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Conserved domains on  [gi|213972556|ref|NP_001093978|]
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3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial [Rattus norvegicus]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase family protein( domain architecture ID 408)

beta-ketoacyl-[acyl-carrier-protein] synthase family protein may catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cond_enzymes super family cl09938
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 38-451 0e+00

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.


The actual alignment was detected with superfamily member PRK07314:

Pssm-ID: 447866 [Multi-domain]  Cd Length: 411  Bit Score: 583.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  38 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIvSVVGDEYKS-IPCSVAAFVPRgsdkgqFNEQNFVSKSDAKSMSSPT 116
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGI-GPITHFDTSdLAVKIAGEVKD------FNPDDYMSRKEARRMDRFI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 117 IMAVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLK 196
Cdd:PRK07314  74 QYGIAAAKQAVEDAGLEIT-EENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 197 GPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGE 275
Cdd:PRK07314 153 GPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 276 GAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAA 355
Cdd:PRK07314 233 GAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKA 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 356 ENRAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrc 435
Cdd:PRK07314 313 ETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID--- 389

                        410
                 ....*....|....*.
gi 213972556 436 IGLTNSFGFGGTNATL 451
Cdd:PRK07314 390 YALSNSFGFGGTNASL 405
 
Name Accession Description Interval E-value
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
38-451 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 583.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  38 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIvSVVGDEYKS-IPCSVAAFVPRgsdkgqFNEQNFVSKSDAKSMSSPT 116
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGI-GPITHFDTSdLAVKIAGEVKD------FNPDDYMSRKEARRMDRFI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 117 IMAVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLK 196
Cdd:PRK07314  74 QYGIAAAKQAVEDAGLEIT-EENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 197 GPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGE 275
Cdd:PRK07314 153 GPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 276 GAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAA 355
Cdd:PRK07314 233 GAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKA 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 356 ENRAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrc 435
Cdd:PRK07314 313 ETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID--- 389

                        410
                 ....*....|....*.
gi 213972556 436 IGLTNSFGFGGTNATL 451
Cdd:PRK07314 390 YALSNSFGFGGTNASL 405
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 39-453 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: 582.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPRgsdkgqFNEQNFVSKSDAKSMSSPTIM 118
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 119 AVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGP 198
Cdd:cd00834   75 ALAAAEEALADAGLDPE-ELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 199 NHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGEGA 277
Cdd:cd00834  154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 278 AVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAAEN 357
Cdd:cd00834  234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 358 RAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrcIG 437
Cdd:cd00834  314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390

                        410
                 ....*....|....*.
gi 213972556 438 LTNSFGFGGTNATLCI 453
Cdd:cd00834  391 LSNSFGFGGHNASLVF 406
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 39-452 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: 580.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPrgsdkgQFNEQNFVSKSDAKSMSSPTIM 118
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  119 AVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGP 198
Cdd:TIGR03150  75 ALAAAKEAVEDSGLDIE-EEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  199 NHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGEGA 277
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  278 AVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAAEN 357
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  358 RAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrcIG 437
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390

                         410
                  ....*....|....*
gi 213972556  438 LTNSFGFGGTNATLC 452
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 39-453 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: 567.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPrgsdkgQFNEQNFVSKSDAKSMSSPTIM 118
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 119 AVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGP 198
Cdd:COG0304   75 ALAAAREALADAGLDLD-EVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 199 NHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGEGA 277
Cdd:COG0304  154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 278 AVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAAEN 357
Cdd:COG0304  234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 358 RAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrcIG 437
Cdd:COG0304  314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390

                        410
                 ....*....|....*.
gi 213972556 438 LTNSFGFGGTNATLCI 453
Cdd:COG0304  391 LSNSFGFGGHNASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 39-288 9.91e-56

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: 185.53  E-value: 9.91e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGD-----EYKSIPCSVAAFVPRG----SDKGQFNEQNF-VSKSD 108
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAGKIYTKwgglDDIFDFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  109 AKSMSSPTIMAVGAAELALKDSGWYPKlEADQVATGVAIGMGMvplEVVSETALMFQTKGYSKVSPFFVPKIlINMAAGQ 188
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPD-SLDGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  189 VSIRYKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNpDPklaCRPFHPER 268
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231

                         250       260
                  ....*....|....*....|
gi 213972556  269 DGFVMGEGAAVLVLEEHEHA 288
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 201-449 6.13e-29

