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Conserved domains on  [gi|568985607|ref|XP_006518164|]
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3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial isoform X1 [Mus musculus]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase family protein( domain architecture ID 10095930)

beta-ketoacyl-[acyl-carrier-protein] synthase family protein similar to nodulation protein E (nodE), which is involved in the synthesis of a highly unsaturated fatty acid moiety that is part of a lipo-oligosaccharide responsible for host specificity, and to polyketide beta-ketoacyl synthases, which are involved in the synthesis of polyketide antibiotics and related compounds

CATH:  3.40.47.10
EC:  2.3.1.-
Gene Ontology:  GO:0006633|GO:0004315
PubMed:  11969206
SCOP:  3000122

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 42-456 0e+00

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: 593.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPRgphegqFNEENFVSKSDAKSMSSSTIM 121
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 122 AVGAAELALKDSGWHPKREaDQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:cd00834   75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:cd00834  154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:cd00834  234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:cd00834  314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390

                        410
                 ....*....|....*.
gi 568985607 441 LTNSFGFGGTNATLCI 456
Cdd:cd00834  391 LSNSFGFGGHNASLVF 406
 
Name Accession Description Interval E-value
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 42-456 0e+00

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: 593.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPRgphegqFNEENFVSKSDAKSMSSSTIM 121
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 122 AVGAAELALKDSGWHPKREaDQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:cd00834   75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:cd00834  154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:cd00834  234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:cd00834  314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390

                        410
                 ....*....|....*.
gi 568985607 441 LTNSFGFGGTNATLCI 456
Cdd:cd00834  391 LSNSFGFGGHNASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
41-454 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 592.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  41 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTI 120
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVK------DFNPDDYMSRKEARRMDRFIQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 121 MAVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKG 200
Cdd:PRK07314  75 YGIAAAKQAVEDAGLEIT-EENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALS-SNPDPKLACRPFHPERDGFVMGEG 279
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALStRNDDPERASRPFDKDRDGFVMGEG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 280 AAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAE 359
Cdd:PRK07314 234 AGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAE 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 360 NRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcI 439
Cdd:PRK07314 314 TQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---Y 390

                        410
                 ....*....|....*
gi 568985607 440 GLTNSFGFGGTNATL 454
Cdd:PRK07314 391 ALSNSFGFGGTNASL 405
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 42-455 0e+00

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: 588.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  122 AVGAAELALKDSGWhPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:TIGR03150  75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390

                         410
                  ....*....|....*
gi 568985607  441 LTNSFGFGGTNATLC 455
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 42-456 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: 575.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 122 AVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:COG0304   75 ALAAAREALADAGLDLD-EVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:COG0304  154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:COG0304  234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:COG0304  314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390

                        410
                 ....*....|....*.
gi 568985607 441 LTNSFGFGGTNATLCI 456
Cdd:COG0304  391 LSNSFGFGGHNASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 42-291 1.07e-57

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: 190.54  E-value: 1.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGD-----EYKNIPCSVA--AYVPRGP--HEGQFNEENF-VSKSD 111
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAgkIYTKWGGldDIFDFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  112 AKSMSSSTIMAVGAAELALKDSGWHPkREADQVATGVAIGMGMvplEVISETALLFQTKGYNKVSPFFVPKIlINMAAGQ 191
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITP-DSLDGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  192 VSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNpDPklaCRPFHPER 271
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231

                         250       260
                  ....*....|....*....|
gi 568985607  272 DGFVMGEGAAVLVLEEHEHA 291
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 204-452 1.07e-30

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: 120.13  E-value: 1.07e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   204 SVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnPDPKlaCRPFHPERDGFVMGEGAAVL 283
Cdd:smart00825  92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS--PDGR--CKTFDASADGYVRGEGVGVV 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   284 VLEEHEHAVQRGARIYAEILGYGL--SGDAGHITAPDPEGegalrcmaaavkdagvspeQisyvnahatstplgdaaenr 361
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA-------------------Q-------------------- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   362 aikrlfrdhacaLAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLN----YVPLESQEWKAEG- 436
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPGr 276

                          250
                   ....*....|....*..
gi 568985607   437 -RCIGLtNSFGFGGTNA 452
Cdd:smart00825 277 pRRAGV-SSFGFGGTNA 292
 
