|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-385 |
1.66e-162 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 461.23 E-value: 1.66e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 1 MTFWLNDLGIVSAMGKGVEDTiisLNNLQNNEAPQLlKTKDLSTEGLPFYIG---HVDCVPLNQK-HRIDT----LIDIA 72
Cdd:PRK09185 2 TPVYISAFGATSALGRGLDAI---LAALRAGRASGM-RPCDFWLVDLPTWVGevvGVELPALPAAlAAFDCrnnrLALLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 73 LEQISPTLK----RFSHidkSRIAVVVGTSTSGVHDGEQA-RAEHDSSGVWPSDFLYADQELATPSHYIAEKVGALGPCY 147
Cdd:PRK09185 78 LQQIEPAVEaaiaRYGA---DRIGVVLGTSTSGILEGELAyRRRDPAHGALPADYHYAQQELGSLADFLRAYLGLSGPAY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 148 SISTACTSSAKALISAKALITADLADVVICGGVDSLCKLTINGFNALASMSTGMCKPFCDDRDGINIGEGAALFVMSKEA 227
Cdd:PRK09185 155 TISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLSPQPCRPFSANRDGINIGEAAAFFLLERED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 228 PLEngVMFLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNNTPLS 307
Cdd:PRK09185 235 DAA--VALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDGVPCS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 308 SSKYLTGHTLGAAGAIEAGICWLLLRGRgnitLP---FNKCTHRNKLADVNVIEQASTVKLNYCLSNSFAFGGNNASLIL 384
Cdd:PRK09185 313 STKGLTGHTLGAAGAVEAAICWLALRHG----LPphgWNTGQPDPALPPLYLVENAQALAIRYVLSNSFAFGGNNCSLIF 388
|
.
gi 2525019225 385 G 385
Cdd:PRK09185 389 G 389
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
8-384 |
1.49e-111 |
|
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: 332.20 E-value: 1.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 8 LGIVSAMGKGVEDTiisLNNLQNNEAPQLLKTKDLSTEGLPFYIGHVDCVPLN------QKHRIDTLIDIALEQISPTLK 81
Cdd:cd00834 8 LGAVTPLGNGVEEF---WEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEdyldrkELRRMDRFAQFALAAAEEALA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 82 ----RFSHIDKSRIAVVVGTSTSGVHDGE-QARAEHDSSGVWPSDFLYADQELATPSHYIAEKVGALGPCYSISTACTSS 156
Cdd:cd00834 85 daglDPEELDPERIGVVIGSGIGGLATIEeAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 157 AKALISAKALITADLADVVICGGVDSLC-KLTINGFNALASMSTG------MCKPFCDDRDGINIGEGAALFVM-SKEAP 228
Cdd:cd00834 165 AHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRnddpekASRPFDKDRDGFVLGEGAGVLVLeSLEHA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 229 LENGVM----FLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGN-- 302
Cdd:cd00834 245 KARGAKiyaeILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGEha 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 303 -NTPLSSSKYLTGHTLGAAGAIEAGICWLLLRgRGNITLPFNkCTHRNKLADVNVI-EQASTVKLNYCLSNSFAFGGNNA 380
Cdd:cd00834 325 kKVPVSSTKSMTGHLLGAAGAVEAIATLLALR-DGVLPPTIN-LEEPDPECDLDYVpNEAREAPIRYALSNSFGFGGHNA 402
|
....
gi 2525019225 381 SLIL 384
Cdd:cd00834 403 SLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
83-385 |
2.11e-96 |
|
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: 293.54 E-value: 2.11e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 83 FSHIDKSRIAVVVGTSTSGVHDGEQARAEHDSSGV-WPSDFLYADQELATPSHYIAEKVGALGPCYSISTACTSSAKALI 161
Cdd:COG0304 90 LDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPrRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 162 SAKALITADLADVVICGGVDS-LCKLTINGFNALASMSTGM------CKPFCDDRDGINIGEGAALFVM-SKEAPLENGV 233
Cdd:COG0304 170 EAYRLIRRGRADVMIAGGAEAaITPLGLAGFDALGALSTRNddpekaSRPFDKDRDGFVLGEGAGVLVLeELEHAKARGA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 234 ----MFLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGN---NTPL 306
Cdd:COG0304 250 kiyaEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFGDhayKVPV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 307 SSSKYLTGHTLGAAGAIEAGICWLLLRgRG------NITLPFNKCthrnklaDVNVI-EQASTVKLNYCLSNSFAFGGNN 379
Cdd:COG0304 330 SSTKSMTGHLLGAAGAIEAIASVLALR-DGvipptiNLENPDPEC-------DLDYVpNEAREAKIDYALSNSFGFGGHN 401
|
....*.
gi 2525019225 380 ASLILG 385
Cdd:COG0304 402 ASLVFK 407
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
136-385 |
4.57e-73 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 233.53 E-value: 4.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 136 IAEKVGALGPCYSISTACTSSAKALISAKALITADLADVVICGGVDS-LCKLTINGFNALASMST------GMCKPFCDD 208
Cdd:TIGR03150 144 ISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAaITPLGIAGFAAMKALSTrnddpeKASRPFDKD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 209 RDGINIGEGAALFVM-SKEAPLENGVMFL----GGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGT 283
Cdd:TIGR03150 224 RDGFVMGEGAGVLVLeELEHAKARGAKIYaeivGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 284 ATIKNDEMEALAINSVFGN---NTPLSSSKYLTGHTLGAAGAIEAGICWLLLRgRG------NITLPFNKCthrnklaDV 354
Cdd:TIGR03150 304 STPLGDKAETKAIKKVFGDhayKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIR-DGivpptiNLDNPDPEC-------DL 375
|
250 260 270
....*....|....*....|....*....|..
