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Conserved domains on  [gi|1235056357|gb|OZP68100|]
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beta-ketoacyl-ACP synthase II [Enterobacter asburiae]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase( domain architecture ID 11483566)

beta-ketoacyl-[acyl-carrier-protein] synthase is responsible for the elongation steps in fatty acid biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
2-406 0e+00

beta-ketoacyl-ACP synthase;


:

Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 856.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   2 TRRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVYDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRA 81
Cdd:PRK09116    1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  82 TELALEQAGLIGEAVLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPT 161
Cdd:PRK09116   81 SELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIPT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 162 SSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAGTLIL 241
Cdd:PRK09116  161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTLVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 242 EELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQATAAIY 321
Cdd:PRK09116  241 EELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 322 GDSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGALDYIMGEARQIDCEYLQSNNFAFGGINT 401
Cdd:PRK09116  321 GARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMSNNFAFGGINT 400


                  ....*
gi 1235056357 402 SIIIK 406
Cdd:PRK09116  401 SLIFK 405
 
Name Accession Description Interval E-value
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
2-406 0e+00

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 856.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   2 TRRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVYDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRA 81
Cdd:PRK09116    1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  82 TELALEQAGLIGEAVLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPT 161
Cdd:PRK09116   81 SELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIPT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 162 SSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAGTLIL 241
Cdd:PRK09116  161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTLVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 242 EELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQATAAIY 321
Cdd:PRK09116  241 EELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 322 GDSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGALDYIMGEARQIDCEYLQSNNFAFGGINT 401
Cdd:PRK09116  321 GARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMSNNFAFGGINT 400


                  ....*
gi 1235056357 402 SIIIK 406
Cdd:PRK09116  401 SLIFK 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 3-408 0e+00

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: 516.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVyDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRAT 82
Cdd:COG0304     1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDA-SGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  83 ELALEQAGLIGEAVlTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:COG0304    80 REALADAGLDLDEV-DPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAGTLIL 241
Cdd:COG0304   159 TACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 242 EELEHARARGATIYGEIVGFATNCDAAHITQPQRD--TMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQATAA 319
Cdd:COG0304   239 EELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDgeGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 320 IYGD---SVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCgALDYIMGEARQIDCEYLQSNNFAF 396
Cdd:COG0304   319 VFGDhayKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPEC-DLDYVPNEAREAKIDYALSNSFGF 397

                         410
                  ....*....|..
gi 1235056357 397 GGINTSIIIKRW 408
Cdd:COG0304   398 GGHNASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 3-405 2.10e-157

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: 449.68  E-value: 2.10e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVyDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRAT 82
Cdd:cd00834     1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDA-SGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  83 ELALEQAGLIGEAvLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:cd00834    80 EEALADAGLDPEE-LDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELC-PSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAGTLIL 241
Cdd:cd00834   159 TACASGAHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 242 EELEHARARGATIYGEIVGFATNCDAAHITQPQRD--TMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQATAA 319
Cdd:cd00834   239 ESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDgeGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 320 IYGDS---VPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGaLDYIMGEARQIDCEYLQSNNFAF 396
Cdd:cd00834   319 VFGEHakkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD-LDYVPNEAREAPIRYALSNSFGF 397


                  ....*....
gi 1235056357 397 GGINTSIII 405
Cdd:cd00834   398 GGHNASLVF 406
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 3-406 5.52e-116

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: 344.08  E-value: 5.52e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFG----ETWQSvsskLLAYENAVRKMPEWQVyDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMS 78
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGngveEFWEN----LLAGKSGIGPITRFDA-SDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  79 TRATELALEQAGLIGEAVLTNgQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRV 158
Cdd:TIGR03150  76 LAAAKEAVEDSGLDIEEEDAE-RVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 159 IPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAG 237
Cdd:TIGR03150 155 HAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAaITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 238 TLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRD--TMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQ 315
Cdd:TIGR03150 235 VLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEgeGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETK 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 316 ATAAIYGD---SVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCgALDYIMGEARQIDCEYLQSN 392
Cdd:TIGR03150 315 AIKKVFGDhayKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPEC-DLDYVPNEAREAKIDYALSN 393

                         410
                  ....*....|....
gi 1235056357 393 NFAFGGINTSIIIK 406
Cdd:TIGR03150 394 SFGFGGTNASLVFK 407
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 3-247 6.64e-31

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: 118.51  E-value: 6.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPE--WQVYD---------GLHTLLGAPIDDFTLPEHY----TRKR 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrWDPDKlydppsriaGKIYTKWGGLDDIFDFDPLffgiSPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  68 IRAMGRVSLMSTRATELALEQAGlIGEAVLTNGQTGIAYGSSTGSTGPVsefaTMLTEKHTNNITGTTYVQMMPHTTAVN 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAG-ITPDSLDGSRTGVFIGSGIGDYAAL----LLLDEDGGPRRGSPFAVGTMPSVIAGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 148 TGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSQrnDEPKTtpsPFDTQ 226
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSP--DGPCK---AFDPF 230

                         250       260
                  ....*....|....*....|.
gi 1235056357 227 RDGLVIGEGAGTLILEELEHA 247
Cdd:pfam00109 231 ADGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 147-405 2.33e-12

