|
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: 575.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 1 MYTKILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVAT 80
Cdd:PRK09352 2 MYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 81 TSSTHAFPSAACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGDG 160
Cdd:PRK09352 82 TTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 161 AGAVLLGQSEEQGIISTHLHADGSYGELLTLPNADRVNPDNSIFLTMAGNEVFKVAVTELAHIVDETLSENNLERSALDW 240
Cdd:PRK09352 162 AGAVVLGASEEPGILSTHLGSDGSYGDLLYLPGGGSRGPASPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDIDW 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586954384 241 LVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTWGSALVRF 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: 516.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 1 MYTKILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVAT 80
Cdd:TIGR00747 1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 81 TSSTHAFPSAACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGDG 160
Cdd:TIGR00747 81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 161 AGAVLLGQSEEQG-IISTHLHADGSYGELLTLPNADRVNPDNSIFLTMAGNEVFKVAVTELAHIVDETLSENNLERSALD 239
Cdd:TIGR00747 161 AGAVVLGESEDPGgIISTHLGADGTQGEALYLPAGGRPTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDID 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586954384 240 WLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTWGSALVRF 317
Cdd:TIGR00747 241 WFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
1-317 |
2.45e-169 |
|
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: 472.67 E-value: 2.45e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 1 MYTKILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVAT 80
Cdd:COG0332 1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 81 TSSTHAFPSAACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGDG 160
Cdd:COG0332 81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 161 AGAVLLGQSEE-QGIISTHLHADGSYGELLTLPNADRVNPDNSI-----FLTMAGNEVFKVAVTELAHIVDETLSENNLE 234
Cdd:COG0332 161 AGAVVLEASEEgPGILGSVLGSDGSGADLLVVPAGGSRNPPSPVdegdhYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 235 RSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTWGSAL 314
Cdd:COG0332 241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320
|
...
gi 1586954384 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 |
9.76e-158 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 443.13 E-value: 9.76e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 2 YTKILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATT 81
Cdd:cd00830 1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 82 SSTHAFPSAACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGDGA 161
Cdd:cd00830 81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 162 GAVLLGQSEE-QGIISTHLHADGSYGELLTLPNADRVNPDNSI-----FLTMAGNEVFKVAVTELAHIVDETLSENNLER 235
Cdd:cd00830 161 GAVVLEATEEdPGILDSVLGSDGSGADLLTIPAGGSRSPFEDAeggdpYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 236 SALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTWGSALV 315
Cdd:cd00830 241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-316 |
4.69e-137 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 391.15 E-value: 4.69e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 1 MYTKILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVAT 80
Cdd:PRK12879 3 SYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 81 TSSTHAFPSAACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGDG 160
Cdd:PRK12879 83 TTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 161 AGAVLLGQSEEQ-GIISTHLHADGSYGELLTLPNA----DRVNPDNSIFLTMAGNEVFKVAVTELAHIVDETLSENNLER 235
Cdd:PRK12879 163 AGAVVLEATENEpGFIDYVLGTDGDGGDILYRTGLgttmDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGLTK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 236 SALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTWGSALV 315
Cdd:PRK12879 243 DDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLV 322
|
.
gi 1586954384 316 R 316
Cdd:PRK12879 323 K 323
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
3-317 |
7.06e-109 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 321.69 E-value: 7.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 3 TKILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTS 82
Cdd:PLN02326 48 SKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 83 STHAFPSAaCQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGDGAG 162
Cdd:PLN02326 128 PDDLFGSA-PQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGAG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 163 AVLL--GQSEEQGIISTHLHADGS---------YGELLTLPNADR-----VNPDNSIF--LTMAGNEVFKVAVTELAHIV 224
Cdd:PLN02326 207 AVVLqaCDDDEDGLLGFDMHSDGNghkhlhatfKGEDDDSSGGNTngvgdFPPKKASYscIQMNGKEVFKFAVRCVPQVI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 225 DETLSENNLERSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAF 304
Cdd:PLN02326 287 ESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAGF 366
|
330
....*....|...