gi 2525019225 355 NVI-EQASTVKLNYCLSNSFAFGGNNASLILG 385
Cdd:TIGR03150 376 DYVpNEAREAKIDYALSNSFGFGGTNASLVFK 407
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
236-325 |
5.87e-29 |
|
Beta-ketoacyl synthase, C-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.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 108.81 E-value: 5.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 236 LGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNNT-----PLSSSK 310
Cdd:pfam02801 5 KGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkqplAIGSVK 84
|
90
....*....|....*
gi 2525019225 311 YLTGHTLGAAGAIEA 325
Cdd:pfam02801 85 SNIGHLEGAAGAAGL 99
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
140-223 |
2.87e-06 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 48.48 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 140 VGALGPCYSIS--TACTSSAKALISA-KALITADlADVVICGGVdSLCkLTINGFNALASM----STGMCKPFCDDRDGI 212
Cdd:smart00825 82 VGVSSSDYSVTvdTACSSSLVALHLAcQSLRSGE-CDMALAGGV-NLI-LSPDTFVGLSRAgmlsPDGRCKTFDASADGY 158
|
90
....*....|.
gi 2525019225 213 NIGEGAALFVM 223
Cdd:smart00825 159 VRGEGVGVVVL 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-385 |
1.66e-162 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 461.23 E-value: 1.66e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 1 MTFWLNDLGIVSAMGKGVEDTiisLNNLQNNEAPQLlKTKDLSTEGLPFYIG---HVDCVPLNQK-HRIDT----LIDIA 72
Cdd:PRK09185 2 TPVYISAFGATSALGRGLDAI---LAALRAGRASGM-RPCDFWLVDLPTWVGevvGVELPALPAAlAAFDCrnnrLALLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 73 LEQISPTLK----RFSHidkSRIAVVVGTSTSGVHDGEQA-RAEHDSSGVWPSDFLYADQELATPSHYIAEKVGALGPCY 147
Cdd:PRK09185 78 LQQIEPAVEaaiaRYGA---DRIGVVLGTSTSGILEGELAyRRRDPAHGALPADYHYAQQELGSLADFLRAYLGLSGPAY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 148 SISTACTSSAKALISAKALITADLADVVICGGVDSLCKLTINGFNALASMSTGMCKPFCDDRDGINIGEGAALFVMSKEA 227
Cdd:PRK09185 155 TISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLSPQPCRPFSANRDGINIGEAAAFFLLERED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 228 PLEngVMFLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNNTPLS 307
Cdd:PRK09185 235 DAA--VALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDGVPCS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 308 SSKYLTGHTLGAAGAIEAGICWLLLRGRgnitLP---FNKCTHRNKLADVNVIEQASTVKLNYCLSNSFAFGGNNASLIL 384
Cdd:PRK09185 313 STKGLTGHTLGAAGAVEAAICWLALRHG----LPphgWNTGQPDPALPPLYLVENAQALAIRYVLSNSFAFGGNNCSLIF 388
|
.
gi 2525019225 385 G 385
Cdd:PRK09185 389 G 389
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
8-384 |
1.49e-111 |
|
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: 332.20 E-value: 1.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 8 LGIVSAMGKGVEDTiisLNNLQNNEAPQLLKTKDLSTEGLPFYIGHVDCVPLN------QKHRIDTLIDIALEQISPTLK 81
Cdd:cd00834 8 LGAVTPLGNGVEEF---WEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEdyldrkELRRMDRFAQFALAAAEEALA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 82 ----RFSHIDKSRIAVVVGTSTSGVHDGE-QARAEHDSSGVWPSDFLYADQELATPSHYIAEKVGALGPCYSISTACTSS 156
Cdd:cd00834 85 daglDPEELDPERIGVVIGSGIGGLATIEeAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 157 AKALISAKALITADLADVVICGGVDSLC-KLTINGFNALASMSTG------MCKPFCDDRDGINIGEGAALFVM-SKEAP 228
Cdd:cd00834 165 AHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRnddpekASRPFDKDRDGFVLGEGAGVLVLeSLEHA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 229 LENGVM----FLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGN-- 302
Cdd:cd00834 245 KARGAKiyaeILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGEha 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 303 -NTPLSSSKYLTGHTLGAAGAIEAGICWLLLRgRGNITLPFNkCTHRNKLADVNVI-EQASTVKLNYCLSNSFAFGGNNA 380
Cdd:cd00834 325 kKVPVSSTKSMTGHLLGAAGAVEAIATLLALR-DGVLPPTIN-LEEPDPECDLDYVpNEAREAPIRYALSNSFGFGGHNA 402
|
....