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: 66.97  E-value: 2.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  147 NTGLFFGLRGR----VIPTssACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSqrndepkttPS 221
Cdd:smart00825  77 RTGVFVGVSSSdysvTVDT--ACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLS---------PD 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  222 ----PFDTQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAH--ITQPQrdtmqicmeqslamaglsard 295
Cdd:smart00825 146 grckTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPS--------------------- 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  296 mgyisahgtatdrgdiAESQataaiygdsVPVSSLKSYFGHTLGACGAleawMSL----QMMREGWFAPTLNLTQP---- 367
Cdd:smart00825 205 ----------------GPAQ---------LLIGSVKSNIGHLEAAAGV----AGLikvvLALKHGVIPPTLHFETPnphi 255

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1235056357  368 DEQCGALdYIMGEARQIDCEYLQS----NNFAFGGINTSIII 405
Cdd:smart00825 256 DLEESPL-RVPTELTPWPPPGRPRragvSSFGFGGTNAHVIL 296
 
Name Accession Description Interval E-value
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
2-406 0e+00

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 856.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   2 TRRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVYDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRA 81
Cdd:PRK09116    1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  82 TELALEQAGLIGEAVLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPT 161
Cdd:PRK09116   81 SELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIPT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 162 SSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAGTLIL 241
Cdd:PRK09116  161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTLVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 242 EELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQATAAIY 321
Cdd:PRK09116  241 EELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 322 GDSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGALDYIMGEARQIDCEYLQSNNFAFGGINT 401
Cdd:PRK09116  321 GARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMSNNFAFGGINT 400


                  ....*
gi 1235056357 402 SIIIK 406
Cdd:PRK09116  401 SLIFK 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 3-408 0e+00

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: 516.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVyDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRAT 82
Cdd:COG0304     1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDA-SGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  83 ELALEQAGLIGEAVlTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:COG0304    80 REALADAGLDLDEV-DPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAGTLIL 241
Cdd:COG0304   159 TACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 242 EELEHARARGATIYGEIVGFATNCDAAHITQPQRD--TMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQATAA 319
Cdd:COG0304   239 EELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDgeGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 320 IYGD---SVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCgALDYIMGEARQIDCEYLQSNNFAF 396
Cdd:COG0304   319 VFGDhayKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPEC-DLDYVPNEAREAKIDYALSNSFGF 397

                         410
                  ....*....|..
gi 1235056357 397 GGINTSIIIKRW 408
Cdd:COG0304   398 GGHNASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 3-405 2.10e-157

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: 449.68  E-value: 2.10e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVyDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRAT 82
Cdd:cd00834     1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDA-SGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  83 ELALEQAGLIGEAvLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:cd00834    80 EEALADAGLDPEE-LDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELC-PSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAGTLIL 241
Cdd:cd00834   159 TACASGAHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 242 EELEHARARGATIYGEIVGFATNCDAAHITQPQRD--TMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQATAA 319
Cdd:cd00834   239 ESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDgeGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 320 IYGDS---VPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGaLDYIMGEARQIDCEYLQSNNFAF 396
Cdd:cd00834   319 VFGEHakkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD-LDYVPNEAREAPIRYALSNSFGF 397


                  ....*....
gi 1235056357 397 GGINTSIII 405
Cdd:cd00834   398 GGHNASLVF 406
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 3-406 5.52e-116

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: 344.08  E-value: 5.52e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFG----ETWQSvsskLLAYENAVRKMPEWQVyDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMS 78
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGngveEFWEN----LLAGKSGIGPITRFDA-SDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  79 TRATELALEQAGLIGEAVLTNgQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRV 158
Cdd:TIGR03150  76 LAAAKEAVEDSGLDIEEEDAE-RVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 159 IPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAG 237
Cdd:TIGR03150 155 HAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAaITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 238 TLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRD--TMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQ 315
Cdd:TIGR03150 235 VLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEgeGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETK 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 316 ATAAIYGD---SVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCgALDYIMGEARQIDCEYLQSN 392
Cdd:TIGR03150 315 AIKKVFGDhayKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPEC-DLDYVPNEAREAKIDYALSN 393

                         410
                  ....*....|....
gi 1235056357 393 NFAFGGINTSIIIK 406
Cdd:TIGR03150 394 SFGFGGTNASLVFK 407
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-409 6.42e-114

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 339.07  E-value: 6.42e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFG----ETWQSvsskLLAYENAVRKMPEWQVYDgLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMS 78
Cdd:PRK07314    2 RRVVVTGLGAVSPLGndveSTWKN----LLAGKSGIGPITHFDTSD-LAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  79 TRATELALEQAGLIGEAVLTNgQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRV 158
Cdd:PRK07314   77 IAAAKQAVEDAGLEITEENAD-RIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 159 IPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAG 237
Cdd:PRK07314  156 HSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAaITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 238 TLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTM--QICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQ 315
Cdd:PRK07314  236 ILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEgaARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQ 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 316 ATAAIYGDS---VPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCgALDYIMGEARQIDCEYLQSN 392
Cdd:PRK07314  316 AIKRVFGEHaykVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEEC-DLDYVPNEARERKIDYALSN 394

                         410
                  ....*....|....*..
gi 1235056357 393 NFAFGGINTSIIIKRWA 409
Cdd:PRK07314  395 SFGFGGTNASLVFKRYE 411
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-408 1.84e-94