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: 115.12  E-value: 6.13e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   201 SVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnPDPKlaCRPFHPERDGFVMGEGAAVL 280
Cdd:smart00825  92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS--PDGR--CKTFDASADGYVRGEGVGVV 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   281 VLEEHEHAVQRGARIYAEVLGYGL--SGDAGHITAPDPEGegalrcmaaavkdagvspdQisyvnahatstplgdaaenr 358
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA-------------------Q-------------------- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   359 aikrlfrdharaLAISSTKGATGHLLGAAGAveAAF--TALACYHHKLPPTLNLDCTEAEFDLN----YVPLEAQEWKTE 432
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPP 274

                          250
                   ....*....|....*....
gi 213972556   433 G--RCIGLtNSFGFGGTNA 449
Cdd:smart00825 275 GrpRRAGV-SSFGFGGTNA 292
 
Name Accession Description Interval E-value
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
38-451 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 583.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  38 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIvSVVGDEYKS-IPCSVAAFVPRgsdkgqFNEQNFVSKSDAKSMSSPT 116
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGI-GPITHFDTSdLAVKIAGEVKD------FNPDDYMSRKEARRMDRFI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 117 IMAVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLK 196
Cdd:PRK07314  74 QYGIAAAKQAVEDAGLEIT-EENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 197 GPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGE 275
Cdd:PRK07314 153 GPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 276 GAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAA 355
Cdd:PRK07314 233 GAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKA 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 356 ENRAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrc 435
Cdd:PRK07314 313 ETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID--- 389

                        410
                 ....*....|....*.
gi 213972556 436 IGLTNSFGFGGTNATL 451
Cdd:PRK07314 390 YALSNSFGFGGTNASL 405
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 39-453 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: 582.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPRgsdkgqFNEQNFVSKSDAKSMSSPTIM 118
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 119 AVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGP 198
Cdd:cd00834   75 ALAAAEEALADAGLDPE-ELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 199 NHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGEGA 277
Cdd:cd00834  154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 278 AVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAAEN 357
Cdd:cd00834  234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 358 RAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrcIG 437
Cdd:cd00834  314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390

                        410
                 ....*....|....*.
gi 213972556 438 LTNSFGFGGTNATLCI 453
Cdd:cd00834  391 LSNSFGFGGHNASLVF 406
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 39-452 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: 580.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPrgsdkgQFNEQNFVSKSDAKSMSSPTIM 118
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  119 AVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGP 198
Cdd:TIGR03150  75 ALAAAKEAVEDSGLDIE-EEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  199 NHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGEGA 277
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  278 AVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAAEN 357
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  358 RAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrcIG 437
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390

                         410
                  ....*....|....*
gi 213972556  438 LTNSFGFGGTNATLC 452
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 39-453 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: 567.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPrgsdkgQFNEQNFVSKSDAKSMSSPTIM 118
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 119 AVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGP 198
Cdd:COG0304   75 ALAAAREALADAGLDLD-EVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 199 NHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGEGA 277
Cdd:COG0304  154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 278 AVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAAEN 357
Cdd:COG0304  234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 358 RAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrcIG 437
Cdd:COG0304  314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390

                        410
                 ....*....|....*.
gi 213972556 438 LTNSFGFGGTNATLCI 453
Cdd:COG0304  391 LSNSFGFGGHNASLVF 406
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 39-451 0e+00

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 517.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYK--------------SIPCSVAAFVPRGSDKGQFNEQNFV 104
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKmksedeetqlytldQLPSRVAALVPRGTGPGDFDEELWL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 105 SksdAKSMSSPTIMAVGAAELALKDSGWYPKLEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINM 184
Cdd:PLN02836  86 N---SRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINM 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 185 AAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NPDPKLACR 262
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfNSCPTEASR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 263 PFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYV 342
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYV 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 343 NAHATSTPLGDAAENRAIKRLFRDHAR--ALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLN 420
Cdd:PLN02836 323 NAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDG 402

                        410       420       430
                 ....*....|....*....|....*....|.
gi 213972556 421 YVPLEAQewKTEGRCIGLTNSFGFGGTNATL 451
Cdd:PLN02836 403 FVPLTAS--KAMLIRAALSNSFGFGGTNASL 431
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
37-451 4.03e-171

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 487.20  E-value: 4.03e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  37 SRRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPRGSD--KGQFNEQNFVSKSDAKSMSS 114
Cdd:PRK06333   2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDLAEdaEAGFDPDRYLDPKDQRKMDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 115 PTIMAVGAAELALKDSGWYPKLEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYK 194
Cdd:PRK06333  82 FILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 195 LKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NPDPKLACRPFHPERDGFV 272
Cdd:PRK06333 162 FKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTrfNDAPEQASRPFDRDRDGFV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 273 MGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLG 352
Cdd:PRK06333 242 MGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVG 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 353 DAAENRAIKRLFrDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFD-LNYVPLEAQEWKT 431
Cdd:PRK06333 322 DLGEVAAIKKVF-GHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDM 400

