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Conserved domains on  [gi|490458877|ref|WP_004329552|]
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MULTISPECIES: beta-ketoacyl-ACP synthase II [Alistipes]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase family protein( domain architecture ID 11416750)

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:  25456814|11969206
SCOP:  3000122

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 4-415 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: 677.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGdGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:COG0304   81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEK-GPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVST 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:COG0304  160 ACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:COG0304  240 ELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:COG0304  320 FGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECD--LDYVPNEAREAKIDYALSNSFGF 397

                        410
                 ....*....|..
gi 490458877 404 GGHNSTVIFRKI 415
Cdd:COG0304  398 GGHNASLVFKRY 409
 
Name Accession Description Interval E-value
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 4-415 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: 677.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGdGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:COG0304   81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEK-GPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVST 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:COG0304  160 ACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:COG0304  240 ELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:COG0304  320 FGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECD--LDYVPNEAREAKIDYALSNSFGF 397

                        410
                 ....*....|..
gi 490458877 404 GGHNSTVIFRKI 415
Cdd:COG0304  398 GGHNASLVFKRY 409
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 4-413 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: 675.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877    4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGdGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEK-GPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:TIGR03150 160 ACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:TIGR03150 240 ELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:TIGR03150 320 FGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECD--LDYVPNEAREAKIDYALSNSFGF 397

                         410
                  ....*....|
gi 490458877  404 GGHNSTVIFR 413
Cdd:TIGR03150 398 GGTNASLVFK 407
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
4-415 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 635.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:PRK07314   2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGdGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:PRK07314  82 QAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEK-GPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECD--LDYVPNEARERKIDYALSNSFGF 398

                        410
                 ....*....|..
gi 490458877 404 GGHNSTVIFRKI 415
Cdd:PRK07314 399 GGTNASLVFKRY 410
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 4-412 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: 616.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFfDECLGYAAGDGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:cd00834   81 EALADAGLDPEELDPERIGVVIGSGIGGLATI-EEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVST 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:cd00834  160 ACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:cd00834  240 SLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:cd00834  320 FGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD--LDYVPNEAREAPIRYALSNSFGF 397


                 ....*....
gi 490458877 404 GGHNSTVIF 412
Cdd:cd00834  398 GGHNASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 4-248 6.55e-53

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: 177.06  E-value: 6.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877    4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPI--THFDAEKF-----------KTKFACEVKNYDWTQHFDR---KE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydppsriagkiYTKWGGLDDIFDFDPLFFGispRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   68 VRKYDLFTQYALIAATQAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTffdecLGYAAGDGTPRF-SPFFIPRMIAdIAAG 146
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAA-----LLLLDEDGGPRRgSPFAVGTMPS-VIAG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  147 YISIKYGFMGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTrnDDPVHASRPFDk 226
Cdd:pfam00109 155 RISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA- 231

                         250       260
                  ....*....|....*....|..
gi 490458877  227 drDGFVIGEGAGALILEEYEHA 248
Cdd:pfam00109 232 --DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 152-411 3.10e-20

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: 90.08  E-value: 3.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   152 YGFMGPNYC-TV-SACASSNHGLIDSFNAIRFGVADVMVAGGseaaVN---EPSVG-GFNSMQALStrnddPVHASRPFD 225
Cdd:smart00825  82 VGVSSSDYSvTVdTACSSSLVALHLACQSLRSGECDMALAGG----VNlilSPDTFvGLSRAGMLS-----PDGRCKTFD 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   226 KDRDGFVIGEGAGALILEEYEHAKARGAKIYCEMVG-----GGRSADayhFTAPHPEGkgamksmrdaikdagikpedid 300
Cdd:smart00825 153 ASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGsavnqDGRSNG---ITAPSGPA---------------------- 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   301 yvnvhgtstpagdlpelkalhgvlgdHIYdvnISSTKSMTGHLLGAAGaVEALA-CIFAINNGVIPPTINNENLDPEIDP 379
Cdd:smart00825 208 --------------------------QLL---IGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDL 257

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 490458877   380 -RLNLTLNK-----AQKRDVKCAMSNTFGFGGHNSTVI 411
Cdd:smart00825 258 eESPLRVPTeltpwPPPGRPRRAGVSSFGFGGTNAHVI 295
 
Name Accession Description Interval E-value
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 4-415 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: 677.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGdGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:COG0304   81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEK-GPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVST 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:COG0304  160 ACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:COG0304  240 ELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:COG0304  320 FGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECD--LDYVPNEAREAKIDYALSNSFGF 397

                        410
                 ....*....|..
gi 490458877 404 GGHNSTVIFRKI 415
Cdd:COG0304  398 GGHNASLVFKRY 409
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 4-413 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: 675.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877    4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGdGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEK-GPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:TIGR03150 160 ACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:TIGR03150 240 ELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:TIGR03150 320 FGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECD--LDYVPNEAREAKIDYALSNSFGF 397