Name Accession Description Interval E-value
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 42-456 0e+00

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: 593.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPRgphegqFNEENFVSKSDAKSMSSSTIM 121
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 122 AVGAAELALKDSGWHPKREaDQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:cd00834   75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:cd00834  154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:cd00834  234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:cd00834  314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390

                        410
                 ....*....|....*.
gi 568985607 441 LTNSFGFGGTNATLCI 456
Cdd:cd00834  391 LSNSFGFGGHNASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
41-454 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 592.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  41 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTI 120
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVK------DFNPDDYMSRKEARRMDRFIQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 121 MAVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKG 200
Cdd:PRK07314  75 YGIAAAKQAVEDAGLEIT-EENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALS-SNPDPKLACRPFHPERDGFVMGEG 279
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALStRNDDPERASRPFDKDRDGFVMGEG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 280 AAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAE 359
Cdd:PRK07314 234 AGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAE 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 360 NRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcI 439
Cdd:PRK07314 314 TQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---Y 390

                        410
                 ....*....|....*
gi 568985607 440 GLTNSFGFGGTNATL 454
Cdd:PRK07314 391 ALSNSFGFGGTNASL 405
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 42-455 0e+00

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: 588.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  122 AVGAAELALKDSGWhPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:TIGR03150  75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390

                         410
                  ....*....|....*
gi 568985607  441 LTNSFGFGGTNATLC 455
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 42-456 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: 575.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 122 AVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:COG0304   75 ALAAAREALADAGLDLD-EVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:COG0304  154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:COG0304  234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:COG0304  314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390

                        410
                 ....*....|....*.
gi 568985607 441 LTNSFGFGGTNATLCI 456
Cdd:COG0304  391 LSNSFGFGGHNASLVF 406
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 42-454 0e+00

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 523.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYK--------------NIPCSVAAYVPRGPHEGQFNEENFV 107
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKmksedeetqlytldQLPSRVAALVPRGTGPGDFDEELWL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 108 SksdAKSMSSSTIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINM 187
Cdd:PLN02836  86 N---SRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINM 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 188 AAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACR 265
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfNSCPTEASR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 266 PFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYV 345
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYV 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 346 NAHATSTPLGDAAENRAIKRLFRDHAC--ALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLN 423
Cdd:PLN02836 323 NAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDG 402

                        410       420       430
                 ....*....|....*....|....*....|.
gi 568985607 424 YVPLESQewKAEGRCIGLTNSFGFGGTNATL 454
Cdd:PLN02836 403 FVPLTAS--KAMLIRAALSNSFGFGGTNASL 431
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
39-454 5.23e-175

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 497.21  E-value: 5.23e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  39 MLRRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVP--RGPHEGQFNEENFVSKSDAKSMS 116
Cdd:PRK06333   1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlAEDAEAGFDPDRYLDPKDQRKMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 117 SSTIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRY 196
Cdd:PRK06333  81 RFILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 197 KLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACRPFHPERDGF 274
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTrfNDAPEQASRPFDRDRDGF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 275 VMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPL 354
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 355 GDAAENRAIKRLFrDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFD-LNYVPLESQEWK 433
Cdd:PRK06333 321 GDLGEVAAIKKVF-GHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399

                        410       420
                 ....*....|....*....|.
gi 568985607 434 AEgrcIGLTNSFGFGGTNATL 454
Cdd:PRK06333 400 MD---YALSNGFGFGGVNASI 417
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 51-454 5.62e-168

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 479.19  E-value: 5.62e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  51 LVTPLGVGTQLVWDRLLRGESGIVSVVGDEYK----------------NIPCSVAAYVPrgphegqfnEENFVSKSDAKS 114
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFlpdcipeqkalenlvaAMPCQIAAEVD---------QSEFDPSDFAPT 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 115 MSSS--TIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQV 192
Cdd:PTZ00050  72 KRESraTHFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 193 SIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACRPFHPE 270
Cdd:PTZ00050 152 AIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkyNDDPQRASRPFDKD 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 271 RDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAG-VSPEQISYVNAHA 349
Cdd:PTZ00050 232 RAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHA 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 350 TSTPLGDAAENRAIKRLFRDHAC-ALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPlE 428
Cdd:PTZ00050 312 TSTPIGDKIELKAIKKVFGDSGApKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQ-G 390

