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Conserved domains on  [gi|76883454|gb|ABA58135|]
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3-oxoacyl-[acyl-carrier-protein] synthase II [Nitrosococcus oceani ATCC 19707]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase II( domain architecture ID 11496422)

beta-ketoacyl-[acyl-carrier-protein] synthase II catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP, part of the dissociated (or type II) fatty acid biosynthesis system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 5-412 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: 753.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454     5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKgLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECD-LDYVPNEAREAKIDYALSNSFGFGG 399


                  ....*...
gi 76883454   405 TNGSLIFR 412
Cdd:TIGR03150 400 TNASLVFK 407
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 5-412 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: 753.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454     5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKgLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECD-LDYVPNEAREAKIDYALSNSFGFGG 399


                  ....*...
gi 76883454   405 TNGSLIFR 412
Cdd:TIGR03150 400 TNASLVFK 407
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
5-412 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 740.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:PRK07314   2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:PRK07314  82 QAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVTA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:PRK07314 162 CATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:PRK07314 242 LEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVF 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKgLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:PRK07314 322 GEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECD-LDYVPNEARERKIDYALSNSFGFGG 400


                 ....*...
gi 76883454  405 TNGSLIFR 412
Cdd:PRK07314 401 TNASLVFK 408
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 5-412 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: 699.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECkGLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPEC-DLDYVPNEAREAKIDYALSNSFGFGG 399


                ....*...
gi 76883454 405 TNGSLIFR 412
Cdd:COG0304 400 HNASLVFK 407
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 5-411 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: 644.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECkGLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPEC-DLDYVPNEAREAPIRYALSNSFGFGG 399


                ....*..
gi 76883454 405 TNGSLIF 411
Cdd:cd00834 400 HNASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 5-248 2.50e-67

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: 214.42  E-value: 2.50e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454     5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITG--FDVTNF---PVRFGGAVKG-----FEIGDYLPL------KD 68
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrWDPDKLydpPSRIAGKIYTkwgglDDIFDFDPLffgispRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    69 ARKMDPFIHYGIAAARQALEDSGLEINEANATQVGVAIGSGIGGLHGIELghnAYLQGGPRRISPFFVPsNIINMIAGNL 148
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLL---LDEDGGPRRGSPFAVG-TMPSVIAGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   149 SILYGMKGPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTrnEEPETASRPWDkdr 228
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA--- 231

                         250       260
                  ....*....|....*....|
gi 76883454   229 DGFVLSDGAGVLVLEELEHA 248
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 7-413 1.05e-21

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: 94.32  E-value: 1.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454      7 VAVTGLGIVCPVGVDVEGSWANLLAGKSGIGpitGFDvtnfPVRFGgavkgfeigdyLPLKDARKMDP----FIHygiaA 82
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD---LFD----AAFFG-----------ISPREAEAMDPqqrlLLE----V 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454     83 ARQALEDSGLEINEANATQVGVAIGSGigglhgielgHNAYlqggprrispffvpsniinmiagnlsilygmkgpNIAIV 162
Cdd:smart00825  59 AWEALEDAGIDPESLRGSRTGVFVGVS----------SSDY----------------------------------SVTVD 94

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    163 TACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALStrneePETASRPWDKDRDGFVLSDGAGVLVL 242
Cdd:smart00825  95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVL 169

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    243 EELEHAKRRGAQIYAEVVGFGMSADAYH--MTQPprNGEgaarcmmnalkdahingeeidyinahgtstpagdraetlai 320
Cdd:smart00825 170 KRLSDALRDGDPILAVIRGSAVNQDGRSngITAP--SGP----------------------------------------- 206

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    321 kavlgshAQkTPVSSTKSMTGHLLGAAG--GIeaIFSVLAIRDQIAPPTINIFNLDPEckgLD------YVPNIAREM-- 390
Cdd:smart00825 207 -------AQ-LLIGSVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPH---IDleesplRVPTELTPWpp 273

                          410       420
                   ....*....|....*....|....*
gi 76883454    391 --KIKTVVSNSFGFGGTNGSLIFRQ 413
Cdd:smart00825 274 pgRPRRAGVSSFGFGGTNAHVILEE 298
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 5-412 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: 753.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454     5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKgLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECD-LDYVPNEAREAKIDYALSNSFGFGG 399