gi 2525019225 381 SLIL 384
Cdd:cd00834 403 SLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
83-385 |
2.11e-96 |
|
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: 293.54 E-value: 2.11e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 83 FSHIDKSRIAVVVGTSTSGVHDGEQARAEHDSSGV-WPSDFLYADQELATPSHYIAEKVGALGPCYSISTACTSSAKALI 161
Cdd:COG0304 90 LDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPrRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 162 SAKALITADLADVVICGGVDS-LCKLTINGFNALASMSTGM------CKPFCDDRDGINIGEGAALFVM-SKEAPLENGV 233
Cdd:COG0304 170 EAYRLIRRGRADVMIAGGAEAaITPLGLAGFDALGALSTRNddpekaSRPFDKDRDGFVLGEGAGVLVLeELEHAKARGA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 234 ----MFLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGN---NTPL 306
Cdd:COG0304 250 kiyaEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFGDhayKVPV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 307 SSSKYLTGHTLGAAGAIEAGICWLLLRgRG------NITLPFNKCthrnklaDVNVI-EQASTVKLNYCLSNSFAFGGNN 379
Cdd:COG0304 330 SSTKSMTGHLLGAAGAIEAIASVLALR-DGvipptiNLENPDPEC-------DLDYVpNEAREAKIDYALSNSFGFGGHN 401
|
....*.
gi 2525019225 380 ASLILG 385
Cdd:COG0304 402 ASLVFK 407
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
136-385 |
4.57e-73 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 233.53 E-value: 4.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 136 IAEKVGALGPCYSISTACTSSAKALISAKALITADLADVVICGGVDS-LCKLTINGFNALASMST------GMCKPFCDD 208
Cdd:TIGR03150 144 ISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAaITPLGIAGFAAMKALSTrnddpeKASRPFDKD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 209 RDGINIGEGAALFVM-SKEAPLENGVMFL----GGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGT 283
Cdd:TIGR03150 224 RDGFVMGEGAGVLVLeELEHAKARGAKIYaeivGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 284 ATIKNDEMEALAINSVFGN---NTPLSSSKYLTGHTLGAAGAIEAGICWLLLRgRG------NITLPFNKCthrnklaDV 354
Cdd:TIGR03150 304 STPLGDKAETKAIKKVFGDhayKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIR-DGivpptiNLDNPDPEC-------DL 375
|
250 260 270
....*....|....*....|....*....|..
gi 2525019225 355 NVI-EQASTVKLNYCLSNSFAFGGNNASLILG 385
Cdd:TIGR03150 376 DYVpNEAREAKIDYALSNSFGFGGTNASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
133-385 |
2.92e-66 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 215.81 E-value: 2.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 133 SHYIAEKVGALGPCYSISTACTSSAKALISAKALITADLADVVICGGVDS-LCKLTINGFNALASMST------GMCKPF 205
Cdd:PRK07314 142 AGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAaITPLGIAGFAAARALSTrnddpeRASRPF 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 206 CDDRDGINIGEGAALFVM-SKEAPLENGVM----FLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINA 280
Cdd:PRK07314 222 DKDRDGFVMGEGAGILVLeELEHAKARGAKiyaeVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 281 HGTATIKNDEMEALAINSVFGN---NTPLSSSKYLTGHTLGAAGAIEAGICWLLLRGRG-----NITLPFNKCthrnkla 352
Cdd:PRK07314 302 HGTSTPAGDKAETQAIKRVFGEhayKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVipptiNLDNPDEEC------- 374
|
250 260 270
....*....|....*....|....*....|....
gi 2525019225 353 DVNVI-EQASTVKLNYCLSNSFAFGGNNASLILG 385
Cdd:PRK07314 375 DLDYVpNEARERKIDYALSNSFGFGGTNASLVFK 408
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
84-385 |
1.16e-59 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 199.15 E-value: 1.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 84 SHIDKSRIAVVVGTSTSGVHDGEQARAEHDSSG---VWPsdFLYADQELATPSHYIAEKVGALGPCYSISTACTSSAKAL 160
Cdd:PTZ00050 98 SEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGhsrVSP--YFIPKILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 161 ISAKALITADLADVVICGGV-DSLCKLTINGFNALASMSTGM-------CKPFCDDRDGINIGEGAALFVM-SKEAPLEN 231
Cdd:PTZ00050 176 GEAFRWIKYGEADIMICGGTeASITPVSFAGFSRMRALCTKYnddpqraSRPFDKDRAGFVMGEGAGILVLeELEHALRR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 232 GVM----FLGGGESSDAHHISAPDPSGNGAKSAMKAALA-VADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNNTP- 305
Cdd:PTZ00050 256 GAKiyaeIRGYGSSSDAHHITAPHPDGRGARRCMENALKdGANININDVDYVNAHATSTPIGDKIELKAIKKVFGDSGAp 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 306 ---LSSSKYLTGHTLGAAGAIEAGICWLLLrgRGNITLPFNKCTHRNKLADVNVIE---QASTVKLNYCLSNSFAFGGNN 379
Cdd:PTZ00050 336 klyVSSTKGGLGHLLGAAGAVESIVTILSL--YEQIIPPTINLENPDAECDLNLVQgktAHPLQSIDAVLSTSFGFGGVN 413
|
....*.
