855 240 WLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTWGSALVRF 317
Cdd:TIGR00747 241 WFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
1-317 |
2.78e-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: 477.68 E-value: 2.78e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVAT 80
Cdd:COG0332 1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 81 TSSTHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:COG0332 81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 161 AGAVVLSASEE-PGILSTHLHADGRYGELLTLPNADRVNPENPI-----HLTMAGNEVFKVAVTELAHIVDETLEANNLD 234
Cdd:COG0332 161 AGAVVLEASEEgPGILGSVLGSDGSGADLLVVPAGGSRNPPSPVdegdhYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 235 RSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTWGSAL 314
Cdd:COG0332 241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320
|
...
gi 489928855 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 |
4.88e-160 |
|
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: 448.91 E-value: 4.88e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 2 YTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVATT 81
Cdd:cd00830 1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 82 SSTHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGDGA 161
Cdd:cd00830 81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 162 GAVVLSASEE-PGILSTHLHADGRYGELLTLPNADRVNP-----ENPIHLTMAGNEVFKVAVTELAHIVDETLEANNLDR 235
Cdd:cd00830 161 GAVVLEATEEdPGILDSVLGSDGSGADLLTIPAGGSRSPfedaeGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 236 SALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTWGSALV 315
Cdd:cd00830 241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-316 |
3.42e-139 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 396.54 E-value: 3.42e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVAT 80
Cdd:PRK12879 3 SYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 81 TSSTHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:PRK12879 83 TTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 161 AGAVVLSASE-EPGILSTHLHADGRYGELLTLPNA----DRVNPENPIHLTMAGNEVFKVAVTELAHIVDETLEANNLDR 235
Cdd:PRK12879 163 AGAVVLEATEnEPGFIDYVLGTDGDGGDILYRTGLgttmDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGLTK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 236 SALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTWGSALV 315
Cdd:PRK12879 243 DDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLV 322
|
.
gi 489928855 316 R 316
Cdd:PRK12879 323 K 323
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
3-317 |
7.41e-112 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 329.01 E-value: 7.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 3 TKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVATTS 82
Cdd:PLN02326 48 SKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 83 STHAFPSAaCQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGDGAG 162
Cdd:PLN02326 128 PDDLFGSA-PQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGAG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 163 AVVLSASEEP--GILSTHLHADGR---------YGELLTLPNADR-VNPENPIH------LTMAGNEVFKVAVTELAHIV 224
Cdd:PLN02326 207 AVVLQACDDDedGLLGFDMHSDGNghkhlhatfKGEDDDSSGGNTnGVGDFPPKkasyscIQMNGKEVFKFAVRCVPQVI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 225 DETLEANNLDRSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAF 304
Cdd:PLN02326 287 ESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAGF 366
|
330
....*....|...
gi 489928855 305 GGGFTWGSALVRF 317
Cdd:PLN02326 367 GAGLTWGSAIVRW 379
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
1-317 |
3.91e-90 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 271.82 E-value: 3.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 1 MYTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVAT 80
Cdd:CHL00203 1 MGVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 81 TSSTHAFPSAAcQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGDG 160
Cdd:CHL00203 81 STPDDLFGSAS-QLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 161 AGAVVLSASEEPGILSTHLHADGRYGELLTLPNADRVNPE---------NPIHLTMAGNEVFKVAVTELAHIVDETLEAN 231
Cdd:CHL00203 160 AGAAIIGASYENSILGFKLCTDGKLNSHLQLMNKPVNNQSfgttklpqgQYQSISMNGKEVYKFAVFQVPAVIIKCLNAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 232 NLDRSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTWG 311
Cdd:CHL00203 240 NISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTWG 319
|
....*.