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 289.59  E-value: 1.84e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   1 MTRRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEwQVYDGLHTLLGAPIDDFTL-------PEHY-TRKRIRAMG 72
Cdd:PRK06333    2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTD-FPVGDLATKIGGQVPDLAEdaeagfdPDRYlDPKDQRKMD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  73 RVSLMSTRATELALEQAGLIGEAVLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFF 152
Cdd:PRK06333   81 RFILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 153 GLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEelcpseAAV-------FDTLFATSQR-NDEPKTTPSPFD 224
Cdd:PRK06333  161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTE------AAIdrvslagFAAARALSTRfNDAPEQASRPFD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 225 TQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQI--CMEQSLAMAGLSARDMGYISAH 302
Cdd:PRK06333  235 RDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGArrAMLIALRQAGIPPEEVQHLNAH 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 303 GTATDRGDIAESQATAAIYGD--SVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGALDYIMGE 380
Cdd:PRK06333  315 ATSTPVGDLGEVAAIKKVFGHvsGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVANK 394

                         410       420
                  ....*....|....*....|....*...
gi 1235056357 381 ARQIDCEYLQSNNFAFGGINTSIIIKRW 408
Cdd:PRK06333  395 ARPMDMDYALSNGFGFGGVNASILFRRW 422
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 6-407 3.58e-88

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 273.49  E-value: 3.58e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   6 VITGMGgVTAfGETWqsvsSKLLAYENAVRKMPE--------WQVYDGLHTLLGA---PIDDFTLPEHYTRKRIRAMGRV 74
Cdd:PTZ00050    1 VVTPLG-VGA-ESTW----EALIAGKSGIRKLTEfpkflpdcIPEQKALENLVAAmpcQIAAEVDQSEFDPSDFAPTKRE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  75 S---LMSTRATELALEQAGLIGEAVLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLF 151
Cdd:PTZ00050   75 SratHFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 152 FGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQR-NDEPKTTPSPFDTQRDG 229
Cdd:PTZ00050  155 HKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEAsITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 230 LVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRD--TMQICMEQSLA-MAGLSARDMGYISAHGTAT 306
Cdd:PTZ00050  235 FVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDgrGARRCMENALKdGANININDVDYVNAHATST 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 307 DRGDIAESQATAAIYGDS----VPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCgALDYIMGEAR 382
Cdd:PTZ00050  315 PIGDKIELKAIKKVFGDSgapkLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEC-DLNLVQGKTA 393

                         410       420
                  ....*....|....*....|....*..
gi 1235056357 383 Q--IDCEYLQSNNFAFGGINTSIIIKR 407
Cdd:PTZ00050  394 HplQSIDAVLSTSFGFGGVNTALLFTK 420
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 3-407 4.49e-87

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 270.07  E-value: 4.49e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVYDglHTL-LGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRA 81
Cdd:PRK08439    2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASD--FPVqIAGEITDFDPTEVMDPKEVKKADRFIQLGLKA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  82 TELALEQAGLIGEAVLTNgQTGIAYGSSTGSTGPVSEFATMLTEKHTNNIT----GTTYVQMMPHTTAVNtglfFGLRGR 157
Cdd:PRK08439   80 AREAMKDAGFLPEELDAE-RFGVSSASGIGGLPNIEKNSIICFEKGPRKISpffiPSALVNMLGGFISIE----HGLKGP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 158 VIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGA 236
Cdd:PRK08439  155 NLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESaICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 237 GTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQICMEQSLAMAGLSARDmgYISAHGTATDRGDIAESQA 316
Cdd:PRK08439  235 GALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAGNPKID--YINAHGTSTPYNDKNETAA 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 317 TAAIYGDSV---PVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGaLDYIMGEARQIDCEYLQSNN 393
Cdd:PRK08439  313 LKELFGSKEkvpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECD-LDYIPNVARKAELNVVMSNS 391

                         410
                  ....*....|....
gi 1235056357 394 FAFGGINTSIIIKR 407
Cdd:PRK08439  392 FGFGGTNGVVIFKK 405
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
3-409 1.19e-80

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 253.83  E-value: 1.19e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEW-------QVYdglhtllGAPidDFTLPEHYTRKRIRAMGRVS 75
Cdd:PRK07967    2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFaemgmrsQVW-------GNV--KLDPTGLIDRKVMRFMGDAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  76 LMSTRATELALEQAGLIGEAVlTNGQTGIAYGSSTGSTGPVSEFA-TMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGL 154
Cdd:PRK07967   73 AYAYLAMEQAIADAGLSEEQV-SNPRTGLIAGSGGGSTRNQVEAAdAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 155 RGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFA-TSQRNDEPKTTPSPFDTQRDGLVIG 233
Cdd:PRK07967  152 KGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGAlSTKYNDTPEKASRAYDANRDGFVIA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 234 EGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQICMEQslAMAGLSArDMGYISAHGTATDRGDIAE 313
Cdd:PRK07967  232 GGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQM--ALATVDT-PIDYINTHGTSTPVGDVKE 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 314 SQATAAIYGDSVP-VSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGALDYIMGEARQIDCEYLQSN 392
Cdd:PRK07967  309 LGAIREVFGDKSPaISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSN 388