                        410       420
                 ....*....|....*....|
gi 213972556 432 EgrcIGLTNSFGFGGTNATL 451
Cdd:PRK06333 401 D---YALSNGFGFGGVNASI 417
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 48-451 3.12e-168

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 479.57  E-value: 3.12e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  48 LVTPLGVGTQLVWDRLLRGESGIVSVVGDEYK----------------SIPCSVAAFVprgsDKGQFNEQNFVSksdAKS 111
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFlpdcipeqkalenlvaAMPCQIAAEV----DQSEFDPSDFAP---TKR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 112 MSSPTIMAVGAAELALKDSGWYPKLEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSI 191
Cdd:PTZ00050  74 ESRATHFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 192 RYKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NPDPKLACRPFHPERD 269
Cdd:PTZ00050 154 KHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkyNDDPQRASRPFDKDRA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 270 GFVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAG-VSPDQISYVNAHATS 348
Cdd:PTZ00050 234 GFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATS 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 349 TPLGDAAENRAIKRLFRDH-ARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQ 427
Cdd:PTZ00050 314 TPIGDKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTA 393

                        410       420
                 ....*....|....*....|....
gi 213972556 428 EWKTEGRcIGLTNSFGFGGTNATL 451
Cdd:PTZ00050 394 HPLQSID-AVLSTSFGFGGVNTAL 416
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
37-451 1.15e-129

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 381.27  E-value: 1.15e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  37 SRRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPrgsdkgQFNEQNFVSKSDAKSMSSPT 116
Cdd:PRK08722   2 SKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVK------DFNCEEYMSKKDARKMDLFI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 117 IMAVGAAELALKDSGwYPKLEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLK 196
Cdd:PRK08722  76 QYGIAAGIQALDDSG-LEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 197 GPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGE 275
Cdd:PRK08722 155 GPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLGD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 276 GAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAA 355
Cdd:PRK08722 235 GAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVA 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 356 ENRAIKR-LFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQewKTEGR 434
Cdd:PRK08722 315 EIKGIKRaLGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTAR--KVESM 392

                        410
                 ....*....|....*..
gi 213972556 435 CIGLTNSFGFGGTNATL 451
Cdd:PRK08722 393 EYAICNSFGFGGTNGSL 409
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 39-448 1.38e-119

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 355.19  E-value: 1.38e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPrgsdkgQFNEQNFVSKSDAKSMSSPTIM 118
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEIT------DFDPTEVMDPKEVKKADRFIQL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 119 AVGAAELALKDSGWYPKlEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGP 198
Cdd:PRK08439  76 GLKAAREAMKDAGFLPE-ELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 199 NHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMGEGA 277
Cdd:PRK08439 155 NLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 278 AVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPegEGALRCMAAAVKDAGVspDQISYVNAHATSTPLGDAAEN 357
Cdd:PRK08439 235 GALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGN--PKIDYINAHGTSTPYNDKNET 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 358 RAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWKTEgrcIG 437
Cdd:PRK08439 311 AALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELN---VV 387

                        410
                 ....*....|.
gi 213972556 438 LTNSFGFGGTN 448
Cdd:PRK08439 388 MSNSFGFGGTN 398
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 38-454 2.91e-94

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 294.58  E-value: 2.91e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  38 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPrgsdkgQFNEQNFVSKSDAKSMSSPTI 117
Cdd:PLN02787 128 QRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIK------SFSTDGWVAPKLSKRMDKFML 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 118 MAVGAAELALKDSGWYPKL--EADQVATGVAIGMGMVPLEVVSEtALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKL 195
Cdd:PLN02787 202 YLLTAGKKALADGGITEDVmkELDKTKCGVLIGSAMGGMKVFND-AIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGW 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 196 KGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFVMG 274
Cdd:PLN02787 281 MGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMG 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 275 EGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDA 354
Cdd:PLN02787 361 EGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDL 440

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 355 AENRAIKRLFRDHARaLAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEwktegR 434
Cdd:PLN02787 441 KEYQALMRCFGQNPE-LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKE-----R 514

                        410       420
                 ....*....|....*....|...
gi 213972556 435 C---IGLTNSFGFGGTNATLCIA 454
Cdd:PLN02787 515 LdikVALSNSFGFGGHNSSILFA 537
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 140-453 2.32e-93