gi 1586954384 305 GGGFTWGSALVRF 317
Cdd:PLN02326 367 GAGLTWGSAIVRW 379
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
1-317 |
3.18e-87 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 264.50 E-value: 3.18e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 1 MYTKILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVAT 80
Cdd:CHL00203 1 MGVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 81 TSSTHAFPSAAcQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGDG 160
Cdd:CHL00203 81 STPDDLFGSAS-QLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 161 AGAVLLGQSEEQGIISTHLHADGSYGELLTLPNADRVNPD---------NSIFLTMAGNEVFKVAVTELAHIVDETLSEN 231
Cdd:CHL00203 160 AGAAIIGASYENSILGFKLCTDGKLNSHLQLMNKPVNNQSfgttklpqgQYQSISMNGKEVYKFAVFQVPAVIIKCLNAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 232 NLERSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTWG 311
Cdd:CHL00203 240 NISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTWG 319
|
....*.
gi 1586954384 312 SALVRF 317
Cdd:CHL00203 320 AIVLKW 325
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
3-317 |
1.59e-79 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 244.63 E-value: 1.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 3 TKILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTS 82
Cdd:PRK05963 4 SRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLATST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 83 STHAFPSAACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAvKYALVIGADVLARTCNPEDRGTIIIFGDGAG 162
Cdd:PRK05963 84 PDHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQG-KPVLVVAANILSRRINMAERASAVLFADAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 163 AVLLGQSEEQ--GIISTHLHADGSYGELLTLPNADRVNPDNS------IFLTMA-GNEVFKVAVTELAHIVDETLSENNL 233
Cdd:PRK05963 163 AVVLAPSAKAnsGVLGSQLISDGSHYDLIKIPAGGSARPFAPerdaseFLMTMQdGRAVFTEAVRMMSGASQNVLASAAM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 234 ERSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTWGSA 313
Cdd:PRK05963 243 TPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAV 322
|
....
gi 1586954384 314 LVRF 317
Cdd:PRK05963 323 VMRV 326
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-315 |
4.06e-76 |
|
"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: 236.18 E-value: 4.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 5 ILGTGSFLPKQVRTNADLEKMVdtSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTSST 84
Cdd:cd00827 4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 85 HAFPSAACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVlARTCNPEDRGTIIIFGDGAGAV 164
Cdd:cd00827 82 DKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDI-ASYLLDEGSALEPTLGDGAAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 165 LLGQSEEQ---GIISTHLHADGSYG----ELLTLPNADRVNPDNSIFLTMA--GNEVFKVAVTELAHIVDETLsENNLER 235
Cdd:cd00827 161 LVSRNPGIlaaGIVSTHSTSDPGYDfspyPVMDGGYPKPCKLAYAIRLTAEpaGRAVFEAAHKLIAKVVRKAL-DRAGLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 236 SALDWLVPHQAN-LRIISATAKKLGMSMDNVVVT----LDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTW 310
Cdd:cd00827 240 EDIDYFVPHQPNgKKILEAVAKKLGGPPEKASQTrwilLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTA 319
|
....*
gi 1586954384 311 GSALV 315
Cdd:cd00827 320 EAFVL 324
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
2-317 |
3.75e-59 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 192.74 E-value: 3.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 2 YTKILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAApDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATT 81
Cdd:PRK07204 4 YISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVD-GETSSYMGAEAAKKAVEDAKLTLDDIDCIICASG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 82 SSTHAFPSAACQIQGMMGIK--GCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGD 159
Cdd:PRK07204 83 TIQQAIPCTASLIQEQLGLQhsGIPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILFGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 160 GAGAVLLGQSEEQG-IISTHL--HADGSY------GELLTLPNADRVNPDNSIFLTMAGNEVFKVAVTELAHIVDETLSE 230
Cdd:PRK07204 163 GAAAVVITKGDHSSrILASHMetYSSGAHlseirgGGTMIHPREYSEERKEDFLFDMNGRAIFKLSSKYLMKFIDKLLMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 231 NNLERSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTW 310
Cdd:PRK07204 243 AGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSI 322
|
....*..