                         410
                  ....*....|
gi 490458877  404 GGHNSTVIFR 413
Cdd:TIGR03150 398 GGTNASLVFK 407
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
4-415 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 635.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:PRK07314   2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGdGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:PRK07314  82 QAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEK-GPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECD--LDYVPNEARERKIDYALSNSFGF 398

                        410
                 ....*....|..
gi 490458877 404 GGHNSTVIFRKI 415
Cdd:PRK07314 399 GGTNASLVFKRY 410
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 4-412 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: 616.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFfDECLGYAAGDGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:cd00834   81 EALADAGLDPEELDPERIGVVIGSGIGGLATI-EEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVST 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:cd00834  160 ACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:cd00834  240 SLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:cd00834  320 FGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD--LDYVPNEAREAPIRYALSNSFGF 397


                 ....*....
gi 490458877 404 GGHNSTVIF 412
Cdd:cd00834  398 GGHNASLVF 406
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-414 1.92e-174

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 493.75  E-value: 1.92e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   1 MTERRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKN--------YDWTQHFDRKEVRKYD 72
Cdd:PRK06333   1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  73 LFTQYALIAATQAVEDSGLDLEK-EDLEQIGVIWSSGIGGLKTFfDECLGYAAGDGTPRFSPFFIPRMIADIAAGYISIK 151
Cdd:PRK06333  81 RFILFAMAAAKEALAQAGWDPDTlEDRERTATIIGSGVGGFPAI-AEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 152 YGFMGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTR-NDDPVHASRPFDKDRDG 230
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 231 FVIGEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTP 310
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 311 AGDLPELKALHGVLGdHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDPrLNLTLNKAQK 390
Cdd:PRK06333 320 VGDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEG-LDVVANKARP 397

                        410       420
                 ....*....|....*....|....
gi 490458877 391 RDVKCAMSNTFGFGGHNSTVIFRK 414
Cdd:PRK06333 398 MDMDYALSNGFGFGGVNASILFRR 421
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 4-415 8.45e-164

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 466.13  E-value: 8.45e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAgDGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVS 163
Cdd:PRK08439  82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFE-KGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 164 ACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGALILE 243
Cdd:PRK08439 161 ACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 244 EYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEgkGAMKSMRDAIKDAGIKPedIDYVNVHGTSTPAGDLPELKALHGV 323
Cdd:PRK08439 241 EYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKEL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 324 LGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKCAMSNTFGF 403
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECD--LDYIPNVARKAELNVVMSNSFGF 394

                        410
                 ....*....|..
gi 490458877 404 GGHNSTVIFRKI 415
Cdd:PRK08439 395 GGTNGVVIFKKV 406
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 14-415 5.07e-153

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 439.51  E-value: 5.07e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  14 INPLGNNIAEFFSNLEKGVSGAAPITHFDAE----------------KFKTKFACEVKNYDWTQHfDRKEVRKYDLFTQY 77
Cdd:PTZ00050   2 VTPLGVGAESTWEALIAGKSGIRKLTEFPKFlpdcipeqkalenlvaAMPCQIAAEVDQSEFDPS-DFAPTKRESRATHF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  78 ALIAATQAVEDSGLD-LEKEDLEQIGVIWSSGIGGLkTFFDECLGYAAGDGTPRFSPFFIPRMIADIAAGYISIKYGFMG 156
Cdd:PTZ00050  81 AMAAAREALADAKLDiLSEKDQERIGVNIGSGIGSL-ADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 157 PNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTR-NDDPVHASRPFDKDRDGFVIGE 235
Cdd:PTZ00050 160 PSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVMGE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 236 GAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAG-IKPEDIDYVNVHGTSTPAGDL 314
Cdd:PTZ00050 240 GAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIGDK 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 315 PELKALHGVLGDH-IYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQ--KR 391
Cdd:PTZ00050 320 IELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECD--LNLVQGKTAhpLQ 397

                        410       420
                 ....*....|....*....|....
gi 490458877 392 DVKCAMSNTFGFGGHNSTVIFRKI 415
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
1-415 5.04e-140

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 405.93  E-value: 5.04e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   1 MTERRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALI 80
Cdd:PRK08722   1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  81 AATQAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFfdECLGYAAGDGTPR-FSPFFIPRMIADIAAGYISIKYGFMGPNY 159
Cdd:PRK08722  81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLI--EAGHQALVEKGPRkVSPFFVPSTIVNMIAGNLSIMRGLRGPNI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 160 CTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGEGAGA 239
Cdd:PRK08722 159 AISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGM 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 240 LILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKA 319
Cdd:PRK08722 239 MVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 320 LHGVLGDH-IYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNEnlDPEIDPRLNLTLNKAQK-RDVKCAM 397
Cdd:PRK08722 319 IKRALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLD--DPEEGLDIDLVPHTARKvESMEYAI 396