gi 489928855 312 SALVRF 317
Cdd:CHL00203 320 AIVLKW 325
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-315 |
1.42e-80 |
|
"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: 247.35 E-value: 1.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 5 IIGTGSYLPEQVRTNADLEKMVetSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVATTSST 84
Cdd:cd00827 4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 85 HAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTiIIFGDGAGAV 164
Cdd:cd00827 82 DKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALE-PTLGDGAAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 165 VLSASEEP---GILSTHLHADGRYG----ELLTLPNADRVNPENPIHLTMA--GNEVFKVAVTELAHIVDETLEANNLDr 235
Cdd:cd00827 161 LVSRNPGIlaaGIVSTHSTSDPGYDfspyPVMDGGYPKPCKLAYAIRLTAEpaGRAVFEAAHKLIAKVVRKALDRAGLS- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 236 SALDWLVPHQAN-LRIISATAKKLGMSMDNVVVT----LDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTW 310
Cdd:cd00827 240 EDIDYFVPHQPNgKKILEAVAKKLGGPPEKASQTrwilLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTA 319
|
....*
gi 489928855 311 GSALV 315
Cdd:cd00827 320 EAFVL 324
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
3-317 |
1.69e-76 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 236.93 E-value: 1.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 3 TKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVATTS 82
Cdd:PRK05963 4 SRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLATST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 83 STHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAvKHALVVGSDVLARTCDPTDRGTIIIFGDGAG 162
Cdd:PRK05963 84 PDHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQG-KPVLVVAANILSRRINMAERASAVLFADAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 163 AVVLSASEEP--GILSTHLHADGRYGELLTLPNADRVNPENP------IHLTMA-GNEVFKVAVTELAHIVDETLEANNL 233
Cdd:PRK05963 163 AVVLAPSAKAnsGVLGSQLISDGSHYDLIKIPAGGSARPFAPerdaseFLMTMQdGRAVFTEAVRMMSGASQNVLASAAM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 234 DRSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTWGSA 313
Cdd:PRK05963 243 TPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAV 322
|
....
gi 489928855 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 |
4.06e-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: 189.96 E-value: 4.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 50 TVATMGFAAANRAIEMAGIDKEQIGLIVVATTSSTHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSG 129
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 130 AVKHALVVGSDvlartcdptdrgtIIIFGDGAGAVVLSASEE---------PGILSTHLHADGRYGElltlpnadrvnpe 200
Cdd:cd00327 86 KADIVLAGGSE-------------EFVFGDGAAAAVVESEEHalrrgahpqAEIVSTAATFDGASMV------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 201 npihltmagnevFKVAVTELAHIVDETLEANNLDRSALDWLVPHQANLRIISATAKKLGMSMD-----NVVVTLDRHGNT 275
Cdd:cd00327 140 ------------PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDgvrspAVSATLIMTGHP 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489928855 276 SAASVPCALDEAVRDGRIKAG-------QLILLEAFGGGFTWGSALV 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 |
2.61e-58 |
|
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: 190.54 E-value: 2.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 51 VATMGFAAANRAIEMAGIDKEQ----IGLIVVATTSSTHAF---------------------PSAACQIQSMLGIKGcPA 105
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYqknpIVGVVVGTGGGSPRFqvfgadamravgpyvvtkamfPGASGQIATPLGIHG-PA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 106 FDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDP------------------TDRGTIIIFGDGAGAVVLS 167
Cdd:cd00825 90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCefdamgalstpekasrtfDAAADGFVFGDGAGALVVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 168 ASEE---------PGILSTHLHADGrygelltlpnadrvnpenpihltmAGNEVFKVAVTELAHIVDETLEANNLDRSAL 238
Cdd:cd00825 170 ELEHalargahiyAEIVGTAATIDG------------------------AGMGAFAPSAEGLARAAKEALAVAGLTVWDI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 239 DWLVPHQANLRIISATAKKLGMSMD-----NVVVTLDRHGNTSAASVPCALDEAVRDGRIKA------------------ 295
Cdd:cd00825 226 DYLVAHGTGTPIGDVKELKLLRSEFgdkspAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFippsihieeldeaglniv 305
|
330 340
....*....|....*....|....*..
gi 489928855 296 -------GQLILLEAFGGGFTWGSALV 315
Cdd:cd00825 306 tettpreLRTALLNGFGLGGTNATLVL 332
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
2-317 |
8.89e-58 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 188.89 E-value: 8.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 2 YTKIIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAApNETVATMGFAAANRAIEMAGIDKEQIGLIVVATT 81
Cdd:PRK07204 4 YISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVD-GETSSYMGAEAAKKAVEDAKLTLDDIDCIICASG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 82 SSTHAFPSAACQIQSMLGIK--GCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGD 159
Cdd:PRK07204 83 TIQQAIPCTASLIQEQLGLQhsGIPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILFGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 160 GAGAVVLSASEEPG-ILSTHL--HADG------RYGELLTLPNADRVNPENPIHLTMAGNEVFKVAVTELAHIVDETLEA 230
Cdd:PRK07204 163 GAAAVVITKGDHSSrILASHMetYSSGahlseiRGGGTMIHPREYSEERKEDFLFDMNGRAIFKLSSKYLMKFIDKLLMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 231 NNLDRSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTW 310
Cdd:PRK07204 243 AGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSI 322
|
....*..