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 285.85  E-value: 2.32e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 140 QVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRL 219
Cdd:PRK14691  25 QERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRM 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 220 IAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NPDPKLACRPFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYA 297
Cdd:PRK14691 105 IRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLA 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 298 EVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAAENRAIKRLFRDhARALAISSTK 377
Cdd:PRK14691 185 EIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITSTK 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213972556 378 GATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTE-AEFDLNYVPLEAQewkTEGRCIGLTNSFGFGGTNATLCI 453
Cdd:PRK14691 264 SATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDpAAKGLNIIAGNAQ---PHDMTYALSNGFGFAGVNASILL 337
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
39-453 2.26e-90

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 280.34  E-value: 2.26e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVG-DEYKSIPCSVAAFVPrgsdkgQFNEQNFVSKSDAKSMSSPTI 117
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEwDRYDGLNTRLAAPID------DFELPAHYTRKKIRSMGRVSL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 118 MAVGAAELALKDSGwypkLEADQV----ATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRY 193
Cdd:PRK09116  76 MATRASELALEDAG----LLGDPIltdgRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 194 KLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDScISPLSLAGFSRARALST-NPDPKLACRPFHPERDGFV 272
Cdd:PRK09116 152 GLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTrNDAPELTPRPFDANRDGLV 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 273 MGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGalRCMAAAVKDAGVSPDQISYVNAHATSTPLG 352
Cdd:PRK09116 231 IGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRG 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 353 DAAENRAIKRLFRDHaraLAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEF-DLNYVPLEAQEWKT 431
Cdd:PRK09116 309 DIAESQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDT 385

                        410       420
                 ....*....|....*....|..
gi 213972556 432 EgrcIGLTNSFGFGGTNATLCI 453
Cdd:PRK09116 386 E---YVMSNNFAFGGINTSLIF 404
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
39-451 9.71e-87

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 271.16  E-value: 9.71e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVsvVGDEYKSI--PCSVAafvprGSDKgqFNEQNFVSKSDAKSMSSPT 116
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT--FSPEFAEMgmRSQVW-----GNVK--LDPTGLIDRKVMRFMGDAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 117 IMAVGAAELALKDSGwypkLEADQVA---TGVAIGMG-MVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIR 192
Cdd:PRK07967  73 AYAYLAMEQAIADAG----LSEEQVSnprTGLIAGSGgGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 193 YKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAgFSRARALST--NPDPKLACRPFHPERDG 270
Cdd:PRK07967 149 FKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTkyNDTPEKASRAYDANRDG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 271 FVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITApdPEGEGALRCMAAAVkdAGVSPDqISYVNAHATSTP 350
Cdd:PRK07967 228 FVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMAL--ATVDTP-IDYINTHGTSTP 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 351 LGDAAENRAIKRLFRDhaRALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEF-DLNYV--PLEAQ 427
Cdd:PRK07967 303 VGDVKELGAIREVFGD--KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVteTTDNA 380

                        410       420
                 ....*....|....*....|....
gi 213972556 428 EWKTEgrcigLTNSFGFGGTNATL 451
Cdd:PRK07967 381 ELTTV-----MSNSFGFGGTNATL 399
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
41-451 4.56e-86

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 269.68  E-value: 4.56e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  41 VVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGD--EYKSIPCSVAAFVPRGSDKGqfneqnfVSKSDAKSMSSPTIM 118
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPfvEEFDLPVRIGGHLLEEFDHQ-------LTRVELRRMSYLQRM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 119 AVGAAELALKDSGwYPKLEADQVAtgVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGP 198
Cdd:PRK07910  87 STVLGRRVWENAG-SPEVDTNRLM--VSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 199 NHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARA-LST-NPDPKLACRPFHPERDGFVMGEG 276
Cdd:PRK07910 164 VITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTnNDDPAGACRPFDKDRDGFVFGEG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 277 AAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAAE 356
Cdd:PRK07910 244 GALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAE 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 357 NRAIKRLFRDHaRAlAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVpleAQEWKTEGRCI 436
Cdd:PRK07910 324 GKAINNALGGH-RP-AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVV---AGEPRPGNYRY 398

                        410
                 ....*....|....*
gi 213972556 437 GLTNSFGFGGTNATL 451
Cdd:PRK07910 399 AINNSFGFGGHNVAL 413
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
40-455 2.65e-83