                        410       420
                 ....*....|....*....|....*.
gi 568985607 429 SQEWKAEGRCIGLTNSFGFGGTNATL 454
Cdd:PTZ00050 391 KTAHPLQSIDAVLSTSFGFGGVNTAL 416
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
39-454 3.73e-131

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 385.13  E-value: 3.73e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  39 MLRRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSS 118
Cdd:PRK08722   1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVK------DFNCEEYMSKKDARKMDLF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 119 TIMAVGAAELALKDSGWHPKREaDQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKL 198
Cdd:PRK08722  75 IQYGIAAGIQALDDSGLEVTEE-NAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 199 KGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMG 277
Cdd:PRK08722 154 RGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 278 EGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDA 357
Cdd:PRK08722 234 DGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDV 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 358 AENRAIKR-LFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQewKAEG 436
Cdd:PRK08722 314 AEIKGIKRaLGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTAR--KVES 391

                        410
                 ....*....|....*...
gi 568985607 437 RCIGLTNSFGFGGTNATL 454
Cdd:PRK08722 392 MEYAICNSFGFGGTNGSL 409
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 42-451 4.75e-122

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 361.74  E-value: 4.75e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEIT------DFDPTEVMDPKEVKKADRFIQL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 122 AVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:PRK08439  76 GLKAAREAMKDAGFLPE-ELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:PRK08439 155 NLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPegEGALRCMAAAVKDAGVSPeqISYVNAHATSTPLGDAAEN 360
Cdd:PRK08439 235 GALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNET 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:PRK08439 311 AALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELN---VV 387

                        410
                 ....*....|.
gi 568985607 441 LTNSFGFGGTN 451
Cdd:PRK08439 388 MSNSFGFGGTN 398
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 41-457 7.84e-97

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 301.51  E-value: 7.84e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  41 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTI 120
Cdd:PLN02787 128 QRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIK------SFSTDGWVAPKLSKRMDKFML 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 121 MAVGAAELALKDSGWHPK--READQVATGVAIGMGMVPLEVISEtALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKL 198
Cdd:PLN02787 202 YLLTAGKKALADGGITEDvmKELDKTKCGVLIGSAMGGMKVFND-AIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGW 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 199 KGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMG 277
Cdd:PLN02787 281 MGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMG 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 278 EGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDA 357
Cdd:PLN02787 361 EGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDL 440

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 358 AENRAIKRLFRDHAcALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNyVPLESQEWKAEGR 437
Cdd:PLN02787 441 KEYQALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTK-VLVGPKKERLDIK 518

                        410       420
                 ....*....|....*....|
gi 568985607 438 cIGLTNSFGFGGTNATLCIA 457
Cdd:PLN02787 519 -VALSNSFGFGGHNSSILFA 537
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 136-456 7.43e-95

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 289.71  E-value: 7.43e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 136 HPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHA 215
Cdd:PRK14691  18 HADNTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 216 VGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACRPFHPERDGFVMGEGAAVLVLEEHEHAVQ 293
Cdd:PRK14691  98 IGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALA 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 294 RGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAENRAIKRLFRDhACA 373
Cdd:PRK14691 178 RGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNA 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 374 LAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFD-LNYVPLESQewkAEGRCIGLTNSFGFGGTNA 452
Cdd:PRK14691 257 LAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQ---PHDMTYALSNGFGFAGVNA 333


                 ....
gi 568985607 453 TLCI 456
Cdd:PRK14691 334 SILL 337
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
42-456 1.44e-89

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 278.41  E-value: 1.44e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVG-DEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTI 120
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEwDRYDGLNTRLAAPID------DFELPAHYTRKKIRSMGRVSL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 121 MAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKG 200
Cdd:PRK09116  76 MATRASELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEG 279
Cdd:PRK09116 156 RVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTrNDAPELTPRPFDANRDGLVIGEG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 280 AAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGalRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAE 359
Cdd:PRK09116 235 AGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAE 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 360 NRAIKRLFRDHacaLAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEF-DLNYVPLESQEWKAEgrc 438
Cdd:PRK09116 313 SQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTE--- 386