                        410
                 ....*....|....*...
gi 490458877 398 SNTFGFGGHNSTVIFRKI 415
Cdd:PRK08722 397 CNSFGFGGTNGSLIFKKM 414
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 4-412 3.07e-137

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 399.94  E-value: 3.07e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPIT-------HFDAE-------KFKTKFACEVKNYDWTQHFDRK--- 66
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTqddlkmkSEDEEtqlytldQLPSRVAALVPRGTGPGDFDEElwl 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  67 EVRKYDLFTQYALIAATQAVEDSG-LDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGDGTpRFSPFFIPRMIADIAA 145
Cdd:PLN02836  86 NSRSSSRFIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLR-RLSPFFVPRILINMAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 146 GYISIKYGFMGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTR-NDDPVHASRPF 224
Cdd:PLN02836 165 GHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPF 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 225 DKDRDGFVIGEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNV 304
Cdd:PLN02836 245 DCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNA 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 305 HGTSTPAGDLPELKALHGVLGDHIYD--VNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDPRLn 382
Cdd:PLN02836 325 HATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGF- 403

                        410       420       430
                 ....*....|....*....|....*....|
gi 490458877 383 LTLNKAQKRDVKCAMSNTFGFGGHNSTVIF 412
Cdd:PLN02836 404 VPLTASKAMLIRAALSNSFGFGGTNASLLF 433
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 1-412 1.49e-133

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 393.96  E-value: 1.49e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   1 MTERRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALI 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  81 AATQAVEDSGL--DLEKE-DLEQIGVIWSSGIGGLKTFFD--ECLGYAagdgTPRFSPFFIPRMIADIAAGYISIKYGFM 155
Cdd:PLN02787 206 AGKKALADGGIteDVMKElDKTKCGVLIGSAMGGMKVFNDaiEALRIS----YRKMNPFCVPFATTNMGSAMLAMDLGWM 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 156 GPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDRDGFVIGE 235
Cdd:PLN02787 282 GPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGE 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 236 GAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLP 315
Cdd:PLN02787 362 GAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLK 441

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 316 ELKALHGVLGDHiYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDPRLnLTLNKAQKRDVKC 395
Cdd:PLN02787 442 EYQALMRCFGQN-PELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKV-LVGPKKERLDIKV 519

                        410
                 ....*....|....*..
gi 490458877 396 AMSNTFGFGGHNSTVIF 412
Cdd:PLN02787 520 ALSNSFGFGGHNSSILF 536
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
4-414 2.77e-108

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 324.70  E-value: 2.77e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGaapITHfdAEKFKTK-FACEVK---NYDWTQHFDRKEVRKYDLFTQYAL 79
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSG---ITF--SPEFAEMgMRSQVWgnvKLDPTGLIDRKVMRFMGDASAYAY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  80 IAATQAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGDGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNY 159
Cdd:PRK07967  77 LAMEQAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 160 CTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGgFNSMQALSTR-NDDPVHASRPFDKDRDGFVIGEGAG 238
Cdd:PRK07967 157 SISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 239 ALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAphPEGKGAMKSMRDAIkdAGIKpEDIDYVNVHGTSTPAGDLPELK 318
Cdd:PRK07967 236 VVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTPVGDVKELG 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 319 ALHGVLGDHIydVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDPrLNLTLNKAQKRDVKCAMS 398
Cdd:PRK07967 311 AIREVFGDKS--PAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAG-MPIVTETTDNAELTTVMS 387

                        410
                 ....*....|....*.
gi 490458877 399 NTFGFGGHNSTVIFRK 414
Cdd:PRK07967 388 NSFGFGGTNATLVFRR 403
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
4-413 3.30e-105

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 316.93  E-value: 3.30e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFD-AEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAA 82
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDrYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  83 TQAVEDSGLdLEKEDLE--QIGVIWSSGIGGLKTFFDecLGYAAGDGTPR-FSPFFIPRMIADIAAGYISIKYGFMGPNY 159
Cdd:PRK09116  82 ELALEDAGL-LGDPILTdgRMGIAYGSSTGSTDPIGA--FGTMLLEGSMSgITATTYVRMMPHTTAVNVGLFFGLKGRVI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 160 CTVSACASSNHGLIDSFNAIRFGVADVMVAGG------SEAAVnepsvggFNSMQALSTRNDDPVHASRPFDKDRDGFVI 233
Cdd:PRK09116 159 PTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGaeelcpTEAAV-------FDTLFATSTRNDAPELTPRPFDANRDGLVI 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 234 GEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEgkgAMK-SMRDAIKDAGIKPEDIDYVNVHGTSTPAG 312
Cdd:PRK09116 232 GEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAE---TMQiAMELALKDAGLAPEDIGYVNAHGTATDRG 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 313 DLPELKALHGVLGDHiydVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIdPRLNLTLNKAQKRD 392
Cdd:PRK09116 309 DIAESQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPAC-GALDYIMGEAREID 384