gi 1586954384 311 GSALVRF 317
Cdd:PRK07204 323 GGILLEY 329
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
50-315 |
5.07e-58 |
|
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: 187.27 E-value: 5.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 50 TVSTMGYEAGLRALEMAGVDKDEIGLIIVATTSSTHAFPSAACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSG 129
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 130 AVKYALVIGADvlartcnpedrgtIIIFGDGAGAVLLGQSEE---------QGIISTHLHADGSYGElltlpnadrvnpd 200
Cdd:cd00327 86 KADIVLAGGSE-------------EFVFGDGAAAAVVESEEHalrrgahpqAEIVSTAATFDGASMV------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 201 nsifltmagnevFKVAVTELAHIVDETLSENNLERSALDWLVPHQANLRIISATAKKLGMSMD-----NVVVTLDRHGNT 275
Cdd:cd00327 140 ------------PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDgvrspAVSATLIMTGHP 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1586954384 276 SAASVPCAFDEAVRDGRIK-------RGQLVLLEAFGGGFTWGSALV 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 |
8.97e-57 |
|
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: 186.69 E-value: 8.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 51 VSTMGYEAGLRALEMAG----VDKDEIGLIIVATTSSTHAF---------------------PSAACQIQGMMGIKGcPA 105
Cdd:cd00825 11 VSILGFEAAERAIADAGlsreYQKNPIVGVVVGTGGGSPRFqvfgadamravgpyvvtkamfPGASGQIATPLGIHG-PA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 106 FDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPE------------------DRGTIIIFGDGAGAVLLG 167
Cdd:cd00825 90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEfdamgalstpekasrtfdAAADGFVFGDGAGALVVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 168 QSEEQ---------GIISTHLHADGSYGELltlpnadrvnpdnsifltmagnevFKVAVTELAHIVDETLSENNLERSAL 238
Cdd:cd00825 170 ELEHAlargahiyaEIVGTAATIDGAGMGA------------------------FAPSAEGLARAAKEALAVAGLTVWDI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 239 DWLVPHQANLRIISATAKKLGMSMD-----NVVVTLDRHGNTSAASVPCAFDEAVRDGRIK------------------- 294
Cdd:cd00825 226 DYLVAHGTGTPIGDVKELKLLRSEFgdkspAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGfippsihieeldeaglniv 305
|
330 340
....*....|....*....|....*..
gi 1586954384 295 ------RGQLVLLEAFGGGFTWGSALV 315
Cdd:cd00825 306 tettprELRTALLNGFGLGGTNATLVL 332
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
228-317 |
2.21e-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: 143.80 E-value: 2.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 228 LSENNLERSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGG 307
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 1586954384 308 FTWGSALVRF 317
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
5-316 |
4.11e-40 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 143.87 E-value: 4.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 5 ILGTGSFLPKQVRTNADL------------------------EKMVDTSDEWIVTRTGIRER----------------RI 44
Cdd:PRK07515 5 ISGTGLYTPPESISNEELvasfnayverfnaenaaaiaagevEALQPSSSEFIEKASGIKSRyvmdkegildpdrmrpRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 45 AA-PDETVST---MGYEAGLRALEMAGVDKDEIGLIIVATTSSTHAFPSAACQIQGMMGIKGCpAFDVAAACAGFTYALS 120
Cdd:PRK07515 85 PErSNDELSIqaeMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIEGF-AFDMNVACSSATFGIQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 121 IADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGDGAGAVLLGQSEEQG------IISTHLHADGS------YGel 188
Cdd:PRK07515 164 TAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATsaggfeILGTRLFTQFSnnirnnFG-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 189 lTLPNADRVNPDNSIFLTM-AGNEVFKVAVTELAHIVDETLSENNLERSALD--WLvpHQANLRIISATAKK-LG--MSM 262
Cdd:PRK07515 242 -FLNRADPEGIGARDKLFVqEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKrfWL--HQANINMNQLIGKKvLGrdATP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1586954384 263 DNVVVTLDRHGNTSAASVPCAFDEAVRDgrIKRGQLVLLEAFGGGFTWGSALVR 316
Cdd:PRK07515 319 EEAPVILDEYANTSSAGSIIAFHKHSDD--LAAGDLGVICSFGAGYSIGSVIVR 370