                        410
                 ....*....|....*...
gi 568985607 439 IGLTNSFGFGGTNATLCI 456
Cdd:PRK09116 387 YVMSNNFAFGGINTSLIF 404
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
44-454 3.65e-89

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 277.77  E-value: 3.65e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  44 VVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGD--EYKNIPCSVAAYVPRGPHEGQFNEENfvsksdaKSMSSSTIM 121
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPfvEEFDLPVRIGGHLLEEFDHQLTRVEL-------RRMSYLQRM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 122 AVGAAELALKDSGwhpKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:PRK07910  87 STVLGRRVWENAG---SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACRPFHPERDGFVMGEG 279
Cdd:PRK07910 164 VITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMStnNDDPAGACRPFDKDRDGFVFGEG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 280 AAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAE 359
Cdd:PRK07910 244 GALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAE 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 360 NRAIKRLFRDHACalAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcI 439
Cdd:PRK07910 324 GKAINNALGGHRP--AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYR---Y 398

                        410
                 ....*....|....*
gi 568985607 440 GLTNSFGFGGTNATL 454
Cdd:PRK07910 399 AINNSFGFGGHNVAL 413
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
42-454 1.24e-86

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 270.77  E-value: 1.24e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVsvVGDEYKNI--PCSVAAYVprgphegQFNEENFVSKSDAKSMSSST 119
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT--FSPEFAEMgmRSQVWGNV-------KLDPTGLIDRKVMRFMGDAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 120 IMAVGAAELALKDSGWhpkrEADQVA---TGVAIGMGMVPLEVISETA-LLFQTKGYNKVSPFFVPKILINMAAGQVSIR 195
Cdd:PRK07967  73 AYAYLAMEQAIADAGL----SEEQVSnprTGLIAGSGGGSTRNQVEAAdAMRGPRGPKRVGPYAVTKAMASTVSACLATP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 196 YKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAgFSRARALSS--NPDPKLACRPFHPERDG 273
Cdd:PRK07967 149 FKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTkyNDTPEKASRAYDANRDG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 274 FVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITApdPEGEGALRCMAAAVkdAGVSPEqISYVNAHATSTP 353
Cdd:PRK07967 228 FVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMAL--ATVDTP-IDYINTHGTSTP 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 354 LGDAAENRAIKRLFRDHACalAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEF-DLNYV--PLESQ 430
Cdd:PRK07967 303 VGDVKELGAIREVFGDKSP--AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVteTTDNA 380

                        410       420
                 ....*....|....*....|....
gi 568985607 431 EWKAEgrcigLTNSFGFGGTNATL 454
Cdd:PRK07967 381 ELTTV-----MSNSFGFGGTNATL 399
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
43-458 1.90e-82

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 259.21  E-value: 1.90e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  43 RVVITGIGLVTPLGVGTQlVWDRLLRGESGIVSVvgDEYKNIPCSVAAYVPRGPhegqfneenfvsksdaKSMSSSTIMA 122
Cdd:PRK05952   3 KVVVTGIGLVSALGDLEQ-SWQRLLQGKSGIKLH--QPFPELPPLPLGLIGNQP----------------SSLEDLTKTV 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 123 VGAAelaLKDSGWHPKrEADqvaTGVAIGMG---------MVPLEVISETALLFQTKGYNKVSpffvpkILINMAAGQVS 193
Cdd:PRK05952  64 VTAA---LKDAGLTPP-LTD---CGVVIGSSrgcqgqwekLARQMYQGDDSPDEELDLENWLD------TLPHQAAIAAA 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 194 IRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnpdpKLACRPFHPERDG 273
Cdd:PRK05952 131 RQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAYPFDRQREG 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 274 FVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTP 353
Cdd:PRK05952 206 LVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATR 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 354 LGDAAENRAIKRLFrdhACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDctEPEFDLNYV------PL 427
Cdd:PRK05952 286 LNDQREANLIQALF---PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQ--EPEFDLNFVrqaqqsPL 360

                        410       420       430
                 ....*....|....*....|....*....|.
gi 568985607 428 ESqewkaegrciGLTNSFGFGGTNATLCIAG 458
Cdd:PRK05952 361 QN----------VLCLSFGFGGQNAAIALGK 381
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
44-458 1.17e-81