                         410
                  ....*....|....*..
gi 1235056357 393 NFAFGGINTSIIIKRWA 409
Cdd:PRK07967  389 SFGFGGTNATLVFRRYK 405
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
3-407 7.51e-78

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 246.84  E-value: 7.51e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVYDgLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRAT 82
Cdd:PRK08722    4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTN-FSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  83 ELALEQAGLigEAVLTNG-QTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPT 161
Cdd:PRK08722   83 IQALDDSGL--EVTEENAhRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 162 SSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELC-PSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGAGTLI 240
Cdd:PRK08722  161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKAStPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 241 LEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTM--QICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQATA 318
Cdd:PRK08722  241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSggALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 319 AIYG----DSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGaLDYIMGEARQID-CEYLQSNN 393
Cdd:PRK08722  321 RALGeagsKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLD-IDLVPHTARKVEsMEYAICNS 399

                         410
                  ....*....|....
gi 1235056357 394 FAFGGINTSIIIKR 407
Cdd:PRK08722  400 FGFGGTNGSLIFKK 413
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 2-404 3.35e-75

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 240.46  E-value: 3.35e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   2 TRRVVITGMGGVTAFG----ETWQsvssKLLAYENAVR-------KMPEWQVYDGLHTL------LGAPIDDFTLPEHYT 64
Cdd:PLN02836    5 TRRVVVTGLGLVTPLGcgveTTWR----RLIAGECGVRaltqddlKMKSEDEETQLYTLdqlpsrVAALVPRGTGPGDFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  65 RK---RIRAMGRVSLMSTRATELALEQAGLIGEAVLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMP 141
Cdd:PLN02836   81 EElwlNSRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 142 HTTAVNTGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQR-NDEPKTT 219
Cdd:PLN02836  161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESsIDALSIAGFSRSRALSTKfNSCPTEA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 220 PSPFDTQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQ--ICMEQSLAMAGLSARDMG 297
Cdd:PLN02836  241 SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGavLAMTRALQQSGLHPNQVD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 298 YISAHGTATDRGDIAESQATAAIYGD-----SVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCG 372
Cdd:PLN02836  321 YVNAHATSTPLGDAVEARAIKTVFSEhatsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFD 400

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1235056357 373 ALDYIMGEARQIDCEYLQSNNFAFGGINTSII 404
Cdd:PLN02836  401 DGFVPLTASKAMLIRAALSNSFGFGGTNASLL 432
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 3-404 6.14e-67

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 221.78  E-value: 6.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPEWQVYDgLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMSTRAT 82
Cdd:PLN02787  129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQ-FPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  83 ELALEQAGLIGEAV--LTNGQTGIAYGSSTGSTGPVSEFATMLTekhtnnitgTTYVQMMPH-----TTAVNTGLF---F 152
Cdd:PLN02787  208 KKALADGGITEDVMkeLDKTKCGVLIGSAMGGMKVFNDAIEALR---------ISYRKMNPFcvpfaTTNMGSAMLamdL 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 153 GLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLV 231
Cdd:PLN02787  279 GWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAaIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFV 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 232 IGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQI--CMEQSLAMAGLSARDMGYISAHGTATDRG 309
Cdd:PLN02787  359 MGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVilCIEKALAQSGVSKEDVNYINAHATSTKAG 438

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 310 DIAESQATAAIYGDS--VPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGALDYIMGEARQIDCE 387
Cdd:PLN02787  439 DLKEYQALMRCFGQNpeLRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIK 518

                         410
                  ....*....|....*..
gi 1235056357 388 YLQSNNFAFGGINTSII 404
Cdd:PLN02787  519 VALSNSFGFGGHNSSIL 535
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
5-407 4.85e-66

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 216.42  E-value: 4.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   5 VVITGMGGVTAFG----ETWQsvssKLLAYENAVRKMPEWQVyDGLHTLLGAPIDdfTLPEhytrKRIRAMGRVSLMSTR 80
Cdd:PRK06501   13 VAVTGMGVVTSLGqgkaDNWA----ALTAGESGIHTITRFPT-EGLRTRIAGTVD--FLPE----SPFGASALSEALARL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  81 ATELALEQAGlIGEAVLtNGQTGIAygsstgsTGPV-----SEFATMLTEKHTNnitGTTYVQMM------PHTTAVNTG 149
Cdd:PRK06501   82 AAEEALAQAG-IGKGDF-PGPLFLA-------APPVelewpARFALAAAVGDND---APSYDRLLraarggRFDALHERF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 150 LF----------FGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAV-FDTLFATSQRNDEPKT 218
Cdd:PRK06501  150 QFgsiadrladrFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIrFSLLSALSTQNDPPEK 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 219 TPSPFDTQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQI--CMEQSLAMAGLSARDM 296
Cdd:PRK06501  230 ASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAigAIRAALADAGLTPEQI 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 297 GYISAHGTATDRGDIAESQATAAIYGD---SVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCgA 373
Cdd:PRK06501  310 DYINAHGTSTPENDKMEYLGLSAVFGErlaSIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAI-P 388

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1235056357 374 LDYIMGEARQIDCEYLQSNNFAFGGINTSIIIKR 407
Cdd:PRK06501  389 LDVVPNVARDARVTAVLSNSFGFGGQNASLVLTA 422
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
5-408 5.97e-66