                        410       420
                 ....*....|....*....|.
gi 490458877 393 VKCAMSNTFGFGGHNSTVIFR 413
Cdd:PRK09116 385 TEYVMSNNFAFGGINTSLIFK 405
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
6-412 1.02e-96

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 295.77  E-value: 1.02e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   6 VVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVknydwtQHFDRKEVRKYDLFTQYALIAATQA 85
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------DFLPESPFGASALSEALARLAAEEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  86 VEDSGLD--------------LEKEDLEQIGVIWSSGigglktfFDECLGYA---AGDGTPRFSPFFIPRMIADIAAgYI 148
Cdd:PRK06501  87 LAQAGIGkgdfpgplflaappVELEWPARFALAAAVG-------DNDAPSYDrllRAARGGRFDALHERFQFGSIAD-RL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 149 SIKYGFMGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHASRPFDKDR 228
Cdd:PRK06501 159 ADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 229 DGFVIGEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTS 308
Cdd:PRK06501 239 DGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTS 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 309 TPAGDLPELKALHGVLGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKA 388
Cdd:PRK06501 319 TPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIP--LDVVPNVA 396

                        410       420
                 ....*....|....*....|....
gi 490458877 389 QKRDVKCAMSNTFGFGGHNSTVIF 412
Cdd:PRK06501 397 RDARVTAVLSNSFGFGGQNASLVL 420
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
6-414 8.06e-91

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 280.46  E-value: 8.06e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   6 VVVTGIGTINPLGNNIAEFFSNLEKGVSGaapITHFDaEKFKTKFACEVK-------NYDwtQHFDRKEVRKYDLFTQYA 78
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSG---IRTLD-DPFVEEFDLPVRigghlleEFD--HQLTRVELRRMSYLQRMS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  79 LIAATQAVEDSGLdlEKEDLEQIGVIWSSGIGGLKTFFDECLGYAAGdGTPRFSPFFIPRMIADIAAGYISI----KYGF 154
Cdd:PRK07910  88 TVLGRRVWENAGS--PEVDTNRLMVSIGTGLGSAEELVFAYDDMRAR-GLRAVSPLAVQMYMPNGPAAAVGLerhaKAGV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 155 MGPnyctVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQA-LSTRNDDPVHASRPFDKDRDGFVI 233
Cdd:PRK07910 165 ITP----VSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 234 GEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGD 313
Cdd:PRK07910 241 GEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGD 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 314 LPELKALHGVLGDHIYDVniSSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDV 393
Cdd:PRK07910 321 VAEGKAINNALGGHRPAV--YAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEID--LDVVAGEPRPGNY 396

                        410       420
                 ....*....|....*....|.
gi 490458877 394 KCAMSNTFGFGGHNSTVIFRK 414
Cdd:PRK07910 397 RYAINNSFGFGGHNVALAFGR 417
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 96-414 7.66e-89

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 272.76  E-value: 7.66e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  96 EDLEQIGVIWSSGIGGLKTFfDECLGYAAGDGTPRFSPFFIPRMIADIAAGYISIKYGFMGPNYCTVSACASSNHGLIDS 175
Cdd:PRK14691  23 EKQERTATIIGAGIGGFPAI-AHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 176 FNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTR-NDDPVHASRPFDKDRDGFVIGEGAGALILEEYEHAKARGAK 254
Cdd:PRK14691 102 VRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAK 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 255 IYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGVLGDHiYDVNIS 334
Cdd:PRK14691 182 PLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGES-NALAIT 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 335 STKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDPrLNLTLNKAQKRDVKCAMSNTFGFGGHNSTVIFRK 414
Cdd:PRK14691 261 STKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKG-LNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 5-414 1.74e-78

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 248.41  E-value: 1.74e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   5 RVVVTGIGTINPLGNNIAEFFSNLEKGVS--------GAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQ 76
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHafgvmrrpGRQVPDDAGAGLASAFIGAELDSLALPERLDAKLLRRASLSAQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  77 YALIAATQAVEDSGLDleKEDLEQIGVIwssgIGGLKTFFDE-CLGYAAGDGTPRFSP--FFIPRMIADIAaGYISIKYG 153
Cdd:PRK07103  83 AALAAAREAWRDAALG--PVDPDRIGLV----VGGSNLQQREqALVHETYRDRPAFLRpsYGLSFMDTDLV-GLCSEQFG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 154 FMGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRN--DDPVHASRPFDKDRDGF 231
Cdd:PRK07103 156 IRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 232 VIGEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKgaMKSMRDAIKDAGIKPEDIDYVNVHGTSTPA 311
Cdd:PRK07103 236 IYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGSPL 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 312 GDLPELKALHGVLGDHIYdvnISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTInneNLDPEIDPRLNLTLNKAQKR 391
Cdd:PRK07103 314 GDETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSR---NLDEPIDERFRWVGSTAESA 387