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
4-317 |
9.11e-40 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 142.80 E-value: 9.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 4 KILGTGSFLPKQVRTNADLEKMVDTSDEWIVTR----TGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVA 79
Cdd:PRK12880 9 KISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 80 TTSSTHAFPSAACQIQGMMGIK-GCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGaDVLARTCNPEDRGTIIIFG 158
Cdd:PRK12880 89 TQSPDFFMPSTACYLHQLLNLSsKTIAFDLGQACAGYLYGLFVAHSLIQSGLGKILLICG-DTLSKFIHPKNMNLAPIFG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 159 DGAGAVLLGQSEEQGIIsTHLHADGSYGELLTLPNADRVNPDNSIF----------------LTMAGNEVFKVAVTELAH 222
Cdd:PRK12880 168 DGVSATLIEKTDFNEAF-FELGSDGKYFDKLIIPKGAMRIPKADIFnddslmqteefrqlenLYMDGANIFNMALECEPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 223 IVDETLSENNLERSALDWLVPHQANLRIISATAKKLGMSMDNVV-VTLDRHGNTSAASVPCAFDEAVRDGRIKrgqlVLL 301
Cdd:PRK12880 247 SFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPnFIMEKYANLSACSLPALLCELDTPKEFK----ASL 322
|
330
....*....|....*.
gi 1586954384 302 EAFGGGFTWGSALVRF 317
Cdd:PRK12880 323 SAFGAGLSWGSAVLNF 338
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
5-316 |
9.74e-34 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 126.27 E-value: 9.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 5 ILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIvaTTSST 84
Cdd:PRK06840 7 IVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVI--YIGSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 85 HA-FP--SAACQIQGMMGIKGCPAFDVAAACAGFTYALSIA-DQYVKSGAVKYALVIGAdvlARTC------NPEDRgTI 154
Cdd:PRK06840 85 HKdYPvwSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAkDLLYSDPSIENVLLVGG---YRNSdlvdydNPRTR-FM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 155 IIFGDGAGAVLLG-QSEEQGIISTHLHADGSYGELLTLPNADRVNP------DNSIF-LTMAGNEVFK-----VAVTELA 221
Cdd:PRK06840 161 FNFAAGGSAALLKkDAGKNRILGSAIITDGSFSEDVRVPAGGTKQPaspetvENRQHyLDVIDPESMKerldeVSIPNFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 222 HIVDETLSENNLERSALDWLVP-------HQANLRiisatakKLGMSMDNVVVtLDRHGNTSAASVPCAFDEAVRDGRIK 294
Cdd:PRK06840 241 KVIREALRKSGYTPKDIDYLAIlhmkrsaHIALLE-------GLGLTEEQAIY-LDEYGHLGQLDQILSLHLALEQGKLK 312
|
330 340
....*....|....*....|..
gi 1586954384 295 RGQLVLLEAFGGGFTWGSALVR 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 |
8.37e-33 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 116.08 E-value: 8.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 106 FDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVLARTCNPEDRGTIIIFGDGAGAVLLGQSEEQG--IISTHLHADG 183
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEPGarILDSVLGSDG 80
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
5-307 |
6.84e-26 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 104.96 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 5 ILGTGSFLPKQVRTNADLEKMV-DTSD-----EWIVTR-TGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLII 77
Cdd:PRK09258 8 ILSLAYELAPVVVTSSEIEERLaPLYErlrlpPGQLEAlTGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGLLI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 78 VATTSSTHAFPSAACQIQGMMGI-KGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGAD--------VLARTCNP 148
Cdd:PRK09258 88 NTSVCRDYLEPATACRVHHNLGLpKSCANFDVSNACLGFLNGMLDAANMIELGQIDYALVVSGEsareiveaTIDRLLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 149 ED-RGTIIIF------GDGAGAVLLGQSEeqgiisthLHADG------------SYGElLTLPNADRVNPDnSIFLTMAG 209
Cdd:PRK09258 168 ETtREDFAQSfatltlGSGAAAAVLTRGS--------LHPRGhrllggvtraatEHHE-LCQGGRDGMRTD-AVGLLKEG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 210 nevfkvavTELAHIV-DETLSENNLERSALDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCAFDEAV 288
Cdd:PRK09258 238 --------VELAVDTwEAFLAQLGWAVEQVDRVICHQVGAAHTRAILKALGIDPEKVFTTFPTLGNMGPASLPITLAMAA 309
|
330
....*....|....*....