gi 2525019225 380 ASLILG 385
Cdd:PTZ00050 414 TALLFT 419
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
136-384 |
2.90e-58 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 195.22 E-value: 2.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 136 IAEKVGALGPCYSISTACTSSAKALISAKALITADLADVVICGGVDS-LCKLTINGFNALASMSTGM-------CKPFCD 207
Cdd:PRK06333 156 VSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAaIDRVSLAGFAAARALSTRFndapeqaSRPFDR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 208 DRDGINIGEGAALFVM-SKEAPLENGVM----FLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHG 282
Cdd:PRK06333 236 DRDGFVMGEGAGILVIeTLEHALARGAPplaeLVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 283 TATIKNDEMEALAINSVFGN--NTPLSSSKYLTGHTLGAAGAIEAGICWLLLR-GRGNITLPFNKCTHRNKLADVnVIEQ 359
Cdd:PRK06333 316 TSTPVGDLGEVAAIKKVFGHvsGLAVSSTKSATGHLLGAAGGVEAIFTILALRdQIAPPTLNLENPDPAAEGLDV-VANK 394
|
250 260
....*....|....*....|....*
gi 2525019225 360 ASTVKLNYCLSNSFAFGGNNASLIL 384
Cdd:PRK06333 395 ARPMDMDYALSNGFGFGGVNASILF 419
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
8-385 |
2.18e-55 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 186.80 E-value: 2.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 8 LGIVSAMGKgVEDTIISLnnLQNNEAPQLLKTkdlSTEGLPFYIGHVDCVPLNQKHRIDTLIDIALE--QISPTLKRfsh 85
Cdd:PRK05952 9 IGLVSALGD-LEQSWQRL--LQGKSGIKLHQP---FPELPPLPLGLIGNQPSSLEDLTKTVVTAALKdaGLTPPLTD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 86 idksrIAVVVGTSTSGVHDGEQ-ARAEHDSSGVWPSDFLYAD--QEL-ATPSHYIAEKVGALGPCYSISTACTSSAKALI 161
Cdd:PRK05952 80 -----CGVVIGSSRGCQGQWEKlARQMYQGDDSPDEELDLENwlDTLpHQAAIAAARQIGTQGPVLAPMAACATGLWAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 162 SAKALITADLADVVICGGVDS-LCKLTINGFNALASMSTGMCKPFCDDRDGINIGEGAALFVM-SKEAPLENGV----MF 235
Cdd:PRK05952 155 QGVELIQTGQCQRVIAGAVEApITPLTLAGFQQMGALAKTGAYPFDRQREGLVLGEGGAILVLeSAELAQKRGAkiygQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 236 LGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNNTPLSSSKYLTGH 315
Cdd:PRK05952 235 LGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFPHRVAVSSTKGATGH 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525019225 316 TLGAAGAIEAGICWLLLRgrgNITLPfnKCTH-RNKLADVNVIEQASTVKLNYCLSNSFAFGGNNASLILG 385
Cdd:PRK05952 315 TLGASGALGVAFSLLALR---HQQLP--PCVGlQEPEFDLNFVRQAQQSPLQNVLCLSFGFGGQNAAIALG 380
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
144-383 |
1.77e-48 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 169.14 E-value: 1.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 144 GPCYSISTACTSSAKALISAKALITADLADVVICGGVDS-LCKLTINGFNALASMST------GMCKPFCDDRDGINIGE 216
Cdd:PRK08439 153 GPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESaICPVGIGGFAAMKALSTrnddpkKASRPFDKDRDGFVMGE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 217 GAALFVMSK-EAPLENGVM----FLGGGESSDAHHISAPDPsgNGAKSAMKAALAVADLLPsdIDYINAHGTATIKNDEM 291
Cdd:PRK08439 233 GAGALVLEEyESAKKRGAKiyaeIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKN 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 292 EALAINSVFGNNT---PLSSSKYLTGHTLGAAGAIEAGICWLLLRgRGNITLPFNKCThRNKLADVNVI-EQASTVKLNY 367
Cdd:PRK08439 309 ETAALKELFGSKEkvpPVSSTKGQIGHCLGAAGAIEAVISIMAMR-DGILPPTINQET-PDPECDLDYIpNVARKAELNV 386
|
250
....*....|....*.
gi 2525019225 368 CLSNSFAFGGNNASLI 383
Cdd:PRK08439 387 VMSNSFGFGGTNGVVI 402
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
136-385 |
2.82e-48 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 169.04 E-value: 2.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 136 IAEKVGALGPCYSISTACTSSAKALISAKALITADLADVVICGGVD-SLCKLTINGFNALASMST------GMCKPFCDD 208
Cdd:PRK06501 158 LADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDgSVSAEALIRFSLLSALSTqndppeKASKPFSKD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 209 RDGINIGEGAALFVM-SKEAPLENGVMFLG----GGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGT 283
Cdd:PRK06501 238 RDGFVMAEGAGALVLeSLESAVARGAKILGivagCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGT 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 284 ATIKNDEMEALAINSVFGN---NTPLSSSKYLTGHTLGAAGAIEAGICWLLLRgRGNI-----------TLPFnkcthrn 349
Cdd:PRK06501 318 STPENDKMEYLGLSAVFGErlaSIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQ-TGRLpptinydnpdpAIPL------- 389
|
250 260 270
....*....|....*....|....*....|....*.
gi 2525019225 350 klaDVnVIEQASTVKLNYCLSNSFAFGGNNASLILG 385
Cdd:PRK06501 390 ---DV-VPNVARDARVTAVLSNSFGFGGQNASLVLT 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
133-387 |
1.18e-47 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 167.66 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 133 SHYIAEKVGALGPCYSISTACTSSAKALISAKALITADLADVVICGGVD-SLCKLTINGFNALASMSTGM-------CKP 204
Cdd:PLN02836 164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTEsSIDALSIAGFSRSRALSTKFnscpteaSRP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 205 FCDDRDGINIGEGAALFVMSK-EAPLENGVMFL----GGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYIN 279
Cdd:PLN02836 244 FDCDRDGFVIGEGAGVLVLEElEHAKRRGAKIYaevrGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVN 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 280 AHGTATIKNDEMEALAINSVFGNNTP-----LSSSKYLTGHTLGAAGAIEAGICWLLLR-GRGNITLPFNKcthRNKLAD 353
Cdd:PLN02836 324 AHATSTPLGDAVEARAIKTVFSEHATsgglaFSSTKGATGHLLGAAGAVEAIFSVLAIHhGIAPPTLNLER---PDPIFD 400
|
250 260 270
....*....|....*....|....*....|....*.