                  ....*...
gi 76883454   405 TNGSLIFR 412
Cdd:TIGR03150 400 TNASLVFK 407
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
5-412 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 740.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:PRK07314   2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:PRK07314  82 QAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVTA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:PRK07314 162 CATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:PRK07314 242 LEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVF 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKgLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:PRK07314 322 GEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECD-LDYVPNEARERKIDYALSNSFGFGG 400


                 ....*...
gi 76883454  405 TNGSLIFR 412
Cdd:PRK07314 401 TNASLVFK 408
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 5-412 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: 699.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECkGLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPEC-DLDYVPNEAREAKIDYALSNSFGFGG 399


                ....*...
gi 76883454 405 TNGSLIFR 412
Cdd:COG0304 400 HNASLVFK 407
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 5-411 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: 644.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECkGLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPEC-DLDYVPNEAREAPIRYALSNSFGFGG 399


                ....*..
gi 76883454 405 TNGSLIF 411
Cdd:cd00834 400 HNASLVF 406
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
5-415 0e+00

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 563.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVK--------GFEIGDYLPLKDARKMDPFI 76
Cdd:PRK06333   4 KRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlaedaeaGFDPDRYLDPKDQRKMDRFI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   77 HYGIAAARQALEDSGLEINEANATQ-VGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMK 155
Cdd:PRK06333  84 LFAMAAAKEALAQAGWDPDTLEDRErTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGFK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  156 GPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTR-NEEPETASRPWDKDRDGFVLS 234
Cdd:PRK06333 164 GPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGFVMG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  235 DGAGVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDR 314
Cdd:PRK06333 244 EGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  315 AETLAIKAVLGsHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKGLDYVPNIAREMKIKT 394
Cdd:PRK06333 324 GEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVANKARPMDMDY 402

                        410       420
                 ....*....|....*....|.
gi 76883454  395 VVSNSFGFGGTNGSLIFRQLE 415
Cdd:PRK06333 403 ALSNGFGFGGVNASILFRRWE 423
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
2-414 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 542.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    2 LSDKRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIA 81
Cdd:PRK08722   1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   82 AARQALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAI 161
Cdd:PRK08722  81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  162 VTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLV 241
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  242 LEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIK 321
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  322 AVLGSH-AQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECkGLDYVPNIAREMK-IKTVVSNS 399
Cdd:PRK08722 321 RALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGL-DIDLVPHTARKVEsMEYAICNS 399

                        410
                 ....*....|....*
gi 76883454  400 FGFGGTNGSLIFRQL 414
Cdd:PRK08722 400 FGFGGTNGSLIFKKM 414
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 5-414 0e+00

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 516.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:PRK08439  82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLEE 244
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  245 LEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRngEGAARCMMNALKDAhiNGEEIDYINAHGTSTPAGDRAETLAIKAVL 324
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMA--GNPKIDYINAHGTSTPYNDKNETAALKELF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  325 GSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKgLDYVPNIAREMKIKTVVSNSFGFGG 404
Cdd:PRK08439 318 GSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECD-LDYIPNVARKAELNVVMSNSFGFGG 396

                        410
                 ....*....|
gi 76883454  405 TNGSLIFRQL 414
Cdd:PRK08439 397 TNGVVIFKKV 406
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 14-413 1.45e-164

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 468.79  E-value: 1.45e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   14 IVCPVGVDVEGSWANLLAGKSGIGPITGFD----------------VTNFPVRFGGAVKGfEIGDYLPLKDARKMDPFIH 77
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPkflpdcipeqkalenlVAAMPCQIAAEVDQ-SEFDPSDFAPTKRESRATH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   78 YGIAAARQALEDSGLEI-NEANATQVGVAIGSGIGGLHGIElGHNAYLQG-GPRRISPFFVPSNIINMIAGNLSILYGMK 155
Cdd:PTZ00050  80 FAMAAAREALADAKLDIlSEKDQERIGVNIGSGIGSLADLT-DEMKTLYEkGHSRVSPYFIPKILGNMAAGLVAIKHKLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  156 GPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTR-NEEPETASRPWDKDRDGFVLS 234
Cdd:PTZ00050 159 GPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVMG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  235 DGAGVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKD-AHINGEEIDYINAHGTSTPAGD 313
Cdd:PTZ00050 239 EGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANININDVDYVNAHATSTPIGD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  314 RAETLAIKAVLGSH-AQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKgLDYVPN--IAREM 390
Cdd:PTZ00050 319 KIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECD-LNLVQGktAHPLQ 397