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 258.41  E-value: 1.17e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  44 VVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVprgphegqfneeNFVSKSDAKSMSSSTIMAV 123
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------------DFLPESPFGASALSEALAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 124 GAAELALKDSG--------------------WHPKREADQVAtgvaigmgmvPLEVISETALLFQTKGYNKVSPFFvPKI 183
Cdd:PRK06501  81 LAAEEALAQAGigkgdfpgplflaappveleWPARFALAAAV----------GDNDAPSYDRLLRAARGGRFDALH-ERF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 184 LINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNPD-PKL 262
Cdd:PRK06501 150 QFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDpPEK 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 263 ACRPFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQI 342
Cdd:PRK06501 230 ASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQI 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 343 SYVNAHATSTPLGDAAENRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDL 422
Cdd:PRK06501 310 DYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPL 389

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 568985607 423 NYVPLESQEwkAEGRCIgLTNSFGFGGTNATLCIAG 458
Cdd:PRK06501 390 DVVPNVARD--ARVTAV-LSNSFGFGGQNASLVLTA 422
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 42-454 3.23e-79

"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: 251.59  E-value: 3.23e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLV---WDRLLRGESGIvSVVGDEYKNIPCSVAAYVPRGPHEGQFNEENFVsksdaksMSSS 118
Cdd:cd00828    1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGI-APVARLKSRFDRGVAGQIPTGDIPGWDAKRTGI-------VDRT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 119 TIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMvplevISETALLFQTKG-YNKVSPFFVPK--ILINMAAGQVSIR 195
Cdd:cd00828   73 TLLALVATEEALADAGITDPYEVHPSEVGVVVGSGM-----GGLRFLRRGGKLdARAVNPYVSPKwmLSPNTVAGWVNIL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 196 YKLK-GPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALSSNPD-PKLACRPFHPERDG 273
Cdd:cd00828  148 LLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEePEEMSRPFDETRDG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 274 FVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPeGEGALRCMAAAVKDAGVSPEQISYVNAHATSTP 353
Cdd:cd00828  227 FVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTP 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 354 LGDAAENRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWK 433
Cdd:cd00828  306 ANDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLN 385

                        410       420
                 ....*....|....*....|.
gi 568985607 434 AEGRCiGLTNSFGFGGTNATL 454
Cdd:cd00828  386 LKVRA-ALVNAFGFGGSNAAL 405
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
198-454 3.86e-74

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 237.82  E-value: 3.86e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 198 LKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALSSNPdpklaCRPFHPERDGFVMG 277
Cdd:PRK09185 149 LSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSPQP-----CRPFSANRDGINIG 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 278 EGAAVLVLE-EHEHAVQrgariyaeILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGD 356
Cdd:PRK09185 223 EAAAFFLLErEDDAAVA--------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLND 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 357 AAENRAIKRLFRDHacaLAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVpLESQEwKAEG 436
Cdd:PRK09185 295 AMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYL-VENAQ-ALAI 369

                        250
                 ....*....|....*...
gi 568985607 437 RCIgLTNSFGFGGTNATL 454
Cdd:PRK09185 370 RYV-LSNSFAFGGNNCSL 386
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 43-452 1.85e-73

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: 237.07  E-value: 1.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  43 RVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYknipcSVAAYVPRG--PHEGQFNEENFVSKSDAKSMSSSTI 120
Cdd:cd00833    2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRW-----DADGYYPDPgkPGKTYTRRGGFLDDVDAFDAAFFGI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 121 MAVGAAEL-------------ALKDSGWHPKREADQvATGVAIGMGMvpleviSETALLfQTKGYNKVSPFFVPKILINM 187
Cdd:cd00833   77 SPREAEAMdpqqrlllevaweALEDAGYSPESLAGS-RTGVFVGASS------SDYLEL-LARDPDEIDAYAATGTSRAF 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 188 AAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnPDPKlaCRPF 267
Cdd:cd00833  149 LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS--PDGR--CRPF 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 268 HPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLS--GDAGHITAPDPEGEGALrcMAAAVKDAGVSPEQISYV 345
Cdd:cd00833  225 DADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRTKGITAPSGEAQAAL--IRRAYARAGVDPSDIDYV 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 346 NAHATSTPLGDAAENRAIKRLF---RDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDL 422
Cdd:cd00833  303 EAHGTGTPLGDPIEVEALAKVFggsRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDF 382