gi 2525019225 354 VNVIEQASTVKLNY--CLSNSFAFGGNNASLILGTH 387
Cdd:PLN02836 401 DGFVPLTASKAMLIraALSNSFGFGGTNASLLFTSP 436
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
150-385 |
1.74e-45 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 161.31 E-value: 1.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 150 STACTSSAKALISAKALITADLADVVICGGVDSLCKLTINGFNALASMSTG------MCKPFCDDRDGINIGEGAALFVM 223
Cdd:PRK09116 161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRndapelTPRPFDANRDGLVIGEGAGTLVL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 224 SK-EAPLENGVMFL----GGGESSDAHHISAPDPSGNGAksAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINS 298
Cdd:PRK09116 241 EElEHAKARGATIYaeivGFGTNSDGAHVTQPQAETMQI--AMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 299 VFGNNTPLSSSKYLTGHTLGAAGAIEAGICWLLLR-GRGNITLpfNKCTHRNKLADVNVI-EQASTVKLNYCLSNSFAFG 376
Cdd:PRK09116 319 VFGARMPISSLKSYFGHTLGACGALEAWMSIEMMNeGWFAPTL--NLTQVDPACGALDYImGEAREIDTEYVMSNNFAFG 396
|
....*....
gi 2525019225 377 GNNASLILG 385
Cdd:PRK09116 397 GINTSLIFK 405
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
86-385 |
3.33e-44 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 157.97 E-value: 3.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 86 IDKSRIAVVVGTstsGVHDGEQARAEHDSsgvWPSDFLYADQELAT-------PSHYIAEKVGALGPCYSISTACTSSAK 158
Cdd:PRK07910 103 VDTNRLMVSIGT---GLGSAEELVFAYDD---MRARGLRAVSPLAVqmympngPAAAVGLERHAKAGVITPVSACASGSE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 159 ALISAKALITADLADVVICGGVDS-LCKLTINGFNAL-ASMST------GMCKPFCDDRDGINIGEGAALFVMSKE---- 226
Cdd:PRK07910 177 AIAQAWRQIVLGEADIAICGGVETrIEAVPIAGFAQMrIVMSTnnddpaGACRPFDKDRDGFVFGEGGALMVIETEehak 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 227 ---APLENGVMflGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNN 303
Cdd:PRK07910 257 argANILARIM--GASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNALGGH 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 304 TP-LSSSKYLTGHTLGAAGAIEAGICWLLLrgRGNITLPFNKCTHRNKLADVNVIE-QASTVKLNYCLSNSFAFGGNNAS 381
Cdd:PRK07910 335 RPaVYAPKSALGHSVGAVGAVESILTVLAL--RDGVIPPTLNLENLDPEIDLDVVAgEPRPGNYRYAINNSFGFGGHNVA 412
|
....
gi 2525019225 382 LILG 385
Cdd:PRK07910 413 LAFG 416
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
147-384 |
1.69e-41 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 150.59 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 147 YSISTACTSSAKALISAKALITADLADVVICGGVDSLCKLTINGFNALASMSTGM-------CKPFCDDRDGINIGEGAA 219
Cdd:PRK07967 156 YSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYndtpekaSRAYDANRDGFVIAGGGG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 220 LFVMSK-EAPLENGVMF----LGGGESSDAHHISAPdpSGNGAKSAMKAALAVADllpSDIDYINAHGTATIKNDEMEAL 294
Cdd:PRK07967 236 VVVVEElEHALARGAKIyaeiVGYGATSDGYDMVAP--SGEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVKELG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 295 AINSVFGNNTP-LSSSKYLTGHTLGAAGAIEAGICWLLLRGrGNITLPFNKCTHRNKLADVNVI-EQASTVKLNYCLSNS 372
Cdd:PRK07967 311 AIREVFGDKSPaISATKSLTGHSLGAAGVQEAIYSLLMMEH-GFIAPSANIEELDPQAAGMPIVtETTDNAELTTVMSNS 389
|
250
....*....|..
gi 2525019225 373 FAFGGNNASLIL 384
Cdd:PRK07967 390 FGFGGTNATLVF 401
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
86-388 |
6.28e-38 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 143.20 E-value: 6.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 86 IDKSRIAVVVGTSTSGV---HDGEQA-RAEHDSSGvwPSDFLYADQELAtpSHYIAEKVGALGPCYSISTACTSSAKALI 161
Cdd:PLN02787 224 LDKTKCGVLIGSAMGGMkvfNDAIEAlRISYRKMN--PFCVPFATTNMG--SAMLAMDLGWMGPNYSISTACATSNFCIL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 162 SAKALITADLADVVICGGVDS-LCKLTINGFNALASMS------TGMCKPFCDDRDGINIGEGAALFVM-----SKEAPL 229
Cdd:PLN02787 300 NAANHIIRGEADVMLCGGSDAaIIPIGLGGFVACRALSqrnddpTKASRPWDMNRDGFVMGEGAGVLLLeelehAKKRGA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 230 ENGVMFLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNNTPL--S 307
Cdd:PLN02787 380 NIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPELrvN 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 308 SSKYLTGHTLGAAGAIEAGICWLLLRG---RGNITLpfnkcTHRNKLADVNVI--EQASTVKLNYCLSNSFAFGGNNASL 382
Cdd:PLN02787 460 STKSMIGHLLGAAGAVEAIATVQAIRTgwvHPNINL-----ENPESGVDTKVLvgPKKERLDIKVALSNSFGFGGHNSSI 534
|
....*.
