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Conserved domains on  [gi|223972627|ref|NP_001138863|]
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3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial isoform 2 precursor [Homo sapiens]

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) ...
42-372 1.14e-140

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 TIGR03150:

Pssm-ID: 447866 [Multi-domain]  Cd Length: 407  Bit Score: 405.71  E-value: 1.14e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627   42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  122 AIGAAELAMKDSGWhPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:TIGR03150  75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  202 NHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------- 226
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGdadvmiaggaeaaitplgiagfaamkalstrnddpekasrpfdkdrdgfvmgega 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  227 -----------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 277
Cdd:TIGR03150 234 gvlvleelehakargakiyaeivgygmsgDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  278 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 357
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390
                         410
                  ....*....|....*
gi 223972627  358 LTNSFGFGGTNATLC 372
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
42-372 1.14e-140

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: 405.71  E-value: 1.14e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627   42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  122 AIGAAELAMKDSGWhPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:TIGR03150  75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  202 NHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------- 226
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGdadvmiaggaeaaitplgiagfaamkalstrnddpekasrpfdkdrdgfvmgega 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  227 -----------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 277
Cdd:TIGR03150 234 gvlvleelehakargakiyaeivgygmsgDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  278 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 357
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390
                         410
                  ....*....|....*
gi 223972627  358 LTNSFGFGGTNATLC 372
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
42-373 1.35e-140

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: 405.38  E-value: 1.35e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 122 AIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:cd00834   75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 202 NHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------- 226
Cdd:cd00834  154 NYTVSTACASGAHAIGDAARLIRLGradvviaggaealitpltlagfaalralstrnddpekasrpfdkdrdgfvlgega 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 -----------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 277
Cdd:cd00834  234 gvlvleslehakargakiyaeilgygassDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 278 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 357
Cdd:cd00834  314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390
                        410
                 ....*....|....*.
gi 223972627 358 LTNSFGFGGTNATLCI 373
Cdd:cd00834  391 LSNSFGFGGHNASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
42-371 3.41e-138

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 399.55  E-value: 3.41e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIvSLVGEEYKS-IPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTI 120
Cdd:PRK07314   2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGI-GPITHFDTSdLAVKIAGEVKD------FNPDDYMSRKEARRMDRFIQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 121 MAIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKG 200
Cdd:PRK07314  75 YGIAAAKQAVEDAGLEI-TEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 201 PNHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------ 226
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGdadvmvaggaeaaitplgiagfaaaralstrnddperasrpfdkdrdgfvmgeg 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 ------------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAE 276
Cdd:PRK07314 234 agilvleelehakargakiyaevvgygmtgDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAE 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 277 NKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfI 356
Cdd:PRK07314 314 TQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---Y 390
                        410
                 ....*....|....*
gi 223972627 357 GLTNSFGFGGTNATL 371
Cdd:PRK07314 391 ALSNSFGFGGTNASL 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
42-373 2.23e-135

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: 392.54  E-value: 2.23e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:COG0304   75 ALAAAREALADAGLDL-DEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 202 NHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------- 226
Cdd:COG0304  154 NYTVSTACASGAHAIGEAYRLIRRGradvmiaggaeaaitplglagfdalgalstrnddpekasrpfdkdrdgfvlgega 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 -----------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 277
Cdd:COG0304  234 gvlvleelehakargakiyaevvgygassDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 278 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 357
Cdd:COG0304  314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390
                        410
                 ....*....|....*.
gi 223972627 358 LTNSFGFGGTNATLCI 373
Cdd:COG0304  391 LSNSFGFGGHNASLVF 406
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
226-331 1.21e-41

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: 141.94  E-value: 1.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  226 GDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAY--ALAVSSTKGATGHL 303
Cdd:pfam02801  11 HDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqPLAIGSVKSNIGHL 90
                          90       100
                  ....*....|....*....|....*...
gi 223972627  304 LGAAGAVEAAFTTLACYYQKLPPTLNLD 331
Cdd:pfam02801  91 EGAAGAAGLIKVVLALRHGVIPPTLNLE 118
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
291-369 2.20e-11

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: 63.89  E-value: 2.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627   291 LAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWKTE--KRFIGLtNSF 362
Cdd:smart00825 209 LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPgrPRRAGV-SSF 285

                   ....*..
gi 223972627   363 GFGGTNA 369
Cdd:smart00825 286 GFGGTNA 292
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
42-372 1.14e-140