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 261.14  E-value: 2.65e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  40 RVVITGIGLVTPLGVGTQlVWDRLLRGESGIVSVVG-DEYKSIPCSVAAFVPRgsdkgqfneqnfvsksdakSMSSPTIM 118
Cdd:PRK05952   3 KVVVTGIGLVSALGDLEQ-SWQRLLQGKSGIKLHQPfPELPPLPLGLIGNQPS-------------------SLEDLTKT 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 119 AVGAAelaLKDSGWYPKLEAdqvaTGVAIGmgmvplevvSETALMFQ-----TKGY-SKVSPFFVPK------ILINMAA 186
Cdd:PRK05952  63 VVTAA---LKDAGLTPPLTD----CGVVIG---------SSRGCQGQweklaRQMYqGDDSPDEELDlenwldTLPHQAA 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 187 GQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnpdpKLACRPFHP 266
Cdd:PRK05952 127 IAAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAYPFDR 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 267 ERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHA 346
Cdd:PRK05952 202 QREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHG 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 347 TSTPLGDAAENRAIKRLFrdhARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDctEAEFDLNYVpLEA 426
Cdd:PRK05952 282 TATRLNDQREANLIQALF---PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQ--EPEFDLNFV-RQA 355

                        410       420
                 ....*....|....*....|....*....
gi 213972556 427 QEWKTEGrciGLTNSFGFGGTNATLCIAG 455
Cdd:PRK05952 356 QQSPLQN---VLCLSFGFGGQNAAIALGK 381
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 39-451 4.16e-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: 251.20  E-value: 4.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLV---WDRLLRGESGIvSVVGDEYKSIPCSVAAFVPRGSDKGQFNEQNFVsksdaksMSSP 115
Cdd:cd00828    1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGI-APVARLKSRFDRGVAGQIPTGDIPGWDAKRTGI-------VDRT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 116 TIMAVGAAELALKDSGWYPKLEADQVATGVAIGMGMVplevvSETALMFQTKGYS-KVSPFFVPK--ILINMAAGQVSIR 192
Cdd:cd00828   73 TLLALVATEEALADAGITDPYEVHPSEVGVVVGSGMG-----GLRFLRRGGKLDArAVNPYVSPKwmLSPNTVAGWVNIL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 193 YKLK-GPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDScISPLSLAGFSRARALSTNPD-PKLACRPFHPERDG 270
Cdd:cd00828  148 LLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEePEEMSRPFDETRDG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 271 FVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPeGEGALRCMAAAVKDAGVSPDQISYVNAHATSTP 350
Cdd:cd00828  227 FVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTP 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 351 LGDAAENRAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQEWK 430
Cdd:cd00828  306 ANDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLN 385

                        410       420
                 ....*....|....*....|.
gi 213972556 431 TEGRCiGLTNSFGFGGTNATL 451
Cdd:cd00828  386 LKVRA-ALVNAFGFGGSNAAL 405
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
41-455 4.57e-78

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 249.16  E-value: 4.57e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  41 VVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVprgsdkgqfneqNFVsksDAKSMSSPTI--- 117
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------------DFL---PESPFGASALsea 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 118 MAVGAAELALKDSG--------------------WYPKLEADQVAtgvaigmgmvPLEVVSETALMFQTKGYSKVSPFFv 177
Cdd:PRK06501  78 LARLAAEEALAQAGigkgdfpgplflaappveleWPARFALAAAV----------GDNDAPSYDRLLRAARGGRFDALH- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 178 PKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNPD- 256
Cdd:PRK06501 147 ERFQFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDp 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 257 PKLACRPFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSP 336
Cdd:PRK06501 227 PEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTP 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 337 DQISYVNAHATSTPLGDAAENRAIKRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAE 416
Cdd:PRK06501 307 EQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPA 386

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 213972556 417 FDLNYVPLEAQEWKTEGRcigLTNSFGFGGTNATLCIAG 455
Cdd:PRK06501 387 IPLDVVPNVARDARVTAV---LSNSFGFGGQNASLVLTA 422
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
195-451 8.88e-74

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 237.05  E-value: 8.88e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 195 LKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDScISPLSLAGFSRARALSTNPdpklaCRPFHPERDGFVMG 274
Cdd:PRK09185 149 LSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSPQP-----CRPFSANRDGINIG 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 275 EGAAVLVLE-EHEHAVQrgariyaeVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGD 353
Cdd:PRK09185 223 EAAAFFLLErEDDAAVA--------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLND 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 354 AAENRAIKRLFRDHaraLAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAQewKTEG 433
Cdd:PRK09185 295 AMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQ--ALAI 369

                        250
                 ....*....|....*...
gi 213972556 434 RCIgLTNSFGFGGTNATL 451
Cdd:PRK09185 370 RYV-LSNSFAFGGNNCSL 386
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 40-449 1.18e-70