gi 489928855 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 |
9.85e-44 |
|
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: 144.95 E-value: 9.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 228 LEANNLDRSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGG 307
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 489928855 308 FTWGSALVRF 317
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
5-316 |
5.43e-43 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 151.57 E-value: 5.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 5 IIGTGSYLPEQVRTNADL------------------------EKMVETSDEWIVTRTGIRERHI---------------- 44
Cdd:PRK07515 5 ISGTGLYTPPESISNEELvasfnayverfnaenaaaiaagevEALQPSSSEFIEKASGIKSRYVmdkegildpdrmrpri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 45 -AAPNETV---ATMGFAAANRAIEMAGIDKEQIGLIVVATTSSTHAFPSAACQIQSMLGIKGCpAFDVAAACAGFTYALS 120
Cdd:PRK07515 85 pERSNDELsiqAEMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIEGF-AFDMNVACSSATFGIQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 121 VADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGDGAGAVVLSASEEPG------ILSTHLHAD------GRYGEL 188
Cdd:PRK07515 164 TAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATsaggfeILGTRLFTQfsnnirNNFGFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 189 ltlpnaDRVNPENP----IHLTMAGNEVFKVAVTELAHIVDETLEANNLDRSALD--WLvpHQANLRIISATAKK-LG-- 259
Cdd:PRK07515 244 ------NRADPEGIgardKLFVQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKrfWL--HQANINMNQLIGKKvLGrd 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489928855 260 MSMDNVVVTLDRHGNTSAASVPCALDEAVRDgrIKAGQLILLEAFGGGFTWGSALVR 316
Cdd:PRK07515 316 ATPEEAPVILDEYANTSSAGSIIAFHKHSDD--LAAGDLGVICSFGAGYSIGSVIVR 370
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
4-317 |
1.50e-40 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 144.72 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 4 KIIGTGSYLPEQVRTNADLEKMVETSDEWIVTR----TGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVA 79
Cdd:PRK12880 9 KISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 80 TTSSTHAFPSAACQIQSMLGIK-GCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGsDVLARTCDPTDRGTIIIFG 158
Cdd:PRK12880 89 TQSPDFFMPSTACYLHQLLNLSsKTIAFDLGQACAGYLYGLFVAHSLIQSGLGKILLICG-DTLSKFIHPKNMNLAPIFG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 159 DGAGAVVLSASEEPGILsTHLHADGRYGELLTLPN-------ADRVNPE---------NPIHLTMAGNEVFKVAVTELAH 222
Cdd:PRK12880 168 DGVSATLIEKTDFNEAF-FELGSDGKYFDKLIIPKgamripkADIFNDDslmqteefrQLENLYMDGANIFNMALECEPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 223 IVDETLEANNLDRSALDWLVPHQANLRIISATAKKLGMSMDNVV-VTLDRHGNTSAASVPCALDEAVRDGRIKAgqliLL 301
Cdd:PRK12880 247 SFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPnFIMEKYANLSACSLPALLCELDTPKEFKA----SL 322
|
330
....*....|....*.
gi 489928855 302 EAFGGGFTWGSALVRF 317
Cdd:PRK12880 323 SAFGAGLSWGSAVLNF 338
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
5-316 |
4.42e-37 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 135.13 E-value: 4.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 5 IIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVvaTTSST 84
Cdd:PRK06840 7 IVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVI--YIGSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 85 HA-FP--SAACQIQSMLGIKGCPAFDVAAACAGFTYALSVA-DQYVKSGAVKHALVVGSdvlARTCDPTDRGT-----II 155
Cdd:PRK06840 85 HKdYPvwSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAkDLLYSDPSIENVLLVGG---YRNSDLVDYDNprtrfMF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 156 IFGDGAGAVVLsaSEEPG---ILSTHLHADGRYGELLTLPNADRVNP------ENPIH-LTMAGNEVFK-----VAVTEL 220
Cdd:PRK06840 162 NFAAGGSAALL--KKDAGknrILGSAIITDGSFSEDVRVPAGGTKQPaspetvENRQHyLDVIDPESMKerldeVSIPNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 221 AHIVDETLEANNLDRSALDWLVP-------HQANLRiisatakKLGMSMDNVVVtLDRHGNTSAASVPCALDEAVRDGRI 293
Cdd:PRK06840 240 LKVIREALRKSGYTPKDIDYLAIlhmkrsaHIALLE-------GLGLTEEQAIY-LDEYGHLGQLDQILSLHLALEQGKL 311
|
330 340
....*....|....*....|...