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 216.13  E-value: 5.97e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   5 VVITGMGGVTAFG----ETWQSvsskLLAYENAVRKMPEWQV--YDGLHTLLGAPIDDFTlpEHYTRKRIRAMGRVSLMS 78
Cdd:PRK07910   14 VVVTGIAMTTALAtdaeTTWKL----LLDGQSGIRTLDDPFVeeFDLPVRIGGHLLEEFD--HQLTRVELRRMSYLQRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  79 TRATELALEQAGliGEAVLTNgQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTyVQM-MPHTTAVNTGLFFGLRGR 157
Cdd:PRK07910   88 TVLGRRVWENAG--SPEVDTN-RLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLA-VQMyMPNGPAAAVGLERHAKAG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 158 VIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAE---ELCPseAAVFDTLFAT-SQRNDEPKTTPSPFDTQRDGLVIG 233
Cdd:PRK07910  164 VITPVSACASGSEAIAQAWRQIVLGEADIAICGGVEtriEAVP--IAGFAQMRIVmSTNNDDPAGACRPFDKDRDGFVFG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 234 EGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQI--CMEQSLAMAGLSARDMGYISAHGTATDRGDI 311
Cdd:PRK07910  242 EGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAghAMTRAIELAGLTPGDIDHVNAHATGTSVGDV 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 312 AESQATAAIYGDSVP-VSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGaLDYIMGEARQIDCEYLQ 390
Cdd:PRK07910  322 AEGKAINNALGGHRPaVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEID-LDVVAGEPRPGNYRYAI 400

                         410
                  ....*....|....*...
gi 1235056357 391 SNNFAFGGINTSIIIKRW 408
Cdd:PRK07910  401 NNSFGFGGHNVALAFGRY 418
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
4-407 5.63e-61

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 201.82  E-value: 5.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   4 RVVITGMGGVTAFG---ETWQsvssKLLAYENAVRKMpewQVYDGLHTLLGAPIDDFTLPEHYTRKRiramgrvslmstr 80
Cdd:PRK05952    3 KVVVTGIGLVSALGdleQSWQ----RLLQGKSGIKLH---QPFPELPPLPLGLIGNQPSSLEDLTKT------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  81 ATELALEQAGLigeaVLTNGQTGIAYGSSTGSTGpvsEFATMLTEKHTNNITGTT------YVQMMPHTTAVNTGLFFGL 154
Cdd:PRK05952   63 VVTAALKDAGL----TPPLTDCGVVIGSSRGCQG---QWEKLARQMYQGDDSPDEeldlenWLDTLPHQAAIAAARQIGT 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 155 RGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSqrndepKTTPSPFDTQRDGLVIG 233
Cdd:PRK05952  136 QGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEApITPLTLAGFQQMGALA------KTGAYPFDRQREGLVLG 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 234 EGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRD--TMQICMEQSLAMAGLSARDMGYISAHGTATDRGDI 311
Cdd:PRK05952  210 EGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDgkSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQ 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 312 AESQATAAIYGDSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQcgaLDYIMgEARQIDCEYLQS 391
Cdd:PRK05952  290 REANLIQALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFD---LNFVR-QAQQSPLQNVLC 365

                         410
                  ....*....|....*.
gi 1235056357 392 NNFAFGGINTSIIIKR 407
Cdd:PRK05952  366 LSFGFGGQNAAIALGK 381
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 3-405 5.84e-58

"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: 194.97  E-value: 5.84e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETW---QSVSSKLLAYENAVRKMPewQVYDGLHTLLGAPIDDFTLPEhYTRKRIRAMGRVSLMST 79
Cdd:cd00828     1 SRVVITGIGVVSPHGEGCdevEEFWEALREGRSGIAPVA--RLKSRFDRGVAGQIPTGDIPG-WDAKRTGIVDRTTLLAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  80 RATELALEQAGLIGEAVLTNGQTGIAYGSSTGSTGPVsEFATMLTEKHTNNITGTTyvqMMPHTTAVNT---GLFFGLRG 156
Cdd:cd00828    78 VATEEALADAGITDPYEVHPSEVGVVVGSGMGGLRFL-RRGGKLDARAVNPYVSPK---WMLSPNTVAGwvnILLLSSHG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 157 RVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFATSQRNDEPKTTPSPFDTQRDGLVIGEGA 236
Cdd:cd00828   154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 237 GTLILEELEHARARGATIYGEIVGFATNCDAAH--ITQPQRDtMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAES 314
Cdd:cd00828   234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGrsVPAGGKG-IARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 315 QATAAIY---GDSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCgALDYIMGEAR--QIDCEYL 389
Cdd:cd00828   313 RAIAEVAgalGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDV-EHLSVVGLSRdlNLKVRAA 391

                         410
                  ....*....|....*.
gi 1235056357 390 QSNNFAFGGINTSIII 405
Cdd:cd00828   392 LVNAFGFGGSNAALVL 407
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 154-408 4.46e-55

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 185.32  E-value: 4.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 154 LRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEelcpseaAVFDTL----FATSQR-----NDEPKTTPSPFD 224
Cdd:PRK14691   80 FKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAE-------AVIDTVslagFAAARAlsthfNSTPEKASRPFD 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 225 TQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRD------TMQICMEQslamAGLSARDMGY 298
Cdd:PRK14691  153 TARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDgdgayrAMKIALRQ----AGITPEQVQH 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 299 ISAHGTATDRGDIAESQATAAIYGDS--VPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGALDY 376
Cdd:PRK14691  229 LNAHATSTPVGDLGEINAIKHLFGESnaLAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNI 308