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: 405.71  E-value: 1.14e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627   42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  122 AIGAAELAMKDSGWhPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:TIGR03150  75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  202 NHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------- 226
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGdadvmiaggaeaaitplgiagfaamkalstrnddpekasrpfdkdrdgfvmgega 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  227 -----------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 277
Cdd:TIGR03150 234 gvlvleelehakargakiyaeivgygmsgDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  278 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 357
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390
                         410
                  ....*....|....*
gi 223972627  358 LTNSFGFGGTNATLC 372
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
42-373 1.35e-140

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: 405.38  E-value: 1.35e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 122 AIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:cd00834   75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 202 NHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------- 226
Cdd:cd00834  154 NYTVSTACASGAHAIGDAARLIRLGradvviaggaealitpltlagfaalralstrnddpekasrpfdkdrdgfvlgega 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 -----------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 277
Cdd:cd00834  234 gvlvleslehakargakiyaeilgygassDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 278 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 357
Cdd:cd00834  314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390
                        410
                 ....*....|....*.
gi 223972627 358 LTNSFGFGGTNATLCI 373
Cdd:cd00834  391 LSNSFGFGGHNASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
42-371 3.41e-138

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 399.55  E-value: 3.41e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIvSLVGEEYKS-IPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTI 120
Cdd:PRK07314   2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGI-GPITHFDTSdLAVKIAGEVKD------FNPDDYMSRKEARRMDRFIQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 121 MAIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKG 200
Cdd:PRK07314  75 YGIAAAKQAVEDAGLEI-TEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 201 PNHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------ 226
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGdadvmvaggaeaaitplgiagfaaaralstrnddperasrpfdkdrdgfvmgeg 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 ------------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAE 276
Cdd:PRK07314 234 agilvleelehakargakiyaevvgygmtgDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAE 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 277 NKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfI 356
Cdd:PRK07314 314 TQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---Y 390
                        410
                 ....*....|....*
gi 223972627 357 GLTNSFGFGGTNATL 371
Cdd:PRK07314 391 ALSNSFGFGGTNASL 405
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
42-373 2.23e-135

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: 392.54  E-value: 2.23e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:COG0304   75 ALAAAREALADAGLDL-DEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 202 NHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------- 226
Cdd:COG0304  154 NYTVSTACASGAHAIGEAYRLIRRGradvmiaggaeaaitplglagfdalgalstrnddpekasrpfdkdrdgfvlgega 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 -----------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 277
Cdd:COG0304  234 gvlvleelehakargakiyaevvgygassDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 278 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 357
Cdd:COG0304  314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390
                        410
                 ....*....|....*.
gi 223972627 358 LTNSFGFGGTNATLCI 373
Cdd:COG0304  391 LSNSFGFGGHNASLVF 406
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
41-371 4.92e-122

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 359.49  E-value: 4.92e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  41 HRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYK--------------SIPCSVAAYVPRGSDEGQFNEQNF 106
Cdd:PLN02836   5 TRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKmksedeetqlytldQLPSRVAALVPRGTGPGDFDEELW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 107 VSKsdiKSMSSPTIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVN 186
Cdd:PLN02836  85 LNS---RSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILIN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 187 MAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDAG------------------------------------- 229
Cdd:PLN02836 162 MAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADvmvaggtessidalsiagfsrsralstkfnscpteas 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 230 ------------------------------------------------HITAPDPEGEGALRCMAAALKDAGVQPEEISY 261
Cdd:PLN02836 242 rpfdcdrdgfvigegagvlvleelehakrrgakiyaevrgygmsgdahHITQPHEDGRGAVLAMTRALQQSGLHPNQVDY 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 262 INAHATSTPLGDAAENKAIKHLFKDHAY--ALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDL 339
Cdd:PLN02836 322 VNAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDD 401
                        410       420       430
                 ....*....|....*....|....*....|..
gi 223972627 340 NYVPLKAQewKTEKRFIGLTNSFGFGGTNATL 371
Cdd:PLN02836 402 GFVPLTAS--KAMLIRAALSNSFGFGGTNASL 431
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
41-371 4.82e-116