gi 489928855 294 KAGQLILLEAFGGGFTWGSALVR 316
Cdd:PRK06840 312 KDGDLVVLVSAGTGYTWAATVIR 334
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
106-183 |
3.68e-35 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 122.24 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 106 FDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTDRGTIIIFGDGAGAVVLSASEEPG--ILSTHLHADG 183
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEPGarILDSVLGSDG 80
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
37-307 |
1.18e-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: 113.35 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 37 TGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVATTSSTHAFPSAACQIQSMLGI-KGCPAFDVAAACAGF 115
Cdd:COG3425 37 LGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGTESGPDASKPIATYVHGALGLpPNCRAFELKFACYAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 116 TYALSVADQYVKSGAVKHALVVGSDVlARtcdpTDRGTiiiFGD---GAGAVVLSASEEPGILSTHLHAdGRYGElltlp 192
Cdd:COG3425 117 TAALQAALGWVASGPNKKALVIASDI-AR----YGPGS---AGEytqGAGAVAMLVGADPRIAEIEGGS-GSYTT----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 193 naD------RVNPENPIHLTMAGNEVFKVAVTElahIVDETLEANNLDRSALDWLVPHQANLRIISATAKKLGMSM---- 262
Cdd:COG3425 183 --DvmdfwrPNGSDYPLVDGRFSEPAYLDHLEE---AVKDYKEKTGLKPDDFDYFVFHQPFGKMPKKAAKKLGRKAgrei 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489928855 263 -----DNVVVTLD---RHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGG 307
Cdd:COG3425 258 qedfeEQVEPSLIysrRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSG 310
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
3-317 |
1.97e-24 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 101.37 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 3 TKIIGTGSYLPEQVRTNADLEKMVETSDEW----------IVTRTGIRERHIAAPNETVAT-----------------MG 55
Cdd:COG3424 2 ARILSIATAVPPHRYTQEEIAEFAAELFGLderdrrrlrrLFENSGIETRHSVLPLEWYLEppsfgernalyieealeLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 56 FAAANRAIEMAGIDKEQIGLIVvaTTSST-HAFPSAACQIQSMLGIK-----------GCpafdvAAACAGftyaLSVAD 123
Cdd:COG3424 82 EEAARRALDKAGLDPEDIDHLV--TVSCTgFAAPGLDARLINRLGLRpdvrrlpvggmGC-----AAGAAG----LRRAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 124 QYVKSGAVKHALVVGSDVlartC------DPTDRGTII---IFGDGAGAVVLSASEEPG----ILSTHLHadgrygellT 190
Cdd:COG3424 151 DFLRADPDAVVLVVCVEL----CsltfqrDDDSKDNLVanaLFGDGAAAVVVSGDPRPGpgprILAFRSY---------L 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 191 LPNADRVnpenpihltMA---GNEVFKV--------AVTE-LAHIVDETLEANNLDRSALDWLVPHQANLRIISATAKKL 258
Cdd:COG3424 218 IPDTEDV---------MGwdvGDTGFRMvlspevpdLIAEhLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEAL 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489928855 259 GMSMDNVVVT---LDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTWGSALVRF 317
Cdd:COG3424 289 GLPPEALAHSrevLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGFTAELVLLRW 350
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
27-309 |
1.42e-23 |
|
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: 99.22 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 27 ETSDEWIVTRTGIRERHIAAPNETVAtMGFAAANRAIEMAGIDKEQIGLIVVATTSSTHAfPSAACQIQSMLGIKGcpaf 106
Cdd:cd00831 62 ETYAPRPEMSPSLDERNDIALEEARE-LAEEAARGALDEAGLRPSDIDHLVVNTSTGNPT-PSLDAMLINRLGLRP---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 107 DVAA------ACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDPTD-RGTII---IFGDGAGAVVLSASEEPGILS 176
Cdd:cd00831 136 DVKRynlggmGCSAGAIALDLAKDLLEANPGARVLVVSTELCSLWYRGPDhRSMLVgnaLFGDGAAAVLLSNDPRDRRRE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 177 TH---LHADGRYgellTLPNADRVnpenpI--HLTMAGNEV-FKVAVTELAH-----IVDETLEANNLDRSALD---WLV 242