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 568985607 423 N----YVPLESQEWKAEG--RCIGLtNSFGFGGTNA 452
Cdd:cd00833  383 EesplRVPTEARPWPAPAgpRRAGV-SSFGFGGTNA 417
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 43-457 4.08e-61

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 204.49  E-value: 4.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  43 RVVITGIGLVTPLGVGTQLVWDRLLRGESGIvSVVGDEYKNIPCSVAAYVPRGPHEGQFNE---ENFVSKSDAKSMSSST 119
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAF-GVMRRPGRQVPDDAGAGLASAFIGAELDSlalPERLDAKLLRRASLSA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 120 IMAVGAAELALKDSGWHPkreADQVATGVAIGMGMVPLEvisETALLFQTkgYNKVSPFFVPK-ILINM---AAGQVSIR 195
Cdd:PRK07103  82 QAALAAAREAWRDAALGP---VDPDRIGLVVGGSNLQQR---EQALVHET--YRDRPAFLRPSyGLSFMdtdLVGLCSEQ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 196 YKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNP---DPKLACRPFHPERD 272
Cdd:PRK07103 154 FGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfadEPEAACRPFDQDRD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 273 GFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEgaLRCMAAAVKDAGVSPEQISYVNAHATST 352
Cdd:PRK07103 234 GFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGS 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 353 PLGDAAENRAIKrlfrdhACALA---ISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDctEP-EFDLNYVPLE 428
Cdd:PRK07103 312 PLGDETELAALF------ASGLAhawINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLD--EPiDERFRWVGST 383

                        410       420
                 ....*....|....*....|....*....
gi 568985607 429 SQEWKAEgrcIGLTNSFGFGGTNATLCIA 457
Cdd:PRK07103 384 AESARIR---YALSLSFGFGGINTALVLE 409
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 42-291 1.07e-57

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: 190.54  E-value: 1.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGD-----EYKNIPCSVA--AYVPRGP--HEGQFNEENF-VSKSD 111
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAgkIYTKWGGldDIFDFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  112 AKSMSSSTIMAVGAAELALKDSGWHPkREADQVATGVAIGMGMvplEVISETALLFQTKGYNKVSPFFVPKIlINMAAGQ 191
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITP-DSLDGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  192 VSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNpDPklaCRPFHPER 271
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231

                         250       260
                  ....*....|....*....|
gi 568985607  272 DGFVMGEGAAVLVLEEHEHA 291
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 119-454 2.15e-57

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 192.47  E-value: 2.15e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 119 TIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPkilinmAAGQVSIRYKL 198
Cdd:cd00825   12 SILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG------ASGQIATPLGI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 199 KGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnpdPKLACRPFHPERDGFVMGE 278
Cdd:cd00825   86 HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST----PEKASRTFDAAADGFVFGD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 279 GAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAA 358
Cdd:cd00825  162 GAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 359 ENRAIKRLFRDHacALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDctepEFDLNYVPLESQEWKAEGRC 438
Cdd:cd00825  242 ELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIE----ELDEAGLNIVTETTPRELRT 315

                        330
                 ....*....|....*.
gi 568985607 439 iGLTNSFGFGGTNATL 454
Cdd:cd00825  316 -ALLNGFGLGGTNATL 330
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 129-452 8.98e-56

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 200.10  E-value: 8.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  129 ALKDSGWHPKREADQvATGVAIGMGMvplevisETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGPNHSVSTA 208
Cdd:COG3321   102 ALEDAGYDPESLAGS-RTGVFVGASS-------NDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  209 CTTGAHAVgdsfrfiaH--------GDADVMVAGGTDSCISPLSLAGFSRARALSsnPDPKlaCRPFHPERDGFVMGEGA 280
Cdd:COG3321   174 CSSSLVAV--------HlacqslrsGECDLALAGGVNLMLTPESFILFSKGGMLS--PDGR--CRAFDADADGYVRGEGV 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDaGH---ITAPDPEGEGALrcMAAAVKDAGVSPEQISYVNAHATSTPLGDA 357
Cdd:COG3321   242 GVVVLKRLSDALRDGDRIYAVIRGSAVNQD-GRsngLTAPNGPAQAAV--IRRALADAGVDPATVDYVEAHGTGTPLGDP 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  358 AENRAIKRLFRDHACA---LAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLN----YVPLESQ 430
Cdd:COG3321   319 IEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTELR 398