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 343.90  E-value: 4.82e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  41 HRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSD--EGQFNEQNFVSKSDIKSMSSP 118
Cdd:PRK06333   3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDLAEdaEAGFDPDRYLDPKDQRKMDRF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 119 TIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKL 198
Cdd:PRK06333  83 ILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 199 KGPNHAVSTACTTGAHAVGDSFRFIAHG---------------------------------------------------- 226
Cdd:PRK06333 163 KGPLGAPVTACAAGVQAIGDAARLIRSGeadvavcggteaaidrvslagfaaaralstrfndapeqasrpfdrdrdgfvm 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 ---------------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 273
Cdd:PRK06333 243 gegagilvietlehalargapplaelvgygtsaDAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGD 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 274 AAENKAIKHLFKdHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFD-LNYVPLKAQEWKTE 352
Cdd:PRK06333 323 LGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMD 401
                        410
                 ....*....|....*....
gi 223972627 353 krfIGLTNSFGFGGTNATL 371
Cdd:PRK06333 402 ---YALSNGFGFGGVNASI 417
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
51-371 9.81e-101

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 304.69  E-value: 9.81e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  51 LVTPLGVGTHLVWDRLIGGESGIVSLVGEEYK----------------SIPCSVAAYVPrgsdegqfNEQNFVSKSDIKS 114
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFlpdcipeqkalenlvaAMPCQIAAEVD--------QSEFDPSDFAPTK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 115 MSSPTI-MAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVS 193
Cdd:PTZ00050  73 RESRAThFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 194 IRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHG----------------------------------------------- 226
Cdd:PTZ00050 153 IKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGeadimicggteasitpvsfagfsrmralctkynddpqrasrpfdkdr 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 --------------------------------------DAGHITAPDPEGEGALRCMAAALKDAG-VQPEEISYINAHAT 267
Cdd:PTZ00050 233 agfvmgegagilvleelehalrrgakiyaeirgygsssDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHAT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 268 STPLGDAAENKAIKHLFKDH-AYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKA 346
Cdd:PTZ00050 313 STPIGDKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKT 392
                        410       420
                 ....*....|....*....|....*
gi 223972627 347 QEWKTEKRfIGLTNSFGFGGTNATL 371
Cdd:PTZ00050 393 AHPLQSID-AVLSTSFGFGGVNTAL 416
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
42-371 1.36e-73

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 234.51  E-value: 1.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK08722   4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVK------DFNCEEYMSKKDARKMDLFIQY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 122 AIGAAELAMKDSGWHpQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK08722  78 GIAAGIQALDDSGLE-VTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 202 NHAVSTACTTGAHAVGDSFRFIAHGDAG---------------------------------------------------- 229
Cdd:PRK08722 157 NIAISTACTTGLHNIGHAARMIAYGDADamvaggaekastplgmagfgaakalstrndepqkasrpwdkdrdgfvlgdga 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 230 --------------------------------HITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 277
Cdd:PRK08722 237 gmmvleeyehakargakiyaelvgfgmsgdayHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEI 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 278 KAIKH-LFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQewKTEKRFI 356
Cdd:PRK08722 317 KGIKRaLGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTAR--KVESMEY 394
                        410
                 ....*....|....*
gi 223972627 357 GLTNSFGFGGTNATL 371
Cdd:PRK08722 395 AICNSFGFGGTNGSL 409
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
42-368 4.89e-70

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 225.00  E-value: 4.89e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEIT------DFDPTEVMDPKEVKKADRFIQL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK08439  76 GLKAAREAMKDAGFLP-EELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 202 NHAVSTACTTGAHAVGDSFRFIA--------------------------------------------------------- 224
Cdd:PRK08439 155 NLSSVTACAAGTHAIIEAVKTIMlggadkmlvvgaesaicpvgiggfaamkalstrnddpkkasrpfdkdrdgfvmgega 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 225 ---------------------------HGDAGHITAPDPEGegALRCMAAALKDAGVqpEEISYINAHATSTPLGDAAEN 277
Cdd:PRK08439 235 galvleeyesakkrgakiyaeiigfgeSGDANHITSPAPEG--PLRAMKAALEMAGN--PKIDYINAHGTSTPYNDKNET 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 278 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 357
Cdd:PRK08439 311 AALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELN---VV 387
                        410
                 ....*....|.
gi 223972627 358 LTNSFGFGGTN 368
Cdd:PRK08439 388 MSNSFGFGGTN 398
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
227-371 4.51e-49