gi 1586954384 289 RDGRIKRGQLVLLEAFGGG 307
Cdd:PRK09258 310 EEGFLKPGDRVALLGIGSG 328
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
37-170 |
1.06e-25 |
|
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: 105.26 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 37 TGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTSSTHAFPSAACQIQGMMGI-KGCPAFDVAAACAGF 115
Cdd:COG3425 37 LGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGTESGPDASKPIATYVHGALGLpPNCRAFELKFACYAG 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586954384 116 TYALSIADQYVKSGAVKYALVIGADVlARTcnpeDRGTI--IIFGDGAGAVLLGQSE 170
Cdd:COG3425 117 TAALQAALGWVASGPNKKALVIASDI-ARY----GPGSAgeYTQGAGAVAMLVGADP 168
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
5-307 |
6.18e-24 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 99.98 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 5 ILGTGSFLPKQVRTNADLEKMVDTSDEWIVTRTGIRERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTSST 84
Cdd:PRK04262 5 IVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGSESHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 85 HAFPSAACQIQGMMGI-KGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVlARTcNPEDrgtIIIFGDGAGA 163
Cdd:PRK04262 85 YAVKPTATIVAEALGAtPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADT-AQG-APGD---ALEYTAAAGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 164 V--LLGQSEEQGIIsthlhaDGSYGelLTLPNADRVNPDNSIFlTMAGNEV------FKvavtelaHI---VDETLSENN 232
Cdd:PRK04262 160 AafIIGKEEVIAEI------EATYS--YTTDTPDFWRREGEPY-PRHGGRFtgepayFK-------HIisaAKGLMEKLG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586954384 233 LERSALDWLVPHQANLRIISATAKKLGMSMDNVVVTL--DRHGNTSAASVPCAFdEAVRDgRIKRGQLVLLEAFGGG 307
Cdd:PRK04262 224 LKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLltPYIGNTYSGSALLGL-AAVLD-VAKPGDRILVVSFGSG 298
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
41-309 |
7.21e-22 |
|
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: 94.21 E-value: 7.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 41 ERRIAAPDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTSSTHAfPSAACQIQGMMGIKGcpafDVAA------ACAG 114
Cdd:cd00831 75 DERNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPT-PSLDAMLINRLGLRP----DVKRynlggmGCSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 115 FTYALSIADQYVKSGAVKYALVIGADVLART-CNPEDRGTII---IFGDGAGAVLLGQSEEQGIISTHL-HADGSYGELL 189
Cdd:cd00831 150 GAIALDLAKDLLEANPGARVLVVSTELCSLWyRGPDHRSMLVgnaLFGDGAAAVLLSNDPRDRRRERPLfELVRAASTLL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 190 tlpnadrvnPDNsifltmAGNEVFKVAVTELAHIVDE---TLSENNLERSALDWLVPHQANL---------------RII 251
Cdd:cd00831 230 ---------PDS------EDAMGWHLGEEGLTFVLSRdvpRLVEKNLERVLRKLLARLGIGLfklafdhwcvhpggrAVL 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586954384 252 SATAKKLGMSMDNVVV---TLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFT 309
Cdd:cd00831 295 DAVEKALGLSPEDLEAsrmVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFT 355
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
3-317 |
8.66e-21 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 90.97 E-value: 8.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 3 TKILGTGSFLPKQVRTNADLEKMVDTSDEW----------IVTRTGIRERRIAAPDETVST-----------------MG 55
Cdd:COG3424 2 ARILSIATAVPPHRYTQEEIAEFAAELFGLderdrrrlrrLFENSGIETRHSVLPLEWYLEppsfgernalyieealeLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 56 YEAGLRALEMAGVDKDEIGLIIvaTTSSThafpsaacqiqGMMgikgCPAFDVAAA------------------CAGFTY 117
Cdd:COG3424 82 EEAARRALDKAGLDPEDIDHLV--TVSCT-----------GFA----APGLDARLInrlglrpdvrrlpvggmgCAAGAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 118 ALSIADQYVKSGAVKYALVIGADVLARTCNPED--RGTII---IFGDGAGAVLLGQSEEQGIiSTHLHADGSYgellTLP 192