                         330       340
                  ....*....|....*....|....
gi 568985607  431 EWKAEG--RCIGLtNSFGFGGTNA 452
Cdd:COG3321   399 PWPAGGgpRRAGV-SSFGFGGTNA 421
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 42-454 1.30e-54

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: 187.18  E-value: 1.30e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrGPHEGQFNEENFVSKSDaksmsSSTIM 121
Cdd:cd00832    1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVP-DFDAAEHLPGRLLPQTD-----RMTRL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 122 AVGAAELALKDSGWHPKREADQ---VATGVAIG---MGMVPLEvisetALLfqTKGYNKVSPFFVPKILINMAAGQVSIR 195
Cdd:cd00832   75 ALAAADWALADAGVDPAALPPYdmgVVTASAAGgfeFGQRELQ-----KLW--SKGPRHVSAYQSFAWFYAVNTGQISIR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 196 YKLKGPNHSVSTACTTGAHAVGDSFRFIAHGdADVMVAGGTDSCISPLSLAGFSRARALSSNPDPKLACRPFHPERDGFV 275
Cdd:cd00832  148 HGMRGPSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 276 MGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDaghitaPDP---EGEGALRCMAAAVKDAGVSPEQISYVNAHATST 352
Cdd:cd00832  227 PGEGGAILVLEDAAAARERGARVYGEIAGYAATFD------PPPgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGV 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 353 PLGDAAENRAIKRLFRDHacALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVplesqew 432
Cdd:cd00832  301 PELDRAEAAALAAVFGPR--GVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLV------- 371

                        410       420
                 ....*....|....*....|....*.
gi 568985607 433 KAEGRCIGLTNSF----GFGGTNATL 454
Cdd:cd00832  372 TGRPRPAALRTALvlarGRGGFNSAL 397
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 299-414 1.10e-47

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: 159.66  E-value: 1.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  299 YAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAENRAIKRLFRDHAC--ALAI 376
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqPLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568985607  377 SSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLD 414
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 181-451 2.43e-37

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: 145.92  E-value: 2.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   181 PKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNPDp 260
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   261 klaCRPFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDA--GHITAPDPEGEGalRCMAAAVKDAGVS 338
Cdd:TIGR02813  257 ---IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQA--KALKRAYDDAGFA 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   339 PEQISYVNAHATSTPLGDAAENRAIKRLF---RDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDC 415
Cdd:TIGR02813  332 PHTCGLIEAHGTGTAAGDVAEFGGLVSVFsqdNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQ 411

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 568985607   416 TEPEFDLNYVPL----ESQEWKAEG----RCIGLTnSFGFGGTN 451
Cdd:TIGR02813  412 PNPKLDIENSPFylntETRPWMQREdgtpRRAGIS-SFGFGGTN 454
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 188-456 2.42e-33

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: 126.40  E-value: 2.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 188 AAGQVSIRYKLK-GPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCisplslagfsraralssnpdpklacrp 266
Cdd:cd00327   46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF--------------------------- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 267 fhperdgfVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDaGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVN 346
Cdd:cd00327   99 --------VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFD-GASMVPAVSGEGLARAARKALEGAGLTPSDIDYVE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 347 AHATSTPLGDAAENRAIKRLFRDHacALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTlnldctepefdlnyvp 426
Cdd:cd00327  170 AHGTGTPIGDAVELALGLDPDGVR--SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------- 231

                        250       260       270
                 ....*....|....*....|....*....|
gi 568985607 427 lesqewKAEGRCiGLTNSFGFGGTNATLCI 456
Cdd:cd00327  232 ------PREPRT-VLLLGFGLGGTNAAVVL 254
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 204-452 1.07e-30