Cdd:cd00831 216 RPlfeLVRAAST----LLPDSEDA-----MgwHLGEEGLTFvLSRDVPRLVEknlerVLRKLLARLGIGLFKLAfdhWCV 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 243 pHQANLRIISATAKKLGMSMDNVVV---TLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFT 309
Cdd:cd00831 287 -HPGGRAVLDAVEKALGLSPEDLEAsrmVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFT 355
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
37-307 |
2.54e-22 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 95.33 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 37 TGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVATTSSTHAFPSAACQIQSMLGI-KGCPAFDVAAACAGF 115
Cdd:PRK09258 47 TGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGLLINTSVCRDYLEPATACRVHHNLGLpKSCANFDVSNACLGF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 116 TYALSVADQYVKSGAVKHALVVG----SDVLARTCD-----PTDRGTIIIF------GDGAGAVVLSASEepgilsthLH 180
Cdd:PRK09258 127 LNGMLDAANMIELGQIDYALVVSgesaREIVEATIDrllapETTREDFAQSfatltlGSGAAAAVLTRGS--------LH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 181 ADG-RYgelltLPNADRVNPENpIHLTMAGNEVFKV-AVTELAHIV-------DETLEANNLDRSALDWLVPHQANLRII 251
Cdd:PRK09258 199 PRGhRL-----LGGVTRAATEH-HELCQGGRDGMRTdAVGLLKEGVelavdtwEAFLAQLGWAVEQVDRVICHQVGAAHT 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489928855 252 SATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGG 307
Cdd:PRK09258 273 RAILKALGIDPEKVFTTFPTLGNMGPASLPITLAMAAEEGFLKPGDRVALLGIGSG 328
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
5-307 |
1.99e-21 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 93.05 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 5 IIGTGSYLPEQVRTNADLEKMVETSDEWIVTRTGIRERHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVATTSST 84
Cdd:PRK04262 5 IVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGSESHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 85 HAFPSAACQIQSMLGI-KGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVL-ARTCDPTDRGTiiifGDGAG 162
Cdd:PRK04262 85 YAVKPTATIVAEALGAtPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADTAqGAPGDALEYTA----AAGGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 163 AVVLSASEEPGILsthlhaDGRYGelLTLPNADRVNPENpIHLTMAGNEV------FKvavtelaHI---VDETLEANNL 233
Cdd:PRK04262 161 AFIIGKEEVIAEI------EATYS--YTTDTPDFWRREG-EPYPRHGGRFtgepayFK-------HIisaAKGLMEKLGL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489928855 234 DRSALDWLVPHQANLRIISATAKKLGMSMDNVVVTL--DRHGNTSAASVPCALdEAVRDgRIKAGQLILLEAFGGG 307
Cdd:PRK04262 225 KPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLltPYIGNTYSGSALLGL-AAVLD-VAKPGDRILVVSFGSG 298
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
5-301 |
6.94e-18 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 83.03 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 5 IIGTGSYLPEQVRTNADLE-------KMVETSDEWIVTRTGIRERHIA-----APNETVATMGFAAANRAIEMAGIDKEQ 72
Cdd:PRK06816 5 ITSTGAFLPGEPVSNDEMEaylglinGKPSRARRIILRNNGIKTRHYAldpegRPTHSNAQMAAEAIRDLLDDAGFSLGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 73 IGLIVVATTSSTHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVL-----ARTCD 147
Cdd:PRK06816 85 IELLACGTSQPDQLMPGHASMVHGELGAPPIEVVSSAGVCAAGMMALKYAYLSVKAGESRNAVATASELAsrwfrASRFE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 148 P-------TDRGTIIIF---------GDGAGAVVLSASEEPGILS-----THL-----------------HADGRYGELL 189
Cdd:PRK06816 165 AeeeklaeLEENPEIAFekdflrwmlSDGAGAVLLENKPRPDGLSlridwIDLrsyagelpvcmyagaekNEDGSLKGWS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 190 TLPNADRVNpenpihltmAG-----------NEVFKVAVTE-LAHIVDEtleaNNLDRSALDWLVPHQANLRIISATAKK 257