                        410       420
                 ....*....|....*....|...
gi 76883454  391 KIKTVVSNSFGFGGTNGSLIFRQ 413
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTK 420
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 2-411 2.27e-151

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 435.76  E-value: 2.27e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    2 LSDKRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDV--------------TNFPVRFGGAV---KGFEIGDYL 64
Cdd:PLN02836   3 LPTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLkmksedeetqlytlDQLPSRVAALVprgTGPGDFDEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   65 PLKDARKMDPFIHYGIAAARQALEDSG-LEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINM 143
Cdd:PLN02836  83 LWLNSRSSSRFIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINM 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  144 IAGNLSILYGMKGPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTR-NEEPETASR 222
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  223 PWDKDRDGFVLSDGAGVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYI 302
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYV 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  303 NAHGTSTPAGDRAETLAIKAVLGSHA--QKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKGl 380
Cdd:PLN02836 323 NAHATSTPLGDAVEARAIKTVFSEHAtsGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDD- 401

                        410       420       430
                 ....*....|....*....|....*....|..
gi 76883454  381 DYVPNIA-REMKIKTVVSNSFGFGGTNGSLIF 411
Cdd:PLN02836 402 GFVPLTAsKAMLIRAALSNSFGFGGTNASLLF 433
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 5-411 2.93e-128

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 380.48  E-value: 2.93e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGK 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   85 QALEDSGLE---INEANATQVGVAIGSGIGGLH----GIELGHNAYlqggpRRISPFFVPSNIINMIAGNLSILYGMKGP 157
Cdd:PLN02787 209 KALADGGITedvMKELDKTKCGVLIGSAMGGMKvfndAIEALRISY-----RKMNPFCVPFATTNMGSAMLAMDLGWMGP 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  158 NIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGA 237
Cdd:PLN02787 284 NYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGA 363

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  238 GVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAET 317
Cdd:PLN02787 364 GVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEY 443

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  318 LAIKAVLGSHAQkTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKGLDYVPNIAREMKIKTVVS 397
Cdd:PLN02787 444 QALMRCFGQNPE-LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIKVALS 522

                        410
                 ....*....|....
gi 76883454  398 NSFGFGGTNGSLIF 411
Cdd:PLN02787 523 NSFGFGGHNSSILF 536
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
5-415 4.85e-115

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 342.04  E-value: 4.85e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKgFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQG-GPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVT 163
Cdd:PRK07967  81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPrGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  164 ACTTGTHNIGEAVRIIQRGEAKVMIAGGAE-----MATSPTGLGgfasarALSTR-NEEPETASRPWDKDRDGFVLSDGA 237
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEeldweMSCLFDAMG------ALSTKyNDTPEKASRAYDANRDGFVIAGGG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  238 GVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPprNGEGAARCMMNALkdAHINGeEIDYINAHGTSTPAGDRAET 317
Cdd:PRK07967 235 GVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMAL--ATVDT-PIDYINTHGTSTPVGDVKEL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  318 LAIKAVLGShaQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKGLDYVPNIAREMKIKTVVS 397
Cdd:PRK07967 310 GAIREVFGD--KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMS 387

                        410
                 ....*....|....*...
gi 76883454  398 NSFGFGGTNGSLIFRQLE 415
Cdd:PRK07967 388 NSFGFGGTNATLVFRRYK 405
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
5-412 7.99e-112

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 333.88  E-value: 7.99e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDV-TNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAA 83
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRyDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   84 RQALEDSGLeINEANAT--QVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPffvpSNIINMI----AGNLSILYGMKGP 157
Cdd:PRK09116  82 ELALEDAGL-LGDPILTdgRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITA----TTYVRMMphttAVNVGLFFGLKGR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  158 NIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEmATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGA 237
Cdd:PRK09116 157 VIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAE-ELCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  238 GVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPprNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAET 317
Cdd:PRK09116 236 GTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQP--QAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAES 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  318 LAIKAVLGShaqKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKGLDYVPNIAREMKIKTVVS 397
Cdd:PRK09116 314 QATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMS 390