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: 120.13  E-value: 1.07e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   204 SVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnPDPKlaCRPFHPERDGFVMGEGAAVL 283
Cdd:smart00825  92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS--PDGR--CKTFDASADGYVRGEGVGVV 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   284 VLEEHEHAVQRGARIYAEILGYGL--SGDAGHITAPDPEGegalrcmaaavkdagvspeQisyvnahatstplgdaaenr 361
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA-------------------Q-------------------- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607   362 aikrlfrdhacaLAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLN----YVPLESQEWKAEG- 436
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPGr 276

                          250
                   ....*....|....*..
gi 568985607   437 -RCIGLtNSFGFGGTNA 452
Cdd:smart00825 277 pRRAGV-SSFGFGGTNA 292
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
38-412 1.70e-15

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 78.07  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  38 AMLRRRVVITGIGLVTPLGVGTQLVWDRLlrgESGIVSVVGDEYKNIPCSV--------AAYVPRgphegqfneenfvsK 109
Cdd:PRK06519   2 RMQPNDVVITGIGLVSSLGEGLDAHWNAL---SAGRPQPNVDTETFAPYPVhplpeidwSQQIPK--------------R 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 110 SDAKSMSSSTIMAVGAAELALKDSGWhpKREADQVATG---VAIGMGMVPLEVIS----------ETALLFQTKGYNKVS 176
Cdd:PRK06519  65 GDQRQMETWQRLGTYAAGLALDDAGI--KGNEELLSTMdmiVAAGGGERDIAVDTailnearkrnDRGVLLNERLMTELR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 177 PFFVPKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS 256
Cdd:PRK06519 143 PTLFLAQLSNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLK 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 257 NPdpklacrpFHP-------ERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEIlgyglSGDAGHITAPDPegeGAL-RCM 328
Cdd:PRK06519 223 GG--------WAPvwsrggeDGGGFILGSGGAFLVLESREHAEARGARPYARI-----SGVESDRARRAP---GDLeASL 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 329 AAAVKDAGVSPEQiSYVNAHATSTPLGDAAEnraikRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLP 408
Cdd:PRK06519 287 ERLLKPAGGLAAP-TAVISGATGAHPATAEE-----KAALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALF 360


                 ....
gi 568985607 409 PTLN 412
Cdd:PRK06519 361 PPFD 364
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 42-345 5.24e-09

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 57.72  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607  42 RRVVITGIGLVTPLGVgtqlvwdrllrgesgivsvvgdeykNIPCSVAAYvpRGpHEGQFNEENFVSKSDAKsmssstim 121
Cdd:PRK06147   3 RALAIVGSGMVTAVGL-------------------------DAPSSCAAI--RA-RLDNFQETRFIDPPGGE-------- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 122 AVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLfqtkgyNKVSPFFVPKILINMAAG-----QVSIRY 196
Cdd:PRK06147  47 WLIGAPVPLPPPWRGPERLAEMAAPAIAEALEGLPALDASEAPLL------LCVAEEERPGRPPDLEERllrelEARLGL 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 197 KLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNPDPklacrpfhperDGFVM 276
Cdd:PRK06147 121 RLEPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNS-----------NGFIP 189

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568985607 277 GEGAAVLVLEEHEHAVQRGARIYAeiLGYGL--SGDAGHITAPdPEGEGALRCMAAAVKDAGVSPEQISYV 345
Cdd:PRK06147 190 GEAAAAVLLGRPAGGEAPGLPLLG--LGLGRepAPVGESEDLP-LRGDGLTQAIRAALAEAGCGLEDMDYR 257
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 201-280 5.60e-04

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: 41.98  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScispLSLAGFSRARALSSNP-DPKLACRPFHPE----RDGFV 275
Cdd:COG0183   80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVES----MSRAPMLLPKARWGYRmNAKLVDPMINPGltdpYTGLS 155


                 ....*
gi 568985607 276 MGEGA 280
Cdd:COG0183  156 MGETA 160
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 201-280 2.56e-03

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: 39.77  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568985607 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScIS--PLSLAGFSRARALSSNPDPKLACRPFHPERDGFVMGE 278
Cdd:cd00751   76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVES-MSraPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGI 154


                 ..
gi 568985607 279 GA 280
Cdd:cd00751  155 TA 156
 
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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