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 170.02  E-value: 4.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHayaLAVSSTKGATGHLLGA 306
Cdd:PRK09185 248 DAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDG---VPCSSTKGLTGHTLGA 324
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972627 307 AGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYvpLKAQEWKTEKRFIgLTNSFGFGGTNATL 371
Cdd:PRK09185 325 AGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLY--LVENAQALAIRYV-LSNSFAFGGNNCSL 386
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
136-373 5.11e-47

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 163.36  E-value: 5.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 136 HPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHA 215
Cdd:PRK14691  18 HADNTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 216 VGDSFRFIAH---------------------------------------------------------------------- 225
Cdd:PRK14691  98 IGDAVRMIRNneadvalcggaeavidtvslagfaaaralsthfnstpekasrpfdtardgfvmgegaglliieelehala 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 226 ---------------GDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDhAYA 290
Cdd:PRK14691 178 rgakplaeivgygtsADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNA 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 291 LAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFD-LNYVPLKAQewkTEKRFIGLTNSFGFGGTNA 369
Cdd:PRK14691 257 LAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQ---PHDMTYALSNGFGFAGVNA 333

                 ....
gi 223972627 370 TLCI 373
Cdd:PRK14691 334 SILL 337
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
42-374 1.43e-46

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 166.69  E-value: 1.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSDEGqfneqnFVSKSDIKSMSSPTIM 121
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDG------WVAPKLSKRMDKFMLY 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 122 AIGAAELAMKDSGWHPQ--SEADQVATGVAIGMGMIPLEVVSEtALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLK 199
Cdd:PLN02787 203 LLTAGKKALADGGITEDvmKELDKTKCGVLIGSAMGGMKVFND-AIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWM 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 200 GPNHAVSTACTTGAHAVGDSFRFIAHG----------------------------------------------------- 226
Cdd:PLN02787 282 GPNYSISTACATSNFCILNAANHIIRGeadvmlcggsdaaiipiglggfvacralsqrnddptkasrpwdmnrdgfvmge 361
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 -------------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAA 275
Cdd:PLN02787 362 gagvllleelehakkrganiyaeflggsftcDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLK 441
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 276 ENKAIKHLFKDHAyALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNyVPLKAQEWKTEKRf 355
Cdd:PLN02787 442 EYQALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTK-VLVGPKKERLDIK- 518
                        410
                 ....*....|....*....
gi 223972627 356 IGLTNSFGFGGTNATLCIA 374
Cdd:PLN02787 519 VALSNSFGFGGHNSSILFA 537
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
44-371 2.33e-46

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 163.36  E-value: 2.33e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  44 VVITGIGLVTPLGVGTHLVWDRLIGGESGIVSL---VGEEYKSiPCSVAAYVPRGSDEGqfneqnfVSKSDIKSMSSPTI 120
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLddpFVEEFDL-PVRIGGHLLEEFDHQ-------LTRVELRRMSYLQR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 121 MAIGAAELAMKDSGwhpQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKG 200
Cdd:PRK07910  86 MSTVLGRRVWENAG---SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 201 PNHAVSTACTTGAHAVGDSFRFIAHGDAG--------------------------------------------------- 229
Cdd:PRK07910 163 GVITPVSACASGSEAIAQAWRQIVLGEADiaicggvetrieavpiagfaqmrivmstnnddpagacrpfdkdrdgfvfge 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 230 ----------------------------------HITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAA 275
Cdd:PRK07910 243 ggalmvieteehakarganilarimgasitsdgfHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 276 ENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVplkAQEWKTEKRF 355
Cdd:PRK07910 323 EGKAINNALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVV---AGEPRPGNYR 397
                        410
                 ....*....|....*.
gi 223972627 356 IGLTNSFGFGGTNATL 371
Cdd:PRK07910 398 YAINNSFGFGGHNVAL 413
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
42-371 9.87e-44