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1235056357 377 IMGEARQIDCEYLQSNNFAFGGINTSIIIKRW 408
Cdd:PRK14691  309 IAGNAQPHDMTYALSNGFGFAGVNASILLKRW 340
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
5-407 4.67e-53

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 181.58  E-value: 4.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   5 VVITGMGGVTAFGETWQSVSSKLLAyenavRKMPEWQVYDG----LHTLLG--APIDDFTLPEHYTRKRIRamgrvslmS 78
Cdd:PRK09185    4 VYISAFGATSALGRGLDAILAALRA-----GRASGMRPCDFwlvdLPTWVGevVGVELPALPAALAAFDCR--------N 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  79 TRATELALEQaglIGEAVLT------NGQTGIAYGSSTGSTGpvsefATMLTEKHTNNITGTT-----YVQMMPHTTAVN 147
Cdd:PRK09185   71 NRLALLALQQ---IEPAVEAaiarygADRIGVVLGTSTSGIL-----EGELAYRRRDPAHGALpadyhYAQQELGSLADF 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 148 TGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFATSqrndepKTTPSPFDTQR 227
Cdd:PRK09185  143 LRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLS------PQPCRPFSANR 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 228 DGLVIGEGAGTLILEelehaRARGATI----YGEivgfatNCDAAHIT--QPQRDTMQICMEQSLAMAGLSARDMGYISA 301
Cdd:PRK09185  217 DGINIGEAAAFFLLE-----REDDAAVallgVGE------SSDAHHMSapHPEGLGAILAMQQALADAGLAPADIGYINL 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 302 HGTATDRGDIAESQATAAIYGDSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGAlDYIMGEA 381
Cdd:PRK09185  286 HGTATPLNDAMESRAVAAVFGDGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPP-LYLVENA 364

                         410       420
                  ....*....|....*....|....*.
gi 1235056357 382 RQIDCEYLQSNNFAFGGINTSIIIKR 407
Cdd:PRK09185  365 QALAIRYVLSNSFAFGGNNCSLIFGR 390
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 4-407 6.36e-47

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 165.59  E-value: 6.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   4 RVVITGMGGVTAFGETWQSVSSKLLAYENAVRKM-------PEWQVYDGLHTLLGAPIDDFTLPEHYTRKRIRamgRVSL 76
Cdd:PRK07103    3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMrrpgrqvPDDAGAGLASAFIGAELDSLALPERLDAKLLR---RASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  77 mSTRATELAL----EQAGLigEAVLTNgQTGIAYGSStgstgpvsefatmltekhtnNITGTTYVQMMPH---------- 142
Cdd:PRK07103   80 -SAQAALAAAreawRDAAL--GPVDPD-RIGLVVGGS--------------------NLQQREQALVHETyrdrpaflrp 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 143 ---TTAVNTGLF------FGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGA-EELCPSEAAVFDTLFA--TS 210
Cdd:PRK07103  136 sygLSFMDTDLVglcseqFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGAlMDLSYWECQALRSLGAmgSD 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 211 QRNDEPKTTPSPFDTQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITQPQRDTMQICMEQSLAMAG 290
Cdd:PRK07103  216 RFADEPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALRRAG 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 291 LSARDMGYISAHGTATDRGDIAESQATAAIYGDSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQ 370
Cdd:PRK07103  296 LGPEDIDYVNPHGTGSPLGDETELAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIDE 375

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1235056357 371 cgALDYIMGEARQIDCEYLQSNNFAFGGINTSIIIKR 407
Cdd:PRK07103  376 --RFRWVGSTAESARIRYALSLSFGFGGINTALVLER 410
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 4-405 6.42e-41

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: 150.02  E-value: 6.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   4 RVVITGM-----GGVTAfGETWQSVSSKllayENAVRKMPE--WQVY---------DGLHTLLGAPIDDFTLPEH----Y 63
Cdd:cd00833     2 PIAIVGMacrfpGAADP-DEFWENLLEG----RDAISEIPEdrWDADgyypdpgkpGKTYTRRGGFLDDVDAFDAaffgI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  64 TRKRIRAM---GRVSLMSTRAtelALEQAGLIGEAvLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTnnITGTTyvqmm 140
Cdd:cd00833    77 SPREAEAMdpqQRLLLEVAWE---ALEDAGYSPES-LAGSRTGVFVGASSSDYLELLARDPDEIDAYA--ATGTS----- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 141 phtTAVNTGL---FFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSqrndeP 216
Cdd:cd00833   146 ---RAFLANRisyFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNlILSPDMFVGFSKAGMLS-----P 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 217 KTTPSPFDTQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCD--AAHITQPQRDTMQICMEQSLAMAGLSAR 294
Cdd:cd00833   218 DGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgrTKGITAPSGEAQAALIRRAYARAGVDPS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 295 DMGYISAHGTATDRGDIAESQATAAIYG------DSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPD 368
Cdd:cd00833   298 DIDYVEAHGTGTPLGDPIEVEALAKVFGgsrsadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPN 377