Cdd:COG3424 145 GLRRAADFLRADPDAVVLVVCVELCSLTFQRDDdsKDNLVanaLFGDGAAAVVVSGDPRPGP-GPRILAFRSY----LIP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 193 NADRVnpdnsifltMA---GNEVFKV--------AVTE-LAHIVDETLSENNLERSALDWLVPHQANLRIISATAKKLGM 260
Cdd:COG3424 220 DTEDV---------MGwdvGDTGFRMvlspevpdLIAEhLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGL 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 261 SMDNVVVT---LDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLLEAFGGGFTWGSALVRF 317
Cdd:COG3424 291 PPEALAHSrevLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGFTAELVLLRW 350
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
5-301 |
9.38e-15 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 74.18 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 5 ILGTGSFLPKQVRTNADLEK---MVD----TSDEWIVTRTGIRERRIAAPDETVST-----MGYEAGLRALEMAGVDKDE 72
Cdd:PRK06816 5 ITSTGAFLPGEPVSNDEMEAylgLINgkpsRARRIILRNNGIKTRHYALDPEGRPThsnaqMAAEAIRDLLDDAGFSLGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 73 IGLIIVATTSSTHAFPSAACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVL-----ARTCN 147
Cdd:PRK06816 85 IELLACGTSQPDQLMPGHASMVHGELGAPPIEVVSSAGVCAAGMMALKYAYLSVKAGESRNAVATASELAsrwfrASRFE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 148 PE-------DRGTIIIF---------GDGAGAVLL-GQSEEQGI--------ISTHLH-------------ADGSYGELL 189
Cdd:PRK06816 165 AEeeklaelEENPEIAFekdflrwmlSDGAGAVLLeNKPRPDGLslridwidLRSYAGelpvcmyagaeknEDGSLKGWS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 190 TLPNADRVNpdNSIF--------LtmagNEVFKVAVTE-LAHIVDetlsENNLERSALDWLVPHQANLRIISATA---KK 257
Cdd:PRK06816 245 DYPPEEAEA--ASALslkqdvrlL----NENIVVYTIKpLLELVD----KRNLDPDDIDYFLPHYSSEYFREKIVellAK 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1586954384 258 LGMSM--DNVVVTLDRHGNTSAASVPCAFDEAVRDGRIKRGQLVLL 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 |
8.89e-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: 59.20 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 47 PDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTSS--THAFPSAacQIQGMMGIKGCPAFDVAAACAGFTYALSIADQ 124
Cdd:cd00829 12 SDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGgrFQSFPGA--LIAEYLGLLGKPATRVEAAGASGSAAVRAAAA 89
|
90
....*....|....*.
gi 1586954384 125 YVKSGAVKYALVIGAD 140
Cdd:cd00829 90 AIASGLADVVLVVGAE 105
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
48-140 |
1.13e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 46.38 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 48 DETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTS--STHAFPsaACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQY 125
Cdd:PRK12578 18 DVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAyrGIELYP--APIVAEYSGLTGKVPLRVEAMCATGLAASLTAYTA 95
|
90
....*....|....*
gi 1586954384 126 VKSGAVKYALVIGAD 140
Cdd:PRK12578 96 VASGLVDMAIAVGVD 110
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
41-166 |
1.50e-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: 46.24 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 41 ERRIAAPDETVSTMGYEAGLRALEMAG-----VDKDEIGLIIVATTSSTHAF----------------P---------SA 90
Cdd:COG0304 61 DRKELRRMDRFTQYALAAAREALADAGldldeVDPDRTGVIIGSGIGGLDTLeeayrallekgprrvsPffvpmmmpnMA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 91 ACQIQGMMGIKGcPAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGAD---------------VL-------ARTCNP 148
Cdd:COG0304 141 AGHVSIRFGLKG-PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEaaitplglagfdalgALstrnddpEKASRP 219
|
170 180
....*....|....*....|.