gi 2525019225 383 ILGTHN 388
Cdd:PLN02787 535 LFAPYK 540
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
86-384 |
1.46e-36 |
|
"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: 137.19 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 86 IDKSRIAVVVGTSTSG---VHDGEQARAEHDSSGVWPSDFLyadqELATPSHYIAEKV-GALGPCYSISTACTSSAKALI 161
Cdd:cd00828 95 VHPSEVGVVVGSGMGGlrfLRRGGKLDARAVNPYVSPKWML----SPNTVAGWVNILLlSSHGPIKTPVGACATALEALD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 162 SAKALITADLADVVICGGVDSLCKLTINGFNALASMST------GMCKPFCDDRDGINIGEGAALFV-MSKEAPLENGVM 234
Cdd:cd00828 171 LAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTaeeepeEMSRPFDETRDGFVEAEGAGVLVlERAELALARGAP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 235 FLG----GGESSDAHHISAPDPsGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVF---GNNTPLS 307
Cdd:cd00828 251 IYGrvagTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAgalGAPLPVT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 308 SSKYLTGHTLGAAGAIEAgICWLLLRGRGNITLPFNKcTHRNKLADVNVIEQAST---VKLNYCLSNSFAFGGNNASLIL 384
Cdd:cd00828 330 AQKALFGHSKGAAGALQL-IGALQSLEHGLIPPTANL-DDVDPDVEHLSVVGLSRdlnLKVRAALVNAFGFGGSNAALVL 407
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
86-384 |
2.38e-36 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 136.70 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 86 IDKSRIAVVVGTS------TSGVHDGEQARAEHdssgVWPSDFLYA-DQELATpshYIAEKVGALGPCYSISTACTSSAK 158
Cdd:PRK07103 100 VDPDRIGLVVGGSnlqqreQALVHETYRDRPAF----LRPSYGLSFmDTDLVG---LCSEQFGIRGEGFTVGGASASGQL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 159 ALISAKALITADLADVVIC-GGVDSLCKLTINGFNALASMSTG--------MCKPFCDDRDGINIGEG-AALFVMSKEAP 228
Cdd:PRK07103 173 AVIQAARLVQSGSVDACIAvGALMDLSYWECQALRSLGAMGSDrfadepeaACRPFDQDRDGFIYGEAcGAVVLESAESA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 229 LENGV----MFLGGGESSDAHhiSAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNNT 304
Cdd:PRK07103 253 RRRGArpyaKLLGWSMRLDAN--RGPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAALFASGLAHA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 305 PLSSSKYLTGHTLGAAGAIEAGICWLLLRGRG-----NITLPFNkcthrNKLADVNviEQASTVKLNYCLSNSFAFGGNN 379
Cdd:PRK07103 331 WINATKSLTGHGLSAAGIVELIATLLQMRAGFlhpsrNLDEPID-----ERFRWVG--STAESARIRYALSLSFGFGGIN 403
|
....*
gi 2525019225 380 ASLIL 384
Cdd:PRK07103 404 TALVL 408
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
89-384 |
5.62e-35 |
|
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: 131.22 E-value: 5.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 89 SRIAVVVGTsTSGVHDGEQARAEhdssGVWPSDFLYADQELATPSHY-IAEKVGALGPCYSISTACTSSAKALISAKALI 167
Cdd:cd00825 36 PIVGVVVGT-GGGSPRFQVFGAD----AMRAVGPYVVTKAMFPGASGqIATPLGIHGPAYDVSAACAGSLHALSLAADAV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 168 TADLADVVICGGVDSLCKL--TINGFNALASMSTGMCKPFCDDRDGINIGEGA-ALFVMSKEAPLENGVMFLGGGESSDA 244
Cdd:cd00825 111 QNGKQDIVLAGGSEELAAPmdCEFDAMGALSTPEKASRTFDAAADGFVFGDGAgALVVEELEHALARGAHIYAEIVGTAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 245 HHISA----PDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNNTPLSSS-KYLTGHTLGA 319
Cdd:cd00825 191 TIDGAgmgaFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDKSPAVSAtKAMTGNLSSA 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525019225 320 AGAIEagICWLLLRGRGNITLPFNKCTHRNKLADVNVIEqASTVKLNYCLSNSFAFGGNNASLIL 384
Cdd:cd00825 271 AVVLA--VDEAVLMLEHGFIPPSIHIEELDEAGLNIVTE-TTPRELRTALLNGFGLGGTNATLVL 332
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
78-384 |
2.21e-34 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 130.23 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 78 PTLKRFSHIDKS-RIAVVVGTSTSGVHDGEQARAEHDSSGvwP---SDFLYADQELATPSHYIAEKVGALGPCYSISTAC 153
Cdd:PRK14691 14 PSLTHADNTEKQeRTATIIGAGIGGFPAIAHAVRTSDSRG--PkrlSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTAC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 154 TSSAKALISAKALITADLADVVICGGVDSLC-KLTINGFNALASMSTGM-------CKPFCDDRDGINIGEGAALFVMSK 225
Cdd:PRK14691 92 AAGVQAIGDAVRMIRNNEADVALCGGAEAVIdTVSLAGFAAARALSTHFnstpekaSRPFDTARDGFVMGEGAGLLIIEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 226 -EAPLENGVM----FLGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVF 300
Cdd:PRK14691 172 lEHALARGAKplaeIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 301 G--NNTPLSSSKYLTGHTLGAAGAIEAGICWLLLRGRgNITLPFNKCTHRNKLADVNVIE-QASTVKLNYCLSNSFAFGG 377
Cdd:PRK14691 252 GesNALAITSTKSATGHLLGAAGGLETIFTVLALRDQ-IVPATLNLENPDPAAKGLNIIAgNAQPHDMTYALSNGFGFAG 330
|
....*..