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1235056357 369 EQCGALD---YIMGEARQIDCEYLQS----NNFAFGGINTSIII 405
Cdd:cd00833   378 PKIDFEEsplRVPTEARPWPAPAGPRragvSSFGFGGTNAHVIL 421
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 65-405 1.76e-40

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: 146.63  E-value: 1.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  65 RKRIRAMG-RVSLMSTRATELALEQAGLiGEAVLTNGQTGIAYGSSTGSTGPVSEFATMLTEKHTNNITGttyvQMMPhT 143
Cdd:cd00825     1 RAVITGLGsYVSILGFEAAERAIADAGL-SREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTK----AMFP-G 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 144 TAVNTGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCpseaAVFDTLFATSQRNDEPKTTPSPF 223
Cdd:cd00825    75 ASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELA----APMDCEFDAMGALSTPEKASRTF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 224 DTQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAH--ITQPQRDTMQICMEQSLAMAGLSARDMGYISA 301
Cdd:cd00825   151 DAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGmgAFAPSAEGLARAAKEALAVAGLTVWDIDYLVA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 302 HGTATDRGDIAESQATAAIYGD-SVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEqcgALDYIMGE 380
Cdd:cd00825   231 HGTGTPIGDVKELKLLRSEFGDkSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE---AGLNIVTE 307

                         330       340
                  ....*....|....*....|....*
gi 1235056357 381 ARQIDCEYLQSNNFAFGGINTSIII 405
Cdd:cd00825   308 TTPRELRTALLNGFGLGGTNATLVL 332
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 3-382 2.71e-33

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: 128.63  E-value: 2.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFG----ETWQSVssklLAYENAVRKMPEWQVyDGLHTLLGAPIDDFTLPEHYTRKRIRAMGRVSLMS 78
Cdd:cd00832     1 RRAVVTGIGVVAPNGlgveEYWKAV----LDGRSGLGPITRFDP-SGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  79 TRATELALEQAGLiGEAVLTNGQTGIAYGSSTGSTgpvsEFatmlTEKHTNNI--TGTTYV---QMMPHTTAVNTG---L 150
Cdd:cd00832    76 LAAADWALADAGV-DPAALPPYDMGVVTASAAGGF----EF----GQRELQKLwsKGPRHVsayQSFAWFYAVNTGqisI 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 151 FFGLRGrviPTSSACT---SGSQAIGYAWEAIRHGyQTVMVAGGAEE-LCP--SEAAVFDTLFATSqrnDEPKTTPSPFD 224
Cdd:cd00832   147 RHGMRG---PSGVVVAeqaGGLDALAQARRLVRRG-TPLVVSGGVDSaLCPwgWVAQLSSGRLSTS---DDPARAYLPFD 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 225 TQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAHITqPQRDTMQICMEQSLAMAGLSARDMGYISAHGT 304
Cdd:cd00832   220 AAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGS-GRPPGLARAIRLALADAGLTPEDVDVVFADAA 298

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1235056357 305 ATDRGDIAESQATAAIYG-DSVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLTQPDEQCGaLDYIMGEAR 382
Cdd:cd00832   299 GVPELDRAEAAALAAVFGpRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYG-LDLVTGRPR 376
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 3-247 6.64e-31

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: 118.51  E-value: 6.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   3 RRVVITGMGGVTAFGETWQSVSSKLLAYENAVRKMPE--WQVYD---------GLHTLLGAPIDDFTLPEHY----TRKR 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrWDPDKlydppsriaGKIYTKWGGLDDIFDFDPLffgiSPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  68 IRAMGRVSLMSTRATELALEQAGlIGEAVLTNGQTGIAYGSSTGSTGPVsefaTMLTEKHTNNITGTTYVQMMPHTTAVN 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAG-ITPDSLDGSRTGVFIGSGIGDYAAL----LLLDEDGGPRRGSPFAVGTMPSVIAGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 148 TGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSQrnDEPKTtpsPFDTQ 226
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSP--DGPCK---AFDPF 230

                         250       260
                  ....*....|....*....|.
gi 1235056357 227 RDGLVIGEGAGTLILEELEHA 247
Cdd:pfam00109 231 ADGFVRGEGVGAVVLKRLSDA 251
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 255-365 2.90e-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: 109.97  E-value: 2.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 255 YGEIVGFATNCDAAHITQPQRDT--MQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQATAAIYGD-----SVPV 327
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGegQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSgarkqPLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1235056357 328 SSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLT 365
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 85-367 1.87e-24

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 106.11  E-value: 1.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   85 ALEQAGLIGEAvLTNGQTGIAYGSSTgstgpvSEFATMLTEkHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTSSA 164
Cdd:COG3321    102 ALEDAGYDPES-LAGSRTGVFVGASS------NDYALLLLA-DPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTA 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  165 CTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAV-FDTLFATSqrndepkttPS----PFDTQRDGLVIGEGAGTL 239
Cdd:COG3321    174 CSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFIlFSKGGMLS---------PDgrcrAFDADADGYVRGEGVGVV 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  240 ILEELEHARARGATIYGEIVGFATNCDAAH--ITQPQRDTMQICMEQSLAMAGLSARDMGYISAHGTATDRGDIAESQAT 317
Cdd:COG3321    245 VLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAAL 324