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: 229.75  E-value: 1.18e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  40 RVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSV------VGDEYKSIPCSVAAFVPRG---SDKGQFNEQNF-VSKSDA 109
Cdd:cd00833    2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIpedrwdADGYYPDPGKPGKTYTRRGgflDDVDAFDAAFFgISPREA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 110 KSMSsPT--IMAVGAAElALKDSGwYPKLEADQVATGVAIGMGmvplevvSETALMFQTKGYSKVSPFFVPKILINMAAG 187
Cdd:cd00833   82 EAMD-PQqrLLLEVAWE-ALEDAG-YSPESLAGSRTGVFVGAS-------SSDYLELLARDPDEIDAYAATGTSRAFLAN 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 188 QVSIRYKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnPDPKlaCRPFHPE 267
Cdd:cd00833  152 RISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS--PDGR--CRPFDAD 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 268 RDGFVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLS--GDAGHITAPDPEGEGALrcMAAAVKDAGVSPDQISYVNAH 345
Cdd:cd00833  228 ADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRTKGITAPSGEAQAAL--IRRAYARAGVDPSDIDYVEAH 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 346 ATSTPLGDAAENRAIKRLF---RDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLD----CTEAEFD 418
Cdd:cd00833  306 GTGTPLGDPIEVEALAKVFggsRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFEtpnpKIDFEES 385

                        410       420       430
                 ....*....|....*....|....*....|...
gi 213972556 419 LNYVPLEAQEWKTEG--RCIGLtNSFGFGGTNA 449
Cdd:cd00833  386 PLRVPTEARPWPAPAgpRRAGV-SSFGFGGTNA 417
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 40-454 6.14e-62

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 206.81  E-value: 6.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  40 RVVITGIGLVTPLGVGTQLVWDRLLRGESGIvSVVGDEYKSIPCSVAAFVPR---GSDKGQFNEQNFVSKSDAKSMSSPT 116
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAF-GVMRRPGRQVPDDAGAGLASafiGAELDSLALPERLDAKLLRRASLSA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 117 IMAVGAAELALKDSGWYPkleADQVATGVAIGMGMVPLEvvsETALMFQTkgYSKVSPFFVPK-ILINM---AAGQVSIR 192
Cdd:PRK07103  82 QAALAAAREAWRDAALGP---VDPDRIGLVVGGSNLQQR---EQALVHET--YRDRPAFLRPSyGLSFMdtdLVGLCSEQ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 193 YKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNP---DPKLACRPFHPERD 269
Cdd:PRK07103 154 FGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfadEPEAACRPFDQDRD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 270 GFVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEgaLRCMAAAVKDAGVSPDQISYVNAHATST 349
Cdd:PRK07103 234 GFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGS 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 350 PLGDAAENRAIKRLFRDHARalaISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDcTEAEFDLNYVPLEAQEW 429
Cdd:PRK07103 312 PLGDETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLD-EPIDERFRWVGSTAESA 387

                        410       420
                 ....*....|....*....|....*
gi 213972556 430 KTEgrcIGLTNSFGFGGTNATLCIA 454
Cdd:PRK07103 388 RIR---YALSLSFGFGGINTALVLE 409
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 116-451 3.82e-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: 191.70  E-value: 3.82e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 116 TIMAVGAAELALKDSGWYPKLEADQVATGVAIGMGMVPLEVVSETALMFQTKGYSKVSPFFVPkilinmAAGQVSIRYKL 195
Cdd:cd00825   12 SILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG------ASGQIATPLGI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 196 KGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnpdPKLACRPFHPERDGFVMGE 275
Cdd:cd00825   86 HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST----PEKASRTFDAAADGFVFGD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 276 GAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAA 355
Cdd:cd00825  162 GAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 356 ENRAIKRLFRDHARalAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLdcteAEFDLNYVPLEAQEWKTEGRC 435
Cdd:cd00825  242 ELKLLRSEFGDKSP--AVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHI----EELDEAGLNIVTETTPRELRT 315

                        330
                 ....*....|....*.
gi 213972556 436 iGLTNSFGFGGTNATL 451
Cdd:cd00825  316 -ALLNGFGLGGTNATL 330
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 39-288 9.91e-56

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: 185.53  E-value: 9.91e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGD-----EYKSIPCSVAAFVPRG----SDKGQFNEQNF-VSKSD 108
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAGKIYTKwgglDDIFDFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  109 AKSMSSPTIMAVGAAELALKDSGWYPKlEADQVATGVAIGMGMvplEVVSETALMFQTKGYSKVSPFFVPKIlINMAAGQ 188
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPD-SLDGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  189 VSIRYKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNpDPklaCRPFHPER 268
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231