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 156.37  E-value: 9.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVslVGEEYKSI--PCSVAAYVprgsdegQFNEQNFVSKSDIKSMSSPT 119
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT--FSPEFAEMgmRSQVWGNV-------KLDPTGLIDRKVMRFMGDAS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 120 IMAIGAAELAMKDSGWhpqsEADQVA---TGVAIGMG-MIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIR 195
Cdd:PRK07967  73 AYAYLAMEQAIADAGL----SEEQVSnprTGLIAGSGgGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 196 YKLKGPNHAVSTACTTGAHAVGDSFRFIAHG---------------------DA-------------------------- 228
Cdd:PRK07967 149 FKIKGVNYSISSACATSAHCIGNAVEQIQLGkqdivfagggeeldwemsclfDAmgalstkyndtpekasraydanrdgf 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 229 ---------------------GHITAP--------------DPEGEGALRCMAAALkdAGVQpEEISYINAHATSTPLGD 273
Cdd:PRK07967 229 viaggggvvvveelehalargAKIYAEivgygatsdgydmvAPSGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTPVGD 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 274 AAENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF-DLNYVPLKAQEWKTE 352
Cdd:PRK07967 306 VKELGAIREVFGDK--SPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVTETTDNAELT 383
                        410
                 ....*....|....*....
gi 223972627 353 krfIGLTNSFGFGGTNATL 371
Cdd:PRK07967 384 ---TVMSNSFGFGGTNATL 399
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
42-373 9.18e-43

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 153.60  E-value: 9.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVG-EEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTI 120
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEwDRYDGLNTRLAAPID------DFELPAHYTRKKIRSMGRVSL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 121 MAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKG 200
Cdd:PRK09116  76 MATRASELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 201 PNHAVSTACTTGAHAVGDSFRFIAHG------------------------------------------------------ 226
Cdd:PRK09116 156 RVIPTSSACTSGSQGIGYAYEAIKYGyqtvmlaggaeelcpteaavfdtlfatstrndapeltprpfdanrdglvigega 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 -----------------------------DAGHITAPDPEGEGalRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 277
Cdd:PRK09116 236 gtlvleelehakargatiyaeivgfgtnsDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAES 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 278 KAIKHLFKDHayaLAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF-DLNYvpLKAQEWKTEKRFI 356
Cdd:PRK09116 314 QATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDY--IMGEAREIDTEYV 388
                        410
                 ....*....|....*..
gi 223972627 357 gLTNSFGFGGTNATLCI 373
Cdd:PRK09116 389 -MSNNFAFGGINTSLIF 404
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
226-331 1.21e-41

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: 141.94  E-value: 1.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  226 GDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAY--ALAVSSTKGATGHL 303
Cdd:pfam02801  11 HDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqPLAIGSVKSNIGHL 90
                          90       100
                  ....*....|....*....|....*...
gi 223972627  304 LGAAGAVEAAFTTLACYYQKLPPTLNLD 331
Cdd:pfam02801  91 EGAAGAAGLIKVVLALRHGVIPPTLNLE 118
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
42-371 5.18e-41

"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: 149.13  E-value: 5.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLV---WDRLIGGESGIVSLVGEEYKSiPCSVAAYVPRGSDEGQFneqnfVSKSDIksMSSP 118
Cdd:cd00828    1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGIAPVARLKSRF-DRGVAGQIPTGDIPGWD-----AKRTGI--VDRT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 119 TIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFqtkgYNKVSPFFVPK--ILVNMAAGQVSIRY 196
Cdd:cd00828   73 TLLALVATEEALADAGITDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLD----ARAVNPYVSPKwmLSPNTVAGWVNILL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 197 KLK-GPNHAVSTACTTGAHAV---------------------------------------------GDSFRFIAHGD--- 227
Cdd:cd00828  149 LSShGPIKTPVGACATALEALdlaveairsgkadivvvggvedpleeglsgfanmgalstaeeepeEMSRPFDETRDgfv 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 228 ---------------------------AGHITAPDP-------EGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 273
Cdd:cd00828  229 eaegagvlvleraelalargapiygrvAGTASTTDGagrsvpaGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPAND 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 274 AAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEK 353
Cdd:cd00828  309 VAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKV 388
                        410
                 ....*....|....*...
gi 223972627 354 RfIGLTNSFGFGGTNATL 371
Cdd:cd00828  389 R-AALVNAFGFGGSNAAL 405
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
43-375 7.58e-41