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  318 AAIYGDS------VPVSSLKSYFGHTLGACGAleawMSL----QMMREGWFAPTLNLTQP 367
Cdd:COG3321    325 TAAFGQGrpadqpCAIGSVKSNIGHLEAAAGV----AGLikavLALRHGVLPPTLHFETP 380
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 131-361 8.05e-21

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: 90.97  E-value: 8.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 131 ITGTTY-VQMMPHTTAVNTGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELcpseaavfdtlfat 209
Cdd:cd00327    33 IVGTTGgSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF-------------- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 210 sqrndepkttpspfdtqrdglVIGEGAGTLILEELEHARARGATIYGEIVGFATNCD-AAHITQPQRDTMQICMEQSLAM 288
Cdd:cd00327    99 ---------------------VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVSGEGLARAARKALEG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1235056357 289 AGLSARDMGYISAHGTATDRGDIAESQATAAIYGD-SVPVSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPT 361
Cdd:cd00327   158 AGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT 231
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 152-408 2.10e-17

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 84.67  E-value: 2.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  152 FGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGaeeLCPSEAAVFDTLFATSqrndePKTTPS----PFDTQR 227
Cdd:TIGR02813  193 FDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---VCTDNSPFMYMSFSKT-----PAFTTNediqPFDIDS 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  228 DGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDA--AHITQPQRDTMQICMEQSLAMAGLSARDMGYISAHGTA 305
Cdd:TIGR02813  265 KGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTG 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  306 TDRGDIAESQATAAIYGDS------VPVSSLKSYFGH---TLGACGALEAWMSLQmmrEGWFAPTLNLTQPDEQCGALD- 375
Cdd:TIGR02813  345 TAAGDVAEFGGLVSVFSQDndqkqhIALGSVKSQIGHtksTAGTAGMIKAVLALH---HKVLPPTINVDQPNPKLDIENs 421

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1235056357  376 --YIMGEARqidcEYLQS----------NNFAFGGINTSIIIKRW 408
Cdd:TIGR02813  422 pfYLNTETR----PWMQRedgtprragiSSFGFGGTNFHMVLEEY 462
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 147-405 2.33e-12

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: 66.97  E-value: 2.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  147 NTGLFFGLRGR----VIPTssACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSqrndepkttPS 221
Cdd:smart00825  77 RTGVFVGVSSSdysvTVDT--ACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLS---------PD 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  222 ----PFDTQRDGLVIGEGAGTLILEELEHARARGATIYGEIVGFATNCDAAH--ITQPQrdtmqicmeqslamaglsard 295
Cdd:smart00825 146 grckTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPS--------------------- 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  296 mgyisahgtatdrgdiAESQataaiygdsVPVSSLKSYFGHTLGACGAleawMSL----QMMREGWFAPTLNLTQP---- 367
Cdd:smart00825 205 ----------------GPAQ---------LLIGSVKSNIGHLEAAAGV----AGLikvvLALKHGVIPPTLHFETPnphi 255

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1235056357  368 DEQCGALdYIMGEARQIDCEYLQS----NNFAFGGINTSIII 405
Cdd:smart00825 256 DLEESPL-RVPTELTPWPPPGRPRragvSSFGFGGTNAHVIL 296
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
229-340 7.32e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 44.56  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 229 GLVIGEGAGTLILEELEHARARGATIYGEIVGFATNcdaahITQPQRDTMQICMEQSLAMAGLSARDMGYISAhgtATDR 308
Cdd:PRK06519  238 GFILGSGGAFLVLESREHAEARGARPYARISGVESD-----RARRAPGDLEASLERLLKPAGGLAAPTAVISG---ATGA 309

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1235056357 309 GDIAESQATAAIYGDSVPVSSLKSYFGHTLGA 340
Cdd:PRK06519  310 HPATAEEKAALEAALAGPVRGIGTLFGHTMEA 341
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 1-299 5.87e-03

3-oxoacyl-(acyl carrier protein) synthase; Validated


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 38.46  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357   1 MTRRVVITGMGGVTAFGETWQSVSSKLLAyenAVRKMPEWQVYDGLHtllGAPIDDFTLPEHytrKRIRAMGRVSLMSTR 80
Cdd:PRK06147    1 MMRALAIVGSGMVTAVGLDAPSSCAAIRA---RLDNFQETRFIDPPG---GEWLIGAPVPLP---PPWRGPERLAEMAAP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357  81 ATELALEQ--AGLIGEAVLTNGqtgIAYGSSTGSTGPVSE-FATMLTEkhtnnITGTTYvqmmPHTTAVNTglffglRGR 157
Cdd:PRK06147   72 AIAEALEGlpALDASEAPLLLC---VAEEERPGRPPDLEErLLRELEA-----RLGLRL----EPGSAVIA------RGR 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235056357 158 ViptssactSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSeaavfDTLFATSQRnDEPKTTPSPfdtqrDGLVIGEGAG 237
Cdd:PRK06147  134 V--------SGAVALAQARRLIAAGGCPRVLVAGVDSLLTG-----PTLAHYEAR-DRLLTSQNS-----NGFIPGEAAA 194

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1235056357 238 TLILEELEHARARGATIYGeiVGFATncDAAHITQP-----QRDTMQICMEQSLAMAGLSARDMGYI 299
Cdd:PRK06147  195 AVLLGRPAGGEAPGLPLLG--LGLGR--EPAPVGESedlplRGDGLTQAIRAALAEAGCGLEDMDYR 257
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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