gi 2525019225 378 NNASLIL 384
Cdd:PRK14691 331 VNASILL 337
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
72-384 |
2.40e-33 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 128.83 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 72 ALEQ--ISPtlkrfSHIDKSRIAVVVGTSTSgvhDGEQARAEHDSSgvwPSDFLYADQELATPSHYIAEKVGALGPCYSI 149
Cdd:cd00833 98 ALEDagYSP-----ESLAGSRTGVFVGASSS---DYLELLARDPDE---IDAYAATGTSRAFLANRISYFFDLRGPSLTV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 150 STACTSSAKALISA-KALITADlADVVICGGVDslCKLTINGFNALASMS----TGMCKPFCDDRDGINIGEG-AALFVM 223
Cdd:cd00833 167 DTACSSSLVALHLAcQSLRSGE-CDLALVGGVN--LILSPDMFVGFSKAGmlspDGRCRPFDADADGYVRGEGvGVVVLK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 224 SKEAPLENGVMFL----GGGESSDAH--HISAPdpSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAIN 297
Cdd:cd00833 244 RLSDALRDGDRIYavirGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 298 SVFGNNTP------LSSSKYLTGHTLGAAGAieAGI--CWLLLRgRGNI--TLPFNKCTHRNKLAD--VNVIEQASTVKL 365
Cdd:cd00833 322 KVFGGSRSadqpllIGSVKSNIGHLEAAAGL--AGLikVVLALE-HGVIppNLHFETPNPKIDFEEspLRVPTEARPWPA 398
|
330 340
....*....|....*....|...
gi 2525019225 366 NYCLS----NSFAFGGNNASLIL 384
Cdd:cd00833 399 PAGPRragvSSFGFGGTNAHVIL 421
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
87-384 |
3.36e-33 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 128.20 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 87 DKSRIAVVVGTSTSG---VHDGEQARAEHDSSGVWPsdFLYADQELATPSHYIAEKVGALGPCYSISTACTSSAKALISA 163
Cdd:PRK08722 97 NAHRIGVAIGSGIGGlglIEAGHQALVEKGPRKVSP--FFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 164 KALITADLADVVICGGVD-SLCKLTINGFNALASMST------GMCKPFCDDRDGINIGEGAALFVMSK--EAPLENGVM 234
Cdd:PRK08722 175 ARMIAYGDADAMVAGGAEkASTPLGMAGFGAAKALSTrndepqKASRPWDKDRDGFVLGDGAGMMVLEEyeHAKARGAKI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 235 F---LGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFG----NNTPLS 307
Cdd:PRK08722 255 YaelVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRALGeagsKQVLVS 334
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525019225 308 SSKYLTGHTLGAAGAIEAGICWLLLRGRgnITLPFNKCTHRNKLADVNVI-EQASTVK-LNYCLSNSFAFGGNNASLIL 384
Cdd:PRK08722 335 STKSMTGHLLGAAGSVEAIITVMSLVDQ--IVPPTINLDDPEEGLDIDLVpHTARKVEsMEYAICNSFGFGGTNGSLIF 411
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
236-325 |
5.87e-29 |
|
Beta-ketoacyl synthase, C-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.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 108.81 E-value: 5.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 236 LGGGESSDAHHISAPDPSGNGAKSAMKAALAVADLLPSDIDYINAHGTATIKNDEMEALAINSVFGNNT-----PLSSSK 310
Cdd:pfam02801 5 KGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkqplAIGSVK 84
|
90
....*....|....*
gi 2525019225 311 YLTGHTLGAAGAIEA 325
Cdd:pfam02801 85 SNIGHLEGAAGAAGL 99
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
72-327 |
2.13e-23 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 102.64 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 72 ALEQ--ISPtlkrfSHIDKSRIAVVVGTSTSG----VHDGEQARAEHDSSGVWPSdFLyadqelatpSHYIAEKVGALGP 145
Cdd:COG3321 102 ALEDagYDP-----ESLAGSRTGVFVGASSNDyallLLADPEAIDAYALTGNAKS-VL---------AGRISYKLDLRGP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 146 CYSISTACTSSAKALISA-KALITADlADVVICGGVDSLckLTINGFNALASM----STGMCKPFCDDRDGINIGEGAAL 220
Cdd:COG3321 167 SVTVDTACSSSLVAVHLAcQSLRSGE-CDLALAGGVNLM--LTPESFILFSKGgmlsPDGRCRAFDADADGYVRGEGVGV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 221 FVMsKeaPLengvmflgggesSDA----HHI------SA--PD--------PSGNGAKSAMKAALAVADLLPSDIDYINA 280
Cdd:COG3321 244 VVL-K--RL------------SDAlrdgDRIyavirgSAvnQDgrsngltaPNGPAQAAVIRRALADAGVDPATVDYVEA 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2525019225 281 HGTATIKNDEMEALAINSVFGNNTP------LSSSKylT--GHTLGAAGAieAGI 327
Cdd:COG3321 309 HGTGTPLGDPIEAAALTAAFGQGRPadqpcaIGSVK--SniGHLEAAAGV--AGL 359
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
123-384 |
1.94e-22 |
|
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: 95.20 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 123 LYADQELATPSHYIAEKVGAL-GPCYSISTACTSSAKALISAKALITADLADVVICGGVDSlckltingfnalasmstgm 201
Cdd:cd00327 37 TGGSGEFSGAAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 202 ckpfcddrdgINIGEGAA-LFVMSKEAPLENGVMFLGGGESSDAHHISA---PDPSGNGAKSAMKAALAVADLLPSDIDY 277
Cdd:cd00327 98 ----------FVFGDGAAaAVVESEEHALRRGAHPQAEIVSTAATFDGAsmvPAVSGEGLARAARKALEGAGLTPSDIDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 278 INAHGTATIKNDEMEALAINSVFGNNTPLSSS-KYLTGHTLGAAGAIEAGICWLLLRGRGNITLPfnkcthrnkladvnv 356
Cdd:cd00327 168 VEAHGTGTPIGDAVELALGLDPDGVRSPAVSAtLIMTGHPLGAAGLAILDELLLMLEHEFIPPTP--------------- 232
|
250 260
....*....|....*....|....*...