                        410       420
                 ....*....|....*....|...
gi 490458877 392 DVKCAMSNTFGFGGHNSTVIFRK 414
Cdd:PRK07103 388 RIRYALSLSFGFGGINTALVLER 410
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 4-410 1.76e-77

"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: 245.81  E-value: 1.76e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIA---EFFSNLEKGVSGAAPITHFdaekfKTKFACEVKNYDWTQHFDRKEVRKY---DLFTQY 77
Cdd:cd00828    1 SRVVITGIGVVSPHGEGCDeveEFWEALREGRSGIAPVARL-----KSRFDRGVAGQIPTGDIPGWDAKRTgivDRTTLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  78 ALIAATQAVEDSGL-DLEKEDLEQIGVIWSSGIGGLktffdECLGYAAGDGTPRFSPFFIPRMIADI--AAGYISIKYGF 154
Cdd:cd00828   76 ALVATEEALADAGItDPYEVHPSEVGVVVGSGMGGL-----RFLRRGGKLDARAVNPYVSPKWMLSPntVAGWVNILLLS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 155 M-GPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGgFNSMQALSTRNDDPVHASRPFDKDRDGFVI 233
Cdd:cd00828  151 ShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSG-FANMGALSTAEEEPEEMSRPFDETRDGFVE 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 234 GEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPeGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGD 313
Cdd:cd00828  230 AEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPAND 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 314 LPELKALHGVLGDHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDPRLNLTLNKAQKRDV 393
Cdd:cd00828  309 VAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKV 388

                        410
                 ....*....|....*..
gi 490458877 394 KCAMSNTFGFGGHNSTV 410
Cdd:cd00828  389 RAALVNAFGFGGSNAAL 405
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
6-412 9.98e-72

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 230.50  E-value: 9.98e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   6 VVVTGIGTINPLGNNIAEFFSNLEKGV-SGAAPITHFDAEKfkTKFACEVKNYDWTQ---HFDRKEVRKydlfTQYALIA 81
Cdd:PRK09185   4 VYISAFGATSALGRGLDAILAALRAGRaSGMRPCDFWLVDL--PTWVGEVVGVELPAlpaALAAFDCRN----NRLALLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  82 ATQ---AVEDSgldLEKEDLEQIGVIW---SSGIGglktffDECLGYAAGD-GTPRFSPFFIPRM-----IADIAAGYis 149
Cdd:PRK09185  78 LQQiepAVEAA---IARYGADRIGVVLgtsTSGIL------EGELAYRRRDpAHGALPADYHYAQqelgsLADFLRAY-- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 150 ikYGFMGPNYcTVS-ACASSNHGLIDSFNAIRFGVADVMVAGG----SEAAVNepsvgGFNSMQALSTrnddpvHASRPF 224
Cdd:PRK09185 147 --LGLSGPAY-TIStACSSSAKVFASARRLLEAGLCDAAIVGGvdslCRLTLN-----GFNSLESLSP------QPCRPF 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 225 DKDRDGFVIGEGAGALILEeyehaKARGAKIYceMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNV 304
Cdd:PRK09185 213 SANRDGINIGEAAAFFLLE-----REDDAAVA--LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINL 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 305 HGTSTPAGDLPELKALHGVLGDHiydVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDPrLNLt 384
Cdd:PRK09185 286 HGTATPLNDAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPP-LYL- 360

                        410       420
                 ....*....|....*....|....*...
gi 490458877 385 LNKAQKRDVKCAMSNTFGFGGHNSTVIF 412
Cdd:PRK09185 361 VENAQALAIRYVLSNSFAFGGNNCSLIF 388
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 4-411 2.33e-63

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: 208.75  E-value: 2.33e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRKEVRKYDLFTQYALIAAT 83
Cdd:cd00832    1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  84 QAVEDSGLDLEKEDLEQIGVIWSSGIGGLKtFFDECLGYAAGDGTPRFSPFfipRMIA---DIAAGYISIKYGFMGPnyc 160
Cdd:cd00832   81 WALADAGVDPAALPPYDMGVVTASAAGGFE-FGQRELQKLWSKGPRHVSAY---QSFAwfyAVNTGQISIRHGMRGP--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 161 tVSACASSNHGLIDSF----NAIRFGvADVMVAGGSEAAVNEPSVGGFNSMQALSTrNDDPVHASRPFDKDRDGFVIGEG 236
Cdd:cd00832  154 -SGVVVAEQAGGLDALaqarRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 237 AGALILEEYEHAKARGAKIYCEMVGGGRSADAyhftAPHP-EGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLP 315
Cdd:cd00832  231 GAILVLEDAAAARERGARVYGEIAGYAATFDP----PPGSgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRA 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 316 ELKALHGVLGDHiyDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDprLNLTLNKAQKRDVKC 395
Cdd:cd00832  307 EAAALAAVFGPR--GVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYG--LDLVTGRPRPAALRT 382