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 147.89  E-value: 7.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  43 RVVITGIGLVTPLGvGTHLVWDRLIGGESGIvSLVG--EEYKSIPCSVAAYVPrgsdegqfneqnfvskSDIKSMSSPTI 120
Cdd:PRK05952   3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGI-KLHQpfPELPPLPLGLIGNQP----------------SSLEDLTKTVV 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 121 MAigaaelAMKDSGWHPqSEADqvaTGVAIGMG---------MIPLEVVSETALNFQTKGYNKVSpffvpkILVNMAAGQ 191
Cdd:PRK05952  65 TA------ALKDAGLTP-PLTD---CGVVIGSSrgcqgqwekLARQMYQGDDSPDEELDLENWLD------TLPHQAAIA 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 192 VSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHG--------------------------------------------- 226
Cdd:PRK05952 129 AARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGqcqrviagaveapitpltlagfqqmgalaktgaypfdrqreglvl 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 227 ---------------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 273
Cdd:PRK05952 209 geggailvlesaelaqkrgakiygqilgfgltcDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLND 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 274 AAENKAIKHLFkdhAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLdcSEPEFDLNYVpLKAQEWKTEK 353
Cdd:PRK05952 289 QREANLIQALF---PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGL--QEPEFDLNFV-RQAQQSPLQN 362
                        410       420
                 ....*....|....*....|..
gi 223972627 354 rfiGLTNSFGFGGTNATLCIAG 375
Cdd:PRK05952 363 ---VLCLSFGFGGQNAAIALGK 381
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
44-375 2.02e-38

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 142.46  E-value: 2.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  44 VVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVprgsdegqfneqNFVsksDIKSMSSPTI--- 120
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------------DFL---PESPFGASALsea 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 121 MAIGAAELAMKDSG--------------------WHPQSEADQvATGVAIGMGMIPLEVVSETalnfqtkgyNKVSPFFv 180
Cdd:PRK06501  78 LARLAAEEALAQAGigkgdfpgplflaappveleWPARFALAA-AVGDNDAPSYDRLLRAARG---------GRFDALH- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 181 PKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAV---------GDS-----------------FRF------------ 222
Cdd:PRK06501 147 ERFQFGSIADRLADRFGTRGLPISLSTACASGATAIqlgveairrGETdralciatdgsvsaealIRFsllsalstqndp 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 223 ----------------IAHG------------------------------DAGHITAPDPEGEGALRCMAAALKDAGVQP 256
Cdd:PRK06501 227 pekaskpfskdrdgfvMAEGagalvleslesavargakilgivagcgekaDSFHRTRSSPDGSPAIGAIRAALADAGLTP 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 257 EEISYINAHATSTPLGDAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPE 336
Cdd:PRK06501 307 EQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPA 386
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 223972627 337 FDLNYVPLKAQEWKTEKRfigLTNSFGFGGTNATLCIAG 375
Cdd:PRK06501 387 IPLDVVPNVARDARVTAV---LSNSFGFGGQNASLVLTA 422
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
129-369 1.86e-34

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: 131.53  E-value: 1.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 129 AMKDSGWHPQSEADQvATGVAIGMGmiplevvSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTA 208
Cdd:cd00833   98 ALEDAGYSPESLAGS-RTGVFVGAS-------SSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTA 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 209 CTTGAHAV-----------------------------------------GDSFRF------------------------I 223
Cdd:cd00833  170 CSSSLVALhlacqslrsgecdlalvggvnlilspdmfvgfskagmlspdGRCRPFdadadgyvrgegvgvvvlkrlsdaL 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 224 AHGD----------------AGHITAPDPEGEGALrcMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLF--- 284
Cdd:cd00833  250 RDGDriyavirgsavnqdgrTKGITAPSGEAQAAL--IRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFggs 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 285 KDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWK--TEKRFIGL 358
Cdd:cd00833  328 RSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEesplRVPTEARPWPapAGPRRAGV 407
                        330
                 ....*....|.
gi 223972627 359 tNSFGFGGTNA 369
Cdd:cd00833  408 -SSFGFGGTNA 417
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
231-369 2.06e-29

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 120.36  E-value: 2.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  231 ITAPDPEGEGALrcMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAYA---LAVSSTKGATGHLLGAA 307
Cdd:COG3321   277 LTAPNGPAQAAV--IRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAA 354
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  308 GAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWKTEK--RFIGLtNSFGFGGTNA 369
Cdd:COG3321   355 GV--AGLikAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTELRPWPAGGgpRRAGV-SSFGFGGTNA 421
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
234-374 4.76e-29

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 116.28  E-value: 4.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 234 PDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAYalaVSSTKGATGHLLGAAGAVEAA 313
Cdd:PRK07103 276 PDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELI 352
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972627 314 FTTLACYYQKLPPTLNLDcsEP-EFDLNYVPLKAQEWKTEkrfIGLTNSFGFGGTNATLCIA 374
Cdd:PRK07103 353 ATLLQMRAGFLHPSRNLD--EPiDERFRWVGSTAESARIR---YALSLSFGFGGINTALVLE 409
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
42-228 3.73e-28