gi 1586954384 149 EDR---GTIIifGDGAGAVLL 166
Cdd:COG0304 220 FDKdrdGFVL--GEGAGVLVL 238
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
57-139 |
4.42e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 44.50 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 57 EAGLRALEMAGVDKDEIGLIIVATTS----STHAFPSAAcqIQGMMGIKGCPAFDVAAACAGFTYALSIADQYVKSGAVK 132
Cdd:PRK06064 28 EAGLEALEDAGIDGKDIDAMYVGNMSaglfVSQEHIAAL--IADYAGLAPIPATRVEAACASGGAALRQAYLAVASGEAD 105
|
....*..
gi 1586954384 133 YALVIGA 139
Cdd:PRK06064 106 VVLAAGV 112
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
189-316 |
6.87e-05 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 44.19 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 189 LTLPNADRVnpdnSIFLTMAGNEVFKVAVTelAHIVDETLsennlersALDWLVPHQANLRIISATAKKLGMS---MDNV 265
Cdd:PLN02192 364 LVLPMSEQL----LFFATLVGKKLFKMKLK--PYIPDFKL--------AFEHFCIHAGGRAVLDELEKNLQLSdwhMEPS 429
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1586954384 266 VVTLDRHGNTSAASV--PCAFDEAvrDGRIKRGQLVLLEAFGGGFTWGSALVR 316
Cdd:PLN02192 430 RMTLYRFGNTSSSSLwyELAYSEA--KGRIKKGDRTWQIAFGSGFKCNSAVWK 480
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
54-166 |
1.82e-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: 42.91 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 54 MGYEAGLRALEMAG-----VDKDEIGLIIVATTSSTHAFP-------------------------SAACQIQGMMGIKGc 103
Cdd:cd00834 74 FALAAAEEALADAGldpeeLDPERIGVVIGSGIGGLATIEeayrallekgprrvspffvpmalpnMAAGQVAIRLGLRG- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 104 PAFDVAAACAGFTYALSIADQYVKSGAVKYALVIGADVL----------------------ARTCNPEDR---GtiIIFG 158
Cdd:cd00834 153 PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALitpltlagfaalralstrnddpEKASRPFDKdrdG--FVLG 230
|
....*...
gi 1586954384 159 DGAGAVLL 166
Cdd:cd00834 231 EGAGVLVL 238
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
47-174 |
2.98e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 42.24 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 47 PDETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTS---STHAFPSAACqIQGMMGIKGCPAFDVAAACAGFTYALSIAD 123
Cdd:PRK07516 18 DAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNagfSPQDFPASLV-LQADPALRFKPATRVENACATGSAAVYAAL 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1586954384 124 QYVKSGAVKYALVIGADVLARTCNPEdrgtiiifgdgAGAVLLGQS---EEQGI 174
Cdd:PRK07516 97 DAIEAGRARIVLVVGAEKMTATPTAE-----------VGDILLGASylkEEGDT 139
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
54-138 |
3.01e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 42.19 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 54 MGYEAGLRALEMAGVDKDEI-----GLIIVATTSSTHAFPSAacqiqGMMGIkgcPAFDVAAACAGFTYALSIADQYVKS 128
Cdd:PRK08256 25 MAAEAGRAALADAGIDYDAVqqayvGYVYGDSTSGQRALYEV-----GMTGI---PIVNVNNNCSTGSTALFLARQAVRS 96
|
90
....*....|
gi 1586954384 129 GAVKYALVIG 138
Cdd:PRK08256 97 GAADCALALG 106
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
63-316 |