                        410
                 ....*....|....*.
gi 490458877 396 AMSNTFGFGGHNSTVI 411
Cdd:cd00832  383 ALVLARGRGGFNSALV 398
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 5-411 3.60e-63

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: 208.95  E-value: 3.60e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   5 RVVVTGIGTINPLGNNIAEFFSNLEKGVSG--AAPITHFDAEKFK----------TKFACEVKNYDwtqHFD-------R 65
Cdd:cd00833    2 PIAIVGMACRFPGAADPDEFWENLLEGRDAisEIPEDRWDADGYYpdpgkpgktyTRRGGFLDDVD---AFDaaffgisP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  66 KEVRKYD----LFtqyaLIAATQAVEDSGLDLEKEDLEQIGVIwssgIGGLKTFFDECLGYAAgdgtPRFSPFFIPRMIA 141
Cdd:cd00833   79 REAEAMDpqqrLL----LEVAWEALEDAGYSPESLAGSRTGVF----VGASSSDYLELLARDP----DEIDAYAATGTSR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 142 DIAAGYISIKYGFMGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALStrnddPVHAS 221
Cdd:cd00833  147 AFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRC 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 222 RPFDKDRDGFVIGEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAY--HFTAPHPEGKGAMksMRDAIKDAGIKPEDI 299
Cdd:cd00833  222 RPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEAQAAL--IRRAYARAGVDPSDI 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 300 DYVNVHGTSTPAGDLPELKALHGVLGDHIYDVN---ISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPE 376
Cdd:cd00833  300 DYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQpllIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPK 379

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 490458877 377 ID-PRLNLTLNKA-----QKRDVKCAMSNTFGFGGHNSTVI 411
Cdd:cd00833  380 IDfEESPLRVPTEarpwpAPAGPRRAGVSSFGFGGTNAHVI 420
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 73-411 4.96e-61

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: 200.94  E-value: 4.96e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  73 LFTQYALIAATQAVEDSGLDLEKEDLEQIGVIWSSGIGGLKtffdecLGYAAGDGTPRFSPFFIPRMIADIAAGYISIKY 152
Cdd:cd00825   10 YVSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPR------FQVFGADAMRAVGPYVVTKAMFPGASGQIATPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 153 GFMGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVnEPSVGGFNSMQALSTrnddPVHASRPFDKDRDGFV 232
Cdd:cd00825   84 GIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELA-APMDCEFDAMGALST----PEKASRTFDAAADGFV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 233 IGEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAG 312
Cdd:cd00825  159 FGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 313 DLPELKALHGVLGDHiyDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENLDPEIDPrlnlTLNKAQKRD 392
Cdd:cd00825  239 DVKELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLN----IVTETTPRE 312

                        330
                 ....*....|....*....
gi 490458877 393 VKCAMSNTFGFGGHNSTVI 411
Cdd:cd00825  313 LRTALLNGFGLGGTNATLV 331
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
5-414 1.55e-60

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 201.05  E-value: 1.55e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   5 RVVVTGIGTINPLGNnIAEFFSNLEKGVSGAApithfdaekfktkfacevknydWTQHFdrKEVRKYDLftqyALIAA-- 82
Cdd:PRK05952   3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIK----------------------LHQPF--PELPPLPL----GLIGNqp 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  83 -----------TQAVEDSGLDLEkedLEQIGVIWSSGIG-------GLKTFFdecLGYAAGDGTPRFSPF--FIPRMIAD 142
Cdd:PRK05952  54 ssledltktvvTAALKDAGLTPP---LTDCGVVIGSSRGcqgqwekLARQMY---QGDDSPDEELDLENWldTLPHQAAI 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 143 IAAGYISIKygfmGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRnddpvhASR 222
Cdd:PRK05952 128 AAARQIGTQ----GPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKT------GAY 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 223 PFDKDRDGFVIGEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYV 302
Cdd:PRK05952 198 PFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYI 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 303 NVHGTSTPAGDLPE---LKALHGvlgdhiYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTINNENldPEIDp 379
Cdd:PRK05952 278 HAHGTATRLNDQREanlIQALFP------HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFD- 348

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 490458877 380 rLNLtLNKAQKRDVKCAMSNTFGFGGHNSTVIFRK 414
Cdd:PRK05952 349 -LNF-VRQAQQSPLQNVLCLSFGFGGQNAAIALGK 381
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 4-248 6.55e-53

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: 177.06  E-value: 6.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877    4 RRVVVTGIGTINPLGNNIAEFFSNLEKGVSGAAPI--THFDAEKF-----------KTKFACEVKNYDWTQHFDR---KE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydppsriagkiYTKWGGLDDIFDFDPLFFGispRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   68 VRKYDLFTQYALIAATQAVEDSGLDLEKEDLEQIGVIWSSGIGGLKTffdecLGYAAGDGTPRF-SPFFIPRMIAdIAAG 146
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAA-----LLLLDEDGGPRRgSPFAVGTMPS-VIAG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  147 YISIKYGFMGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTrnDDPVHASRPFDk 226
Cdd:pfam00109 155 RISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA- 231