                        410
                 ....*....|....*
gi 76883454  398 NSFGFGGTNGSLIFR 412
Cdd:PRK09116 391 NNFAFGGINTSLIFK 405
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
7-411 3.21e-106

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 320.04  E-value: 3.21e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    7 VAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVkgfeigDYLPlkDARKMDPFIHYGIA--AAR 84
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------DFLP--ESPFGASALSEALArlAAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   85 QALEDSGL----------------EINEANATQVGVAIGsgigglHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNL 148
Cdd:PRK06501  85 EALAQAGIgkgdfpgplflaappvELEWPARFALAAAVG------DNDAPSYDRLLRAARGGRFDALHERFQFGSIADRL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  149 SILYGMKGPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEPETASRPWDKDR 228
Cdd:PRK06501 159 ADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  229 DGFVLSDGAGVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTS 308
Cdd:PRK06501 239 DGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTS 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  309 TPAGDRAETLAIKAVLGSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKgLDYVPNIAR 388
Cdd:PRK06501 319 TPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIP-LDVVPNVAR 397

                        410       420
                 ....*....|....*....|...
gi 76883454  389 EMKIKTVVSNSFGFGGTNGSLIF 411
Cdd:PRK06501 398 DARVTAVLSNSFGFGGQNASLVL 420
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 95-413 1.27e-104

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 313.20  E-value: 1.27e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   95 NEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTACTTGTHNIGE 174
Cdd:PRK14691  21 NTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  175 AVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTR-NEEPETASRPWDKDRDGFVLSDGAGVLVLEELEHAKRRGA 253
Cdd:PRK14691 101 AVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGA 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  254 QIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVLGsHAQKTPV 333
Cdd:PRK14691 181 KPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFG-ESNALAI 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  334 SSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKGLDYVPNIAREMKIKTVVSNSFGFGGTNGSLIFRQ 413
Cdd:PRK14691 260 TSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
7-411 3.00e-95

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 292.02  E-value: 3.00e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    7 VAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNF--PVRFGGAVKGfEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFdlPVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLGR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   85 QALEDSGLEinEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILYGMKGPNIAIVTA 164
Cdd:PRK07910  93 RVWENAGSP--EVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  165 CTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARA-LSTRNEEPETASRPWDKDRDGFVLSDGAGVLVLE 243
Cdd:PRK07910 171 CASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIE 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  244 ELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAV 323
Cdd:PRK07910 251 TEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  324 LGSHaqKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKgLDYVPNIAREMKIKTVVSNSFGFG 403
Cdd:PRK07910 331 LGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEID-LDVVAGEPRPGNYRYAINNSFGFG 407


                 ....*...
gi 76883454  404 GTNGSLIF 411
Cdd:PRK07910 408 GHNVALAF 415
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 6-409 2.03e-93

"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: 286.64  E-value: 2.03e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   6 RVAVTGLGIVCPVGV---DVEGSWANLLAGKSGIGPITGFDVTnFPVRFGGAVKGFEIGDYLpLKDARKMDPFIHYGIAA 82
Cdd:cd00828   2 RVVITGIGVVSPHGEgcdEVEEFWEALREGRSGIAPVARLKSR-FDRGVAGQIPTGDIPGWD-AKRTGIVDRTTLLALVA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  83 ARQALEDSGLEI-NEANATQVGVAIGSGIGGLHgiELGHNAYLQGgpRRISPFFVPSNI--INMIAGNLSILY-GMKGPN 158
Cdd:cd00828  80 TEEALADAGITDpYEVHPSEVGVVVGSGMGGLR--FLRRGGKLDA--RAVNPYVSPKWMlsPNTVAGWVNILLlSSHGPI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 159 IAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEmATSPTGLGGFASARALSTRNEEPETASRPWDKDRDGFVLSDGAG 238
Cdd:cd00828 156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVE-DPLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGAG 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 239 VLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPrNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETL 318
Cdd:cd00828 235 VLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESR 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 319 AIKAVLGSHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKGLDYVPNIA-REMKIKTVVS 397
Cdd:cd00828 314 AIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRdLNLKVRAALV 393

                       410
                ....*....|..
gi 76883454 398 NSFGFGGTNGSL 409
Cdd:cd00828 394 NAFGFGGSNAAL 405
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 5-410 2.99e-82