                         250       260
                  ....*....|....*....|
gi 213972556  269 DGFVMGEGAAVLVLEEHEHA 288
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 39-451 8.52e-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: 184.87  E-value: 8.52e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  39 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKSIPCSVAAFVPrGSDKGQFNEQNFVSKSDAKsmsspTIM 118
Cdd:cd00832    1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVP-DFDAAEHLPGRLLPQTDRM-----TRL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 119 AVGAAELALKDSGWYP-KLEADQVATGVAIGMGMVPLEVVSETALMfqTKGYSKVSPFFVPKILINMAAGQVSIRYKLKG 197
Cdd:cd00832   75 ALAAADWALADAGVDPaALPPYDMGVVTASAAGGFEFGQRELQKLW--SKGPRHVSAYQSFAWFYAVNTGQISIRHGMRG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 198 PNHSVSTACTTGAHAVGDSFRLIAHGdADVMVAGGTDSCISPLSLAGFSRARALSTNPDPKLACRPFHPERDGFVMGEGA 277
Cdd:cd00832  153 PSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEGG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 278 AVLVLEEHEHAVQRGARIYAEVLGYGLSGDaghitaPDP---EGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDA 354
Cdd:cd00832  232 AILVLEDAAAARERGARVYGEIAGYAATFD------PPPgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDR 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 355 AENRAIKRLFrdHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDCTEAEFDLNYVPLEAqewktegR 434
Cdd:cd00832  306 AEAAALAAVF--GPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRP-------R 376

                        410       420
                 ....*....|....*....|.
gi 213972556 435 CIGLTNSF----GFGGTNATL 451
Cdd:cd00832  377 PAALRTALvlarGRGGFNSAL 397
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 126-449 1.73e-53

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 193.55  E-value: 1.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  126 ALKDSGwYPKLEADQVATGVAIGMGMvplevvsETALMFQTKGYSKVSPFFVPKILINMAAGQVSIRYKLKGPNHSVSTA 205
Cdd:COG3321   102 ALEDAG-YDPESLAGSRTGVFVGASS-------NDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  206 CTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnPDPKlaCRPFHPERDGFVMGEGAAVLVLEEH 285
Cdd:COG3321   174 CSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS--PDGR--CRAFDADADGYVRGEGVGVVVLKRL 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  286 EHAVQRGARIYAEVLGYGLSGDaGH---ITAPDPEGEGALrcMAAAVKDAGVSPDQISYVNAHATSTPLGDAAENRAIKR 362
Cdd:COG3321   250 SDALRDGDRIYAVIRGSAVNQD-GRsngLTAPNGPAQAAV--IRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTA 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  363 LF---RDHARALAISSTKGATGHLLGAAGAveAAF--TALACYHHKLPPTLNLDCTEAEFDLN----YVPLEAQEWKTEG 433
Cdd:COG3321   327 AFgqgRPADQPCAIGSVKSNIGHLEAAAGV--AGLikAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTELRPWPAGG 404

                         330
                  ....*....|....*...
gi 213972556  434 --RCIGLtNSFGFGGTNA 449
Cdd:COG3321   405 gpRRAGV-SSFGFGGTNA 421
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 296-411 9.27e-46

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: 154.65  E-value: 9.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  296 YAEVLGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVNAHATSTPLGDAAENRAIKRLFRDHAR--ALAI 373
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqPLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 213972556  374 SSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLD 411
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 178-448 1.42e-36

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: 143.61  E-value: 1.42e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   178 PKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNPDp 257
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   258 klaCRPFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDA--GHITAPDPEGEGalRCMAAAVKDAGVS 335
Cdd:TIGR02813  257 ---IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQA--KALKRAYDDAGFA 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   336 PDQISYVNAHATSTPLGDAAENRAIKRLF---RDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLNLDC 412
Cdd:TIGR02813  332 PHTCGLIEAHGTGTAAGDVAEFGGLVSVFsqdNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQ 411

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 213972556   413 TEAEFDLNYVPL----EAQEW--KTEG--RCIGLTnSFGFGGTN 448
Cdd:TIGR02813  412 PNPKLDIENSPFylntETRPWmqREDGtpRRAGIS-SFGFGGTN 454
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 185-453 1.03e-32