                         250       260
                  ....*....|....*....|..
gi 490458877  227 drDGFVIGEGAGALILEEYEHA 248
Cdd:pfam00109 232 --DGFVRGEGVGAVVLKRLSDA 251
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-411 2.22e-44

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 165.43  E-value: 2.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877    1 MTERRVVVTGIGTINPLGNNIAEFFSNLEKGVSGaapITHFDAE----------------KFKTKFACEVKNYDwtqHFD 64
Cdd:COG3321     1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDA---ITEVPADrwdadayydpdpdapgKTYVRWGGFLDDVD---EFD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   65 R-------KEVRKYD----LFtqyaLIAATQAVEDSGLDLEKEDLEQIGVIwsSGIGGLKtffdecLGYAAGDGTPRFSP 133
Cdd:COG3321    75 AlffgispREAEAMDpqqrLL----LEVAWEALEDAGYDPESLAGSRTGVF--VGASSND------YALLLLADPEAIDA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  134 FFIPRMIADIAAGYISIKYGFMGPNYcTV-SACASSnhgL--ID-SFNAIRFGVADVMVAGGseaaVN---EPSVG-GFN 205
Cdd:COG3321   143 YALTGNAKSVLAGRISYKLDLRGPSV-TVdTACSSS---LvaVHlACQSLRSGECDLALAGG----VNlmlTPESFiLFS 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  206 SMQALST--RnddpvhaSRPFDKDRDGFVIGEGAGALILEEYEHAKARGAKIYCEMVG-----GGRSAdayHFTAPHPEG 278
Cdd:COG3321   215 KGGMLSPdgR-------CRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGsavnqDGRSN---GLTAPNGPA 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  279 KGAMksMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGVLGDHIYDVN---ISSTKSMTGHLLGAAGAVEALAC 355
Cdd:COG3321   285 QAAV--IRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPADQpcaIGSVKSNIGHLEAAAGVAGLIKA 362

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490458877  356 IFAINNGVIPPTINNENLDPEID-PRLNLTLN------KAQKRDVKCAMSnTFGFGGHNSTVI 411
Cdd:COG3321   363 VLALRHGVLPPTLHFETPNPHIDfENSPFYVNtelrpwPAGGGPRRAGVS-SFGFGGTNAHVV 424
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 256-369 1.22e-43

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: 148.10  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  256 YCEMVGGGRSADAYHFTAPHPEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTPAGDLPELKALHGVLGDHIYD--VNI 333
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 490458877  334 SSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTIN 369
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLN 116
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 73-411 3.39e-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: 125.25  E-value: 3.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  73 LFTQYALIAATQAVEDSGLDlekedleqigviwSSGIGGLktffdeCLGYAAGDGtpRFSPffiprmiadiAAGYISIKY 152
Cdd:cd00327    6 TASELGFEAAEQAIADAGLS-------------KGPIVGV------IVGTTGGSG--EFSG----------AAGQLAYHL 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 153 GFM-GPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSEAavnepsvggfnsmqalstrnddpvhasrpfdkdrdgF 231
Cdd:cd00327   55 GISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------F 98

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 232 VIGEGAGALILEEYEHAKARGAKIYCEMVGGGRSAD-AYHFTAPhpEGKGAMKSMRDAIKDAGIKPEDIDYVNVHGTSTP 310
Cdd:cd00327   99 VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAV--SGEGLARAARKALEGAGLTPSDIDYVEAHGTGTP 176

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 311 AGDLPELKALHGVLGDHiyDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTinnenldpeidprlnltlnkaqK 390
Cdd:cd00327  177 IGDAVELALGLDPDGVR--SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------------------P 232

                        330       340
                 ....*....|....*....|.
gi 490458877 391 RDVKCAMSNTFGFGGHNSTVI 411
Cdd:cd00327  233 REPRTVLLLGFGLGGTNAAVV 253
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 137-407 8.40e-32

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: 128.58  E-value: 8.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   137 PRMIADIAAGYISIKYGFMGPNYCTVSACASSNHGLIDSFNAIRFGVADVMVAGGSeAAVNEPSV-GGFNSMQALSTRND 215
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGV-CTDNSPFMyMSFSKTPAFTTNED 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   216 dpvhaSRPFDKDRDGFVIGEGAGALILEEYEHAKARGAKIYCEMVGGGRSADAY--HFTAPHPEGKGamKSMRDAIKDAG 293
Cdd:TIGR02813  257 -----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQA--KALKRAYDDAG 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   294 IKPEDIDYVNVHGTSTPAGDLPELKALHGVLG---DHIYDVNISSTKSMTGHLLGAAGAVEALACIFAINNGVIPPTIN- 369
Cdd:TIGR02813  330 FAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINv 409