gi 2525019225 357 iEQASTVklnycLSNSFAFGGNNASLIL 384
Cdd:cd00327 233 -REPRTV-----LLLGFGLGGTNAAVVL 254
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
85-223 |
1.26e-14 |
|
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: 73.05 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 85 HIDKSRIAVVVGTSTSGVHDGEQARAEHDSSGVWPSDFLYADqelATPSHYIAEKVGALGPCYSISTACTSSAKALISAK 164
Cdd:pfam00109 108 SLDGSRTGVFIGSGIGDYAALLLLDEDGGPRRGSPFAVGTMP---SVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAV 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525019225 165 ALITADLADVVICGGVDSLckLTINGFNALASM----STGMCKPFCDDRDGINIGEGAALFVM 223
Cdd:pfam00109 185 QSIRSGEADVALAGGVNLL--LTPLGFAGFSAAgmlsPDGPCKAFDPFADGFVRGEGVGAVVL 245
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
144-322 |
2.26e-11 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 64.69 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 144 GPCYSISTACTSSAKALISAKALItADLADVVICGGVDS-LCKLTIngfnaLASMSTGMCK----------PFCDDRDGI 212
Cdd:cd00832 152 GPSGVVVAEQAGGLDALAQARRLV-RRGTPLVVSGGVDSaLCPWGW-----VAQLSSGRLStsddparaylPFDAAAAGY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 213 NIGEGAALFVMSKEAPLENGVMFLGGgesSDAHHISAPDP-----SGNGAKSAMKAALAVADLLPSDIDYINAHGTATIK 287
Cdd:cd00832 226 VPGEGGAILVLEDAAAARERGARVYG---EIAGYAATFDPppgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPE 302
|
170 180 190
....*....|....*....|....*....|....*.
gi 2525019225 288 NDEMEALAINSVFG-NNTPLSSSKYLTGHtLGAAGA 322
Cdd:cd00832 303 LDRAEAAALAAVFGpRGVPVTAPKTMTGR-LYAGGA 337
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
140-223 |
2.87e-06 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 48.48 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 140 VGALGPCYSIS--TACTSSAKALISA-KALITADlADVVICGGVdSLCkLTINGFNALASM----STGMCKPFCDDRDGI 212
Cdd:smart00825 82 VGVSSSDYSVTvdTACSSSLVALHLAcQSLRSGE-CDMALAGGV-NLI-LSPDTFVGLSRAgmlsPDGRCKTFDASADGY 158
|
90
....*....|.
gi 2525019225 213 NIGEGAALFVM 223
Cdd:smart00825 159 VRGEGVGVVVL 169
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
145-182 |
3.60e-05 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 45.44 E-value: 3.60e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2525019225 145 PCYSISTACTSSAKALISAKALITADLADVVICGGVDS 182
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVES 117
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
145-182 |
4.06e-05 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 45.16 E-value: 4.06e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2525019225 145 PCYSISTACTSSAKALISAKALITADLADVVICGGVDS 182
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVES 113
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
124-181 |
1.77e-04 |
|
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: 43.41 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525019225 124 YADQELATPSHYIAEKVGALG-PCYSISTACTSSAKALISAKALITADLADVVICGGVD 181
Cdd:cd00829 47 AGGRFQSFPGALIAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAE 105
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
155-278 |
2.36e-04 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 42.70 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525019225 155 SSAKALISAKALITADLADVVICGGVDSLCK-LTINGFNALASMSTGMCKpfcddrDGINIGEGA-ALFVMSKEAPLENG 232
Cdd:PRK06147 135 SGAVALAQARRLIAAGGCPRVLVAGVDSLLTgPTLAHYEARDRLLTSQNS------NGFIPGEAAaAVLLGRPAGGEAPG 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2525019225 233 VMFLGGGESSDAHHISAPD--PS-GNGAKSAMKAALAVADLLPSDIDYI 278
Cdd:PRK06147 209 LPLLGLGLGREPAPVGESEdlPLrGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
137-193 |
5.28e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 41.67 E-value: 5.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525019225 137 AEKVGALG-PCYSISTACTSSAKALISAKALITADLADVVICGGVDSLCKltinGFNA 193
Cdd:PRK06059 68 AQALGWNGaPVSSSYAACASGSQALQSARAQILAGLCDVALVVGADTTPK----GFFA 121
|
|
| |