9.83e-04 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 40.71 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 63 LEMAGVDKDEIGLIIVaTTSSTHAFPSAACQIQGMMGIK-GCPAFDVAA-ACAGFTYALSIADQYVKSGAVKYALVIGAD 140
Cdd:PLN02854 200 FSKTGVKPRDIGILIV-NCSLFNPTPSLSAMIVNHYKLRtDIKSYNLGGmGCSAGLISIDLANDLLKANPNSYAVVVSTE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 141 VLarTCN---PEDRGTII---IFGDGAGAVLL-------GQSEEQ--GIISTHLHADGSYGELLTLPNADRVNPDNSI-- 203
Cdd:PLN02854 279 NI--TLNwyfGNDRSMLLcncIFRMGGAAVLLsnkardrKRSKYQlvHTVRTHKGADDKNYNCVYQREDDKGTIGVSLar 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 204 -FLTMAGnEVFKVAVTELAHIV---DE------TLSENNLERSALDWLVP-----------HQANLRIISATAKKLGMS- 261
Cdd:PLN02854 357 eLMAVAG-DALKTNITTLGPLVlplSEqfmffvTLVRRKLLKAKVKPYIPdfklafehfciHAGGRAVLDELQKNLQLSd 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586954384 262 --MDNVVVTLDRHGNTSAASV--PCAFDEAvrDGRIKRGQLVLLEAFGGGFTWGSALVR 316
Cdd:PLN02854 436 whMEPSRMTLHRFGNTSSSSLwyELAYTEA--KGRVSAGDRVWQIAFGSGFKCNSAVWK 492
|
|
| PLN00415 |
PLN00415 |
3-ketoacyl-CoA synthase |
67-316 |
1.38e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 177808 Cd Length: 466 Bit Score: 40.06 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 67 GVDKDEIGLIIVaTTSSTHAFPSAACQIQGMMGIK-GCPAFDVAA-ACAGFTYALSIADQYVKSGAVKYALVIGADVLAR 144
Cdd:PLN00415 150 GIEPREVGIFIV-NCSLFNPNPSLSSMIVNRYKLKtDVKTYNLSGmGCSAGAISVDLATNLLKANPNTYAVIVSTENMTL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 145 TC-NPEDRGTII---IFGDGAGAVLLGQSEEQGIIS----THL--HADGSYGELLTLPNADR-----VNPDNSIFLTMAG 209
Cdd:PLN00415 229 SMyRGNDRSMLVpncLFRVGGAAVMLSNRSQDRVRSkyelTHIvrTHKGSSDKHYTCAEQKEdskgiVGVALSKELTVVA 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 210 NEVFKVAVTELAHIV---DETLS------ENNLERSALDWLVP-----------HQANLRIISATAKKLGMS---MDNVV 266
Cdd:PLN00415 309 GDTLKTNLTALGPLVlplSEKLRfilflvKSKLFRLKVSPYVPdfklcfkhfciHAGGRALLDAVEKGLGLSefdLEPSR 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1586954384 267 VTLDRHGNTSAASV--PCAFDEAvrDGRIKRGQLVLLEAFGGGFTWGSALVR 316
Cdd:PLN00415 389 MTLHRFGNTSSSSLwyELAYVEA--KCRVKRGDRVWQLAFGSGFKCNSIVWR 438
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
49-140 |
3.70e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 38.59 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 49 ETVSTMGYEAGLRALEMAGVDKDEIGLIIVATTSStHAFPS--AACQIQGMMGIKGCPAFDVAAACAGFTYALSIADQYV 126
Cdd:PRK06059 21 RDFVEYGVVAARAALADAGLDWRDVQLVVGADTIR-NGYPGfvAGATFAQALGWNGAPVSSSYAACASGSQALQSARAQI 99
|
90
....*....|....
gi 1586954384 127 KSGAVKYALVIGAD 140
Cdd:PRK06059 100 LAGLCDVALVVGAD 113
|
|
| PLN02377 |
PLN02377 |
3-ketoacyl-CoA synthase |
237-314 |
9.11e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 166018 Cd Length: 502 Bit Score: 37.69 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586954384 237 ALDWLVPHQANLRIISATAKKLGMSMDNVV---VTLDRHGNTSAASV--PCAFDEAvrDGRIKRGQLVLLEAFGGGFTWG 311
Cdd:PLN02377 394 AFDHFCIHAGGRAVIDELEKNLQLLPVHVEasrMTLHRFGNTSSSSIwyELAYIEA--KGRMRKGNRVWQIAFGSGFKCN 471
|
...
gi 1586954384 312 SAL 314
Cdd:PLN02377 472 SAV 474
|
|
| |