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 490458877   370 ---NENLDPEIDPrlnLTLNKA-----QKRD--VKCAMSNTFGFGGHN 407
Cdd:TIGR02813  410 dqpNPKLDIENSP---FYLNTEtrpwmQREDgtPRRAGISSFGFGGTN 454
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 152-411 3.10e-20

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: 90.08  E-value: 3.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   152 YGFMGPNYC-TV-SACASSNHGLIDSFNAIRFGVADVMVAGGseaaVN---EPSVG-GFNSMQALStrnddPVHASRPFD 225
Cdd:smart00825  82 VGVSSSDYSvTVdTACSSSLVALHLACQSLRSGECDMALAGG----VNlilSPDTFvGLSRAGMLS-----PDGRCKTFD 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   226 KDRDGFVIGEGAGALILEEYEHAKARGAKIYCEMVG-----GGRSADayhFTAPHPEGkgamksmrdaikdagikpedid 300
Cdd:smart00825 153 ASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGsavnqDGRSNG---ITAPSGPA---------------------- 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   301 yvnvhgtstpagdlpelkalhgvlgdHIYdvnISSTKSMTGHLLGAAGaVEALA-CIFAINNGVIPPTINNENLDPEIDP 379
Cdd:smart00825 208 --------------------------QLL---IGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDL 257

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 490458877   380 -RLNLTLNK-----AQKRDVKCAMSNTFGFGGHNSTVI 411
Cdd:smart00825 258 eESPLRVPTeltpwPPPGRPRRAGVSSFGFGGTNAHVI 295
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
1-355 8.58e-10

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 59.97  E-value: 8.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877   1 MTERRVVVTGIGTINPLGNNIAEFFSNLekgvSGAAPITHFDAEKFKTKFACEVKNYDWTQHFDRK-EVRKYDLFTQYAL 79
Cdd:PRK06519   3 MQPNDVVITGIGLVSSLGEGLDAHWNAL----SAGRPQPNVDTETFAPYPVHPLPEIDWSQQIPKRgDQRQMETWQRLGT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877  80 IAATQAVEDSGLDLEKEDLEQIGVIWSSGiGGLKTFFDECL---GYAAGDGTPRF---------SPFFIPRMIADIAAGY 147
Cdd:PRK06519  79 YAAGLALDDAGIKGNEELLSTMDMIVAAG-GGERDIAVDTAilnEARKRNDRGVLlnerlmtelRPTLFLAQLSNLLAGN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 148 ISIKYG-------FMGPNYCTVSAcassnhgLIDSFNAIRFGVADVMVAGGSEAAVNEPSVGGFNSMQALSTRNDDPVHA 220
Cdd:PRK06519 158 ISIVHKvtgssrtFMGEESAGVSA-------IEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKGGWAPVWS 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458877 221 SRPFDKDrdGFVIGEGAGALILEEYEHAKARGAKIYCEM--VGGGRSADAyhftaphpegKGAM-KSMRDAIKDAGIKPE 297
Cdd:PRK06519 231 RGGEDGG--GFILGSGGAFLVLESREHAEARGARPYARIsgVESDRARRA----------PGDLeASLERLLKPAGGLAA 298

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490458877 298 DiDYVNVHGTSTPAGDLPELKALHGVLgdhiyDVNISSTKSMTGHLLGA----AGAVEALAC 355
Cdd:PRK06519 299 P-TAVISGATGAHPATAEEKAALEAAL-----AGPVRGIGTLFGHTMEAqfplGLALAALSV 354
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 229-302 1.05e-04

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 43.86  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490458877 229 DGFVIGEGAGALILEEYEHAKARGAKIYCemVGGGRSADAYHFTAPHP-EGKGAMKSMRDAIKDAGIKPEDIDYV 302
Cdd:PRK06147 185 NGFIPGEAAAAVLLGRPAGGEAPGLPLLG--LGLGREPAPVGESEDLPlRGDGLTQAIRAALAEAGCGLEDMDYR 257
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 232-305 1.25e-04

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 43.79  E-value: 1.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490458877 232 VIGEGAGALIL--EEYehAKARGAKiYCEMVGGGRSADAYHFTAPHPEGK--GAMKSMRDAIKDAGIKPEDIDYVNVH 305
Cdd:cd00829  203 PVSDGAAAVVLasEER--ARELTDR-PVWILGVGAASDTPSLSERDDFLSldAARLAARRAYKMAGITPDDIDVAELY 277
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 286-310 7.07e-03

3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 38.17  E-value: 7.07e-03
                         10        20
                 ....*....|....*....|....*
gi 490458877 286 RDAIKDAGIKPEDIDYVnVHGTSTP 310
Cdd:COG0332   60 RKALEAAGIDPEDIDLI-IVATVTP 83
 
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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