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: 257.67  E-value: 2.99e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITGFDVTNFPVRFGGAVKGFEIGDYLPLKDARKMDPFIHYGIAAAR 84
Cdd:cd00832   1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  85 QALEDSGLEINEANATQVGVAIGSGIGGLhgiELGH---NAYLQGGPRRISPF-----FVPSNiinmiAGNLSILYGMKG 156
Cdd:cd00832  81 WALADAGVDPAALPPYDMGVVTASAAGGF---EFGQrelQKLWSKGPRHVSAYqsfawFYAVN-----TGQISIRHGMRG 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 157 PNIAIVTACTTGTHNIGEAVRIIQRGeAKVMIAGGAEMATSPTGLGGFASARALSTrNEEPETASRPWDKDRDGFVLSDG 236
Cdd:cd00832 153 PSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 237 AGVLVLEELEHAKRRGAQIYAEVVGFGMSADAyhmtqPPRNGEGA--ARCMMNALKDAHINGEEIDYINAHGTSTPAGDR 314
Cdd:cd00832 231 GAILVLEDAAAARERGARVYGEIAGYAATFDP-----PPGSGRPPglARAIRLALADAGLTPEDVDVVFADAAGVPELDR 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 315 AETLAIKAVLGSHAqkTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECkGLDYVPNIAREMKIKT 394
Cdd:cd00832 306 AEAAALAAVFGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAY-GLDLVTGRPRPAALRT 382

                       410
                ....*....|....*.
gi 76883454 395 VVSNSFGFGGTNGSLI 410
Cdd:cd00832 383 ALVLARGRGGFNSALV 398
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
6-409 5.24e-80

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 251.51  E-value: 5.24e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    6 RVAVTGLGIVCPVGvDVEGSWANLLAGKSGIGPITGFdvTNFPVRFGGAvkgfeIGDY-LPLKDARKMdpfihygiaAAR 84
Cdd:PRK05952   3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQPF--PELPPLPLGL-----IGNQpSSLEDLTKT---------VVT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   85 QALEDSGLEINEANAtqvGVAIGSGIGGLHGIELGHNAYLQGGPRrISPFFVPSNIINMIAGNLSIL----YGMKGPNIA 160
Cdd:PRK05952  66 AALKDAGLTPPLTDC---GVVIGSSRGCQGQWEKLARQMYQGDDS-PDEELDLENWLDTLPHQAAIAaarqIGTQGPVLA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  161 IVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTrneepeTASRPWDKDRDGFVLSDGAGVL 240
Cdd:PRK05952 142 PMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGLVLGEGGAIL 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  241 VLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAI 320
Cdd:PRK05952 216 VLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLI 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  321 KAVLGshaQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNldPECKgLDYVPNiAREMKIKTVVSNSF 400
Cdd:PRK05952 296 QALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFD-LNFVRQ-AQQSPLQNVLCLSF 368


                 ....*....
gi 76883454  401 GFGGTNGSL 409
Cdd:PRK05952 369 GFGGQNAAI 377
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 6-410 9.94e-75

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: 239.00  E-value: 9.94e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   6 RVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITG--FDVTNFP----------VRFGGAVKGFEIGD----YLPLKDA 69
Cdd:cd00833   2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEdrWDADGYYpdpgkpgktyTRRGGFLDDVDAFDaaffGISPREA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  70 RKMDP----FIHygiaAARQALEDSGLEINEANATQVGVAIGSGigglhGIELGHNayLQGGPRRISPFFVPSNIINMIA 145
Cdd:cd00833  82 EAMDPqqrlLLE----VAWEALEDAGYSPESLAGSRTGVFVGAS-----SSDYLEL--LARDPDEIDAYAATGTSRAFLA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 146 GNLSILYGMKGPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALStrneePETASRPWD 225
Cdd:cd00833 151 NRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCRPFD 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 226 KDRDGFVLSDGAGVLVLEELEHAKRRGAQIYAEVVGFGMSADAY--HMTQPprNGEGAARCMMNALKDAHINGEEIDYIN 303
Cdd:cd00833 226 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVDPSDIDYVE 303

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 304 AHGTSTPAGDRAETLAIKAVLGSHAQKTP---VSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKGL 380
Cdd:cd00833 304 AHGTGTPLGDPIEVEALAKVFGGSRSADQpllIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFE 383