Cdd:PRK06816 245 DYPPEEAEA---------ASalslkqdvrllNENIVVYTIKpLLELVDK----RNLDPDDIDYFLPHYSSEYFREKIVEL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489928855 258 L-----GMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILL 301
Cdd:PRK06816 312 LakagfMIPEEKWFTNLATVGNTGSASIYIMLDELLNSGRLKPGQKILC 360
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
42-178 |
4.37e-10 |
|
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: 59.97 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 42 RHIAAPNETVATMGFAAANRAIEMAGIDKEQIGLIVVATTSS--THAFPSAacQIQSMLGIKGCPAFDVAAACAGFTYAL 119
Cdd:cd00829 7 PFGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGgrFQSFPGA--LIAEYLGLLGKPATRVEAAGASGSAAV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489928855 120 SVADQYVKSGAVKHALVVGSDVlartcdPTDRGTIIIFGDGAGAVVLSASEEPGILSTH 178
Cdd:cd00829 85 RAAAAAIASGLADVVLVVGAEK------MSDVPTGDEAGGRASDLEWEGPEPPGGLTPP 137
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
54-189 |
7.84e-08 |
|
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: 53.18 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 54 MGFAAANRAIEMAGI-----DKEQIGLIVVATTSSTHAF----------------P---------SAACQIQSMLGIKGc 103
Cdd:COG0304 74 YALAAAREALADAGLdldevDPDRTGVIIGSGIGGLDTLeeayrallekgprrvsPffvpmmmpnMAAGHVSIRFGLKG- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 104 PAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSD---------------VLA-RTCDPT--------DR-GTIIifG 158
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEaaitplglagfdalgALStRNDDPEkasrpfdkDRdGFVL--G 230
|
170 180 190
....*....|....*....|....*....|....*
gi 489928855 159 DGAGAVVLSaSEEpgilsthlHADGR----YGELL 189
Cdd:COG0304 231 EGAGVLVLE-ELE--------HAKARgakiYAEVV 256
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
54-189 |
1.36e-07 |
|
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: 52.54 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 54 MGFAAANRAIEMAGI-----DKEQIGLIVVATTSSTHAFP-------------------------SAACQIQSMLGIKGc 103
Cdd:cd00834 74 FALAAAEEALADAGLdpeelDPERIGVVIGSGIGGLATIEeayrallekgprrvspffvpmalpnMAAGQVAIRLGLRG- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 104 PAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVL----------------ARTCDPT--------DRGTIIIfGD 159
Cdd:cd00834 153 PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALitpltlagfaalralsTRNDDPEkasrpfdkDRDGFVL-GE 231
|
170 180 190
....*....|....*....|....*....|....
gi 489928855 160 GAGAVVLSASEepgilsthlHADGR----YGELL 189
Cdd:cd00834 232 GAGVLVLESLE---------HAKARgakiYAEIL 256
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
18-311 |
5.13e-07 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 50.81 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 18 TNADLEKMVETSDEWIVTRTGIRERHIAAPNET-------------------------VATMGFAAANRAIEMAGIDKEQ 72
Cdd:PLN03168 43 TNCGEKEALKAKFKRICDKSGIRKRHMFLTEEVlkanpgictymepslnvrhdivvvqVPKLAAEAAQKAIKEWGGRKSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 73 IGLIVVATTSSTHaFPSAACQIQSMLGIKgcPAFDVA----AACAGFTYALSVADQYVKSGAVKHALVVGSDVLARTCDP 148
Cdd:PLN03168 123 ITHIVFATTSGVN-MPGADHALAKLLGLK--PTVKRVmmyqTGCFGGASVLRVAKDLAENNKGARVLAVASEVTAVTYRA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 149 TDRGTI------IIFGDGAGAVVLSASEEPGIlSTHLHADGRYGELLtLPNADrvnpeNPI--HLTMAG------NEVFK 214
Cdd:PLN03168 200 PSENHLdglvgsALFGDGAGVYVVGSDPKPEV-EKALFEVHWAGETI-LPESD-----GAIdgHLTEAGlifhlmKDVPG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 215 VAVTELAHIVDETLE-ANNLDRSALDWLVpHQANLRIISATAKKLGMSMDNVVVTLD---RHGNTSAASVPCALDEaVRD 290
Cdd:PLN03168 273 LISKNIEKFLNEARKcVGSPDWNEMFWAV-HPGGPAILDQVEAKLKLTKDKMQGSRDilsEFGNMSSASVLFVLDQ-IRQ 350
|
330 340
....*....|....*....|.