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: 124.48  E-value: 1.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 185 AAGQVSIRYKLK-GPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCisplslagfsraralstnpdpklacrp 263
Cdd:cd00327   46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF--------------------------- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 264 fhperdgfVMGEGAAVLVLEEHEHAVQRGARIYAEVLGYGLSGDaGHITAPDPEGEGALRCMAAAVKDAGVSPDQISYVN 343
Cdd:cd00327   99 --------VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFD-GASMVPAVSGEGLARAARKALEGAGLTPSDIDYVE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 344 AHATSTPLGDAAENRAIKRLFRDHarALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTlnldcteaefdlnyvp 423
Cdd:cd00327  170 AHGTGTPIGDAVELALGLDPDGVR--SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------- 231

                        250       260       270
                 ....*....|....*....|....*....|
gi 213972556 424 leaqewKTEGRCiGLTNSFGFGGTNATLCI 453
Cdd:cd00327  232 ------PREPRT-VLLLGFGLGGTNAAVVL 254
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 201-449 6.13e-29

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: 115.12  E-value: 6.13e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   201 SVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnPDPKlaCRPFHPERDGFVMGEGAAVL 280
Cdd:smart00825  92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS--PDGR--CKTFDASADGYVRGEGVGVV 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   281 VLEEHEHAVQRGARIYAEVLGYGL--SGDAGHITAPDPEGegalrcmaaavkdagvspdQisyvnahatstplgdaaenr 358
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA-------------------Q-------------------- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556   359 aikrlfrdharaLAISSTKGATGHLLGAAGAveAAF--TALACYHHKLPPTLNLDCTEAEFDLN----YVPLEAQEWKTE 432
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPP 274

                          250
                   ....*....|....*....
gi 213972556   433 G--RCIGLtNSFGFGGTNA 449
Cdd:smart00825 275 GrpRRAGV-SSFGFGGTNA 292
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
37-409 1.64e-17

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 83.85  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556  37 SRRRVVITGIGLVTPLGVGTQLVWDRLlrgESGIVSVVGDEYKSIPCSVAAFVPRGSDkgqfneQNFVSKSDAKSMSSPT 116
Cdd:PRK06519   4 QPNDVVITGIGLVSSLGEGLDAHWNAL---SAGRPQPNVDTETFAPYPVHPLPEIDWS------QQIPKRGDQRQMETWQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 117 IMAVGAAELALKDSGwypkLEADQVATG-----VAIGMGMVPLEV----------VSETALMFQTKGYSKVSPFFVPKIL 181
Cdd:PRK06519  75 RLGTYAAGLALDDAG----IKGNEELLStmdmiVAAGGGERDIAVdtailnearkRNDRGVLLNERLMTELRPTLFLAQL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 182 INMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNPdpklac 261
Cdd:PRK06519 151 SNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKGG------ 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 262 rpFHP-------ERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEvlgygLSGDAGHITAPDPegeGAL-RCMAAAVKDAG 333
Cdd:PRK06519 225 --WAPvwsrggeDGGGFILGSGGAFLVLESREHAEARGARPYAR-----ISGVESDRARRAP---GDLeASLERLLKPAG 294

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 213972556 334 VSPDQiSYVNAHATSTPLGDAAEnraikRLFRDHARALAISSTKGATGHLLGAAGAVEAAFTALACYHHKLPPTLN 409
Cdd:PRK06519 295 GLAAP-TAVISGATGAHPATAEE-----KAALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPPFD 364
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 209-342 2.86e-08

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 55.41  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 209 GAHAVGDSFRLIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNPDPklacrpfhperDGFVMGEGAAVLVLEEHEHA 288
Cdd:PRK06147 136 GAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNS-----------NGFIPGEAAAAVLLGRPAGG 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213972556 289 VQRGARIYAevLGYGL--SGDAGHITAPdPEGEGALRCMAAAVKDAGVSPDQISYV 342
Cdd:PRK06147 205 EAPGLPLLG--LGLGRepAPVGESEDLP-LRGDGLTQAIRAALAEAGCGLEDMDYR 257
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 198-277 2.06e-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: 43.52  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 198 PNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDSC-----ISPLSLAGFSR-ARALSTNPDPKLACRpfhpeRDGF 271
Cdd:COG0183   80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMsrapmLLPKARWGYRMnAKLVDPMINPGLTDP-----YTGL 154


                 ....*.
gi 213972556 272 VMGEGA 277
Cdd:COG0183  155 SMGETA 160
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 198-277 1.58e-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: 40.54  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972556 198 PNHSVSTACTTGAHAVGDSFRLIAHGDADVMVAGGTDScIS--PLSLAGFSRARALSTNPDPKLACRPFHPERDGFVMGE 275
Cdd:cd00751   76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVES-MSraPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGI 154


                 ..
gi 213972556 276 GA 277
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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