                       410       420       430
                ....*....|....*....|....*....|....*..
gi 76883454 381 D---YVPNIAREMKIKTVVS----NSFGFGGTNGSLI 410
Cdd:cd00833 384 EsplRVPTEARPWPAPAGPRragvSSFGFGGTNAHVI 420
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 5-248 2.50e-67

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: 214.42  E-value: 2.50e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454     5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIGPITG--FDVTNF---PVRFGGAVKG-----FEIGDYLPL------KD 68
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrWDPDKLydpPSRIAGKIYTkwgglDDIFDFDPLffgispRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    69 ARKMDPFIHYGIAAARQALEDSGLEINEANATQVGVAIGSGIGGLHGIELghnAYLQGGPRRISPFFVPsNIINMIAGNL 148
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLL---LDEDGGPRRGSPFAVG-TMPSVIAGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   149 SILYGMKGPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTrnEEPETASRPWDkdr 228
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA--- 231

                         250       260
                  ....*....|....*....|
gi 76883454   229 DGFVLSDGAGVLVLEELEHA 248
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 5-412 2.02e-66

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 217.21  E-value: 2.02e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    5 KRVAVTGLGIVCPVGVDVEGSWANLLAGKSGIG-------PITGFDVTNFPVRF-GGAVKGFEIGDYLPLKDARKMDPFI 76
Cdd:PRK07103   2 DEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGvmrrpgrQVPDDAGAGLASAFiGAELDSLALPERLDAKLLRRASLSA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   77 HYGIAAARQALEDSGLEinEANATQVGVAI-GSGIGGLHGIELgHNAYlQGGPRRISPFFVPSNIINMIAGNLSILYGMK 155
Cdd:PRK07103  82 QAALAAAREAWRDAALG--PVDPDRIGLVVgGSNLQQREQALV-HETY-RDRPAFLRPSYGLSFMDTDLVGLCSEQFGIR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  156 GPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRN--EEPETASRPWDKDRDGFVL 233
Cdd:PRK07103 158 GEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGFIY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  234 SDGAGVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPprNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGD 313
Cdd:PRK07103 238 GEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGD 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  314 RAETLAIKAVLGSHAQktpVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFN-LDPECkglDYVPNIAREMKI 392
Cdd:PRK07103 316 ETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEpIDERF---RWVGSTAESARI 389

                        410       420
                 ....*....|....*....|
gi 76883454  393 KTVVSNSFGFGGTNGSLIFR 412
Cdd:PRK07103 390 RYALSLSFGFGGINTALVLE 409
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
7-411 3.89e-66

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 215.86  E-value: 3.89e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    7 VAVTGLGIVCPVGVDVEGSWANLLAGK-SGIGPITGFDVTNFPvrFGGAVKGFE---IGDYLPLKDAR----------KM 72
Cdd:PRK09185   4 VYISAFGATSALGRGLDAILAALRAGRaSGMRPCDFWLVDLPT--WVGEVVGVElpaLPAALAAFDCRnnrlallalqQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   73 DPfihygiaAARQALEDSGleineanATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSNIINMIAGNLSILY 152
Cdd:PRK09185  82 EP-------AVEAAIARYG-------ADRIGVVLGTSTSGILEGELAYRRRDPAHGALPADYHYAQQELGSLADFLRAYL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  153 GMKGPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEmATSPTGLGGFASARALStrneepETASRPWDKDRDGFV 232
Cdd:PRK09185 148 GLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVD-SLCRLTLNGFNSLESLS------PQPCRPFSANRDGIN 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  233 LSDGAGVLVLEelehakrRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAG 312
Cdd:PRK09185 221 IGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLN 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  313 DRAETLAIKAVLGSHaqkTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPECKGLDYVPNiAREMKI 392
Cdd:PRK09185 294 DAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVEN-AQALAI 369

                        410
                 ....*....|....*....
gi 76883454  393 KTVVSNSFGFGGTNGSLIF 411
Cdd:PRK09185 370 RYVLSNSFAFGGNNCSLIF 388
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 77-410 7.14e-64