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: 110.42  E-value: 3.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627   42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGE-----EYKSIPCSVA--AYVPRG--SDEGQFNEQNF-VSKSD 111
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAgkIYTKWGglDDIFDFDPLFFgISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  112 IKSMSSPTIMAIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMiplEVVSETALNFQTKGYNKVSPFFVPKIlVNMAAGQ 191
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSL-DGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 223972627  192 VSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDA 228
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEA 192
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
119-371 2.86e-24

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: 101.94  E-value: 2.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 119 TIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPkilvnmAAGQVSIRYKL 198
Cdd:cd00825   12 SILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG------ASGQIATPLGI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 199 KGPNHAVSTACTTGAHAV-------------------------------------------------------------- 216
Cdd:cd00825   86 HGPAYDVSAACAGSLHALslaadavqngkqdivlaggseelaapmdcefdamgalstpekasrtfdaaadgfvfgdgaga 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 217 ------------GDSFRFIAHGDAGHIT-----APDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKA 279
Cdd:cd00825  166 lvveelehalarGAHIYAEIVGTAATIDgagmgAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 280 IKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTekrfiGLT 359
Cdd:cd00825  246 LRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPRELRT-----ALL 318
                        330
                 ....*....|..
gi 223972627 360 NSFGFGGTNATL 371
Cdd:cd00825  319 NGFGLGGTNATL 330
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
42-342 2.77e-20

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: 91.27  E-value: 2.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627  42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrGSDEGQFNEQNFVSKSDiksmsSPTIM 121
Cdd:cd00832    1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVP-DFDAAEHLPGRLLPQTD-----RMTRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPF--FVPKILVNmaAGQVSIRYKLK 199
Cdd:cd00832   75 ALAAADWALADAGVDP-AALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYqsFAWFYAVN--TGQISIRHGMR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 200 GPNHAVSTACTTGAHAVGDSFRFIAHGD---------------------------------------------------- 227
Cdd:cd00832  152 GPSGVVVAEQAGGLDALAQARRLVRRGTplvvsggvdsalcpwgwvaqlssgrlstsddparaylpfdaaaagyvpgegg 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 228 ----------------------AGHITAPDP-----EGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAI 280
Cdd:cd00832  232 ailvledaaaarergarvygeiAGYAATFDPppgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAAL 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972627 281 KHLFKdhAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYV 342
Cdd:cd00832  312 AAVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLV 371
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
231-368 4.71e-17

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


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 83.13  E-value: 4.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627   231 ITAPDPEGEGalRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLF---KDHAYALAVSSTKGATGHLLGAA 307
Cdd:TIGR02813  309 IYAPRPEGQA--KALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFsqdNDQKQHIALGSVKSQIGHTKSTA 386
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223972627   308 GAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPL----KAQEWKTEK----RFIGLTnSFGFGGTN 368
Cdd:TIGR02813  387 GTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFylntETRPWMQREdgtpRRAGIS-SFGFGGTN 454
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
188-373 6.82e-17

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: 79.41  E-value: 6.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 188 AAGQVSIRYKLK-GPNHAVSTACTTGAHAVGDSFRFIAHGDAGHITA--------------------------------- 233
Cdd:cd00327   46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAggseefvfgdgaaaavveseehalrrgahpqae 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627 234 --------------PDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHayALAVSSTKGA 299
Cdd:cd00327  126 ivstaatfdgasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVR--SPAVSATLIM 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972627 300 TGHLLGAAGAVEAAFTTLACYYQKLPPTLN-LDCsepefdlnyvplkaqewktekrfiGLTNSFGFGGTNATLCI 373
Cdd:cd00327  204 TGHPLGAAGLAILDELLLMLEHEFIPPTPRePRT------------------------VLLLGFGLGGTNAAVVL 254
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
291-369 2.20e-11

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: 63.89  E-value: 2.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972627   291 LAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWKTE--KRFIGLtNSF 362
Cdd:smart00825 209 LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPgrPRRAGV-SSF 285

                   ....*..
gi 223972627   363 GFGGTNA 369
Cdd:smart00825 286 GFGGTNA 292
 
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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