gi 489928855 291 GRIKAGQLILLEAFGGGFTWG 311
Cdd:PLN03168 351 RSVKMGASTLGEGSEFGFFIG 371
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
49-140 |
2.85e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 42.06 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 49 ETVATMGFAAANRAIEMAGIDKEQIGLIVVATTSStHAFPS--AACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYV 126
Cdd:PRK06059 21 RDFVEYGVVAARAALADAGLDWRDVQLVVGADTIR-NGYPGfvAGATFAQALGWNGAPVSSSYAACASGSQALQSARAQI 99
|
90
....*....|....
gi 489928855 127 KSGAVKHALVVGSD 140
Cdd:PRK06059 100 LAGLCDVALVVGAD 113
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
51-311 |
3.62e-04 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 42.01 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 51 VATMGFAAANRAIEMAGIDKEQIGLIVVATTSSTHaFPSAACQIQSMLGIKgcPAFD----VAAACAGFTYALSVADQYV 126
Cdd:PLN03170 106 VPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKMLGLR--PSVNrlmmYQQGCFAGGTVLRVAKDLA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 127 KSGAVKHALVVGSDVLARTCDPTDRGTI------IIFGDGAGAVVLSASEEPGILSTHLhadgrygELLTLPNADRVNPE 200
Cdd:PLN03170 183 ENNRGARVLVVCSEITAVTFRGPSESHLdsmvgqALFGDGAAAVIVGADPDERVERPLF-------QLVSASQTILPDSE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 201 NPI--HLTMAG--NEVFKVAVTELAHIVDETLEANNLDRSALDW----LVPHQANLRIISATAKKLGMSMDNVVVT---L 269
Cdd:PLN03170 256 GAIdgHLREVGltFHLLKDVPGLISKNIERSLEEAFKPLGITDYnsifWVAHPGGPAILDQVEAKVGLEKERMRATrhvL 335
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489928855 270 DRHGNTSAASVPCALDE----AVRDGRIKAGQlilleafggGFTWG 311
Cdd:PLN03170 336 SEYGNMSSACVLFILDEmrkrSAEDGQATTGE---------GFDWG 372
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
50-149 |
4.34e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 41.75 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 50 TVATMGFAAANRAIEMAGIDKEQIGLIVVATTS--STHAFPsaACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVK 127
Cdd:PRK12578 20 SVQELAWESIKEALNDAGVSQTDIELVVVGSTAyrGIELYP--APIVAEYSGLTGKVPLRVEAMCATGLAASLTAYTAVA 97
|
90 100
....*....|....*....|..
gi 489928855 128 SGAVKHALVVGSDVLARTCDPT 149
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTEVDTST 119
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
49-138 |
5.31e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 41.47 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 49 ETVATMGFAAANRAIEMAGIDKEQIGLIVVATTS---STHAFPSA-ACQIQSMLGIKgcPAFDVAAACAGFTYALSVADQ 124
Cdd:PRK07516 20 ETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNagfSPQDFPASlVLQADPALRFK--PATRVENACATGSAAVYAALD 97
|
90
....*....|....
gi 489928855 125 YVKSGAVKHALVVG 138
Cdd:PRK07516 98 AIEAGRARIVLVVG 111
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
30-170 |
7.60e-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: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 30 DEWIVTRTGIRERhiaapnetVATMGFAAANRAIEMAGIDKEQI------GLIVVATTSSTHA----------------- 86
Cdd:cd00828 59 PGWDAKRTGIVDR--------TTLLALVATEEALADAGITDPYEvhpsevGVVVGSGMGGLRFlrrggkldaravnpyvs 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 87 ------FPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSD-------------------- 140
Cdd:cd00828 131 pkwmlsPNTVAGWVNILLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEdpleeglsgfanmgalstae 210
|
170 180 190
....*....|....*....|....*....|..