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: 208.26  E-value: 7.14e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  77 HYGIAAARQALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVPSniinmIAGNLSILYGMKG 156
Cdd:cd00825  13 ILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG-----ASGQIATPLGIHG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 157 PNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPtglggFASARALSTRNEEPETASRPWDKDRDGFVLSDG 236
Cdd:cd00825  88 PAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAP-----MDCEFDAMGALSTPEKASRTFDAAADGFVFGDG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 237 AGVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAE 316
Cdd:cd00825 163 AGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKE 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 317 TLAIKAVLGSHaqKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINIFNLDPEckgLDYVPNIAREMKIKTVV 396
Cdd:cd00825 243 LKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEA---GLNIVTETTPRELRTAL 317

                       330
                ....*....|....
gi 76883454 397 SNSFGFGGTNGSLI 410
Cdd:cd00825 318 LNGFGLGGTNATLV 331
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 3-406 6.94e-55

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 196.25  E-value: 6.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    3 SDKRVAVTGLGIVCPvGV-DVEGSWANLLAGKSGIGPITG--FDVTNF-----------PVRFGGAVKG--------FEI 60
Cdd:COG3321    2 ADEPIAIIGMACRFP-GAdDPEEFWRNLRAGRDAITEVPAdrWDADAYydpdpdapgktYVRWGGFLDDvdefdalfFGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   61 gdylPLKDARKMDP----FIHygiaAARQALEDSGLEINEANATQVGVAIGSGIGGlhgielgHNAYLQGGPRRISPFFV 136
Cdd:COG3321   81 ----SPREAEAMDPqqrlLLE----VAWEALEDAGYDPESLAGSRTGVFVGASSND-------YALLLLADPEAIDAYAL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  137 PSNIINMIAGNLSILYGMKGPNIAIVTACTTG---THnigEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALStr 213
Cdd:COG3321  146 TGNAKSVLAGRISYKLDLRGPSVTVDTACSSSlvaVH---LACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS-- 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  214 neePETASRPWDKDRDGFVLSDGAGVLVLEELEHAKRRGAQIYAEVVGFGMSAD-AYH-MTQPprNGEGAARCMMNALKD 291
Cdd:COG3321  221 ---PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgRSNgLTAP--NGPAQAAVIRRALAD 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  292 AHINGEEIDYINAHGTSTPAGDRAETLAIKAVLGSHAQKTP---VSSTKSMTGHLLGAAG--GIeaIFSVLAIRDQIAPP 366
Cdd:COG3321  296 AGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPADQpcaIGSVKSNIGHLEAAAGvaGL--IKAVLALRHGVLPP 373

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 76883454  367 TINIFNLDPEckgLD------YVPNIAREMKIKTV-----VSnSFGFGGTN 406
Cdd:COG3321  374 TLHFETPNPH---IDfenspfYVNTELRPWPAGGGprragVS-SFGFGGTN 420
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 256-370 8.94e-48

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: 158.89  E-value: 8.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   256 YAEVVGFGMSADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAETLAIKAVLGSHAQKTP--V 333
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKQPlaI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 76883454   334 SSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINI 370
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 77-410 2.23e-32

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 122.94  E-value: 2.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  77 HYGIAAARQALEDSGLEINEANATQVGVAIGSGIGglhgielghnaylQGGPRRISpffvpsniinmiagnlSILYGMKG 156
Cdd:cd00327   9 ELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEF-------------SGAAGQLA----------------YHLGISGG 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 157 PNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMatsptglggfasaralstrneepetasrpwdkdrdgFVLSDG 236
Cdd:cd00327  60 PAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGDG 103

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 237 AGVLVLEELEHAKRRGAQIYAEVVGFGMSADAYHMTQPPrNGEGAARCMMNALKDAHINGEEIDYINAHGTSTPAGDRAE 316
Cdd:cd00327 104 AAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAV-SGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVE 182

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454 317 TLAIKAVLGSHAqkTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTinifnldpeckgldyvPNIARemkikTVV 396
Cdd:cd00327 183 LALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------------PREPR-----TVL 239

                       330
                ....*....|....
gi 76883454 397 SNSFGFGGTNGSLI 410
Cdd:cd00327 240 LLGFGLGGTNAAVV 253
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 137-413 3.21e-31