gi 489928855 141 -VLARTCDPTD-RGTIIIFGDGAGAVVLSASE 170
Cdd:cd00828 211 eEPEEMSRPFDeTRDGFVEAEGAGVLVLERAE 242
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
51-311 |
9.99e-04 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 40.45 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 51 VATMGFAAANRAIEMAGIDKEQIGLIVVATTSSTHaFPSAACQIQSMLGIKGCPA--FDVAAACAGFTYALSVADQYVKS 128
Cdd:PLN03173 102 VPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLRSSVKrfMMYQQGCFAGGTVLRLAKDLAEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 129 GAVKHALVVGSDVLARTC-DPTDR--GTII---IFGDGAGAVVLSASEEPGILSTHLhadgrygELLTLPNADRVNPENP 202
Cdd:PLN03173 181 NKGARVLVVCSEITAVTFrGPSDThlDSLVgqaLFGDGAAAIIIGSDPVLGVEKPLF-------ELVSAAQTILPDSDGA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 203 I--HLTMAG------NEVFKVAVTELAHIVDETLEANNL-DRSALDWlVPHQANLRIISATAKKLGMSMDNVVVT---LD 270
Cdd:PLN03173 254 IdgHLREVGltfhllKDVPGLISKNVEKSLTEAFKPLGIsDWNSLFW-IAHPGGPAILDQVEAKLALKPEKLRATrhvLS 332
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489928855 271 RHGNTSAASVPCALDEaVRDGRIKAGqlilLEAFGGGFTWG 311
Cdd:PLN03173 333 EYGNMSSACVLFILDE-MRKKSAEDG----LKSTGEGLEWG 368
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
206-316 |
1.57e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 39.96 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 206 TMAGNEVFKVAVTelAHIVDETLeannldrsALDWLVPHQANLRIISATAKKLGMS---MDNVVVTLDRHGNTSAASVPC 282
Cdd:PLN02192 377 TLVGKKLFKMKLK--PYIPDFKL--------AFEHFCIHAGGRAVLDELEKNLQLSdwhMEPSRMTLYRFGNTSSSSLWY 446
|
90 100 110
....*....|....*....|....*....|....
gi 489928855 283 ALDEAVRDGRIKAGQLILLEAFGGGFTWGSALVR 316
Cdd:PLN02192 447 ELAYSEAKGRIKKGDRTWQIAFGSGFKCNSAVWK 480
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
90-166 |
1.83e-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: 39.16 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 90 AACQIQSMLGIKGcPAFDVAAACAGFTYALSVADQYVKSGAVKHALVVGSDVLA--------------------RTCDPT 149
Cdd:pfam00109 152 IAGRISYFLGLRG-PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLtplgfagfsaagmlspdgpcKAFDPF 230
|
90
....*....|....*..
gi 489928855 150 DRGTiiIFGDGAGAVVL 166
Cdd:pfam00109 231 ADGF--VRGEGVGAVVL 245
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
62-138 |
2.38e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 39.11 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 62 AIEMAGIDKEQIGLIVVATTS----STHAFPSAAcqIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKHALVV 137
Cdd:PRK06064 33 ALEDAGIDGKDIDAMYVGNMSaglfVSQEHIAAL--IADYAGLAPIPATRVEAACASGGAALRQAYLAVASGEADVVLAA 110
|
.
gi 489928855 138 G 138
Cdd:PRK06064 111 G 111
|
|
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
51-311 |
2.77e-03 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 39.27 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 51 VATMGFAAANRAIEMAGIDKEQIGLIVVATTSSTHaFPSAACQIQSMLGIKGCPA--FDVAAACAGFTYALSVADQYVKS 128
Cdd:PLN03172 102 VPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLKPSVKrfMMYQQGCFAGGTVLRLAKDLAEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 129 GAVKHALVVGSDVLARTC-DPTDR--GTII---IFGDGAGAVVLSASEEPGILSTHLhadgrygELLTLPNADRVNPENP 202
Cdd:PLN03172 181 NAGSRVLVVCSEITAVTFrGPSDThlDSLVgqaLFGDGAAAVIIGADPDTKIERPLF-------EIVSAAQTILPDSDGA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489928855 203 I--HLTMAGnEVFKVaVTELAHIVDETLEANNL---------DRSALDWlVPHQANLRIISATAKKLGMSMDNVVVT--- 268
Cdd:PLN03172 254 IdgHLREVG-LTFHL-LKDVPGLISKNIEKSLVeafapiginDWNSIFW-IAHPGGPAILDQVEIKLDLKEEKLRATrhv 330
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489928855 269 LDRHGNTSAASVPCALDEaVRDGRIKAGQlillEAFGGGFTWG 311
Cdd:PLN03172 331 LSDYGNMSSACVLFILDE-MRKKSIEEGK----GSTGEGLEWG 368
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
244-316 |
6.59e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 38.01 E-value: 6.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489928855 244 HQANLRIISATAKKLGMS---MDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKAGQLILLEAFGGGFTWGSALVR 316
Cdd:PLN02854 417 HAGGRAVLDELQKNLQLSdwhMEPSRMTLHRFGNTSSSSLWYELAYTEAKGRVSAGDRVWQIAFGSGFKCNSAVWK 492
|
|
| |