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: 126.66  E-value: 3.21e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    137 PSNIINMIAGNLSILYGMKGPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTrNEE 216
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTT-NED 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    217 petaSRPWDKDRDGFVLSDGAGVLVLEELEHAKRRGAQIYAEVVGFGMSADA-YHMTQPPRNgEGAARCMMNALKDAHIN 295
Cdd:TIGR02813  257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkFKSIYAPRP-EGQAKALKRAYDDAGFA 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    296 GEEIDYINAHGTSTPAGDRAETLAIKAVLG---SHAQKTPVSSTKSMTGHLLGAAGGIEAIFSVLAIRDQIAPPTINI-- 370
Cdd:TIGR02813  332 PHTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVdq 411

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 76883454    371 -----------FNLDPECKgldyvPNIARE--MKIKTVVSnSFGFGGTNGSLIFRQ 413
Cdd:TIGR02813  412 pnpkldienspFYLNTETR-----PWMQREdgTPRRAGIS-SFGFGGTNFHMVLEE 461
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 7-413 1.05e-21

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: 94.32  E-value: 1.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454      7 VAVTGLGIVCPVGVDVEGSWANLLAGKSGIGpitGFDvtnfPVRFGgavkgfeigdyLPLKDARKMDP----FIHygiaA 82
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD---LFD----AAFFG-----------ISPREAEAMDPqqrlLLE----V 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454     83 ARQALEDSGLEINEANATQVGVAIGSGigglhgielgHNAYlqggprrispffvpsniinmiagnlsilygmkgpNIAIV 162
Cdd:smart00825  59 AWEALEDAGIDPESLRGSRTGVFVGVS----------SSDY----------------------------------SVTVD 94

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    163 TACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALStrneePETASRPWDKDRDGFVLSDGAGVLVL 242
Cdd:smart00825  95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVL 169

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    243 EELEHAKRRGAQIYAEVVGFGMSADAYH--MTQPprNGEgaarcmmnalkdahingeeidyinahgtstpagdraetlai 320
Cdd:smart00825 170 KRLSDALRDGDPILAVIRGSAVNQDGRSngITAP--SGP----------------------------------------- 206

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    321 kavlgshAQkTPVSSTKSMTGHLLGAAG--GIeaIFSVLAIRDQIAPPTINIFNLDPEckgLD------YVPNIAREM-- 390
Cdd:smart00825 207 -------AQ-LLIGSVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPH---IDleesplRVPTELTPWpp 273

                          410       420
                   ....*....|....*....|....*
gi 76883454    391 --KIKTVVSNSFGFGGTNGSLIFRQ 413
Cdd:smart00825 274 pgRPRRAGVSSFGFGGTNAHVILEE 298
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
1-347 3.27e-10

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 61.51  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    1 MLSDKRVAVTGLGIVCPVGVDVEGSWANLLAGKsgIGPITgfDVTNF---------PVRFGGAV--KGfeigdylplkDA 69
Cdd:PRK06519   2 RMQPNDVVITGIGLVSSLGEGLDAHWNALSAGR--PQPNV--DTETFapypvhplpEIDWSQQIpkRG----------DQ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   70 RKMDPFIHYGIAAARQALEDSGLEINEA--NATQVGVAIGSG---------------IGGLHGIELghNAYLQGGPRris 132
Cdd:PRK06519  68 RQMETWQRLGTYAAGLALDDAGIKGNEEllSTMDMIVAAGGGerdiavdtailnearKRNDRGVLL--NERLMTELR--- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  133 PFFVPSNIINMIAGNLSILYGMKGPNIAIVTACTTGTHNIGEAVRIIQRGEAKVMIAGGAEMATSPTGLGGFASARALST 212
Cdd:PRK06519 143 PTLFLAQLSNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLK 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  213 RNEEPETASRPWDKDrdGFVLSDGAGVLVLEELEHAKRRGAQIYAEVVgfGMSADayhmtQPPRNGEGAARCMMNALKDA 292
Cdd:PRK06519 223 GGWAPVWSRGGEDGG--GFILGSGGAFLVLESREHAEARGARPYARIS--GVESD-----RARRAPGDLEASLERLLKPA 293

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 76883454  293 HINGEeidyiNAHGTSTPAGDRAETLAIKAVLGSHAqKTPVSSTKSMTGHLLGAA 347
Cdd:PRK06519 294 GGLAA-----PTAVISGATGAHPATAEEKAALEAAL-AGPVRGIGTLFGHTMEAQ 342
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 6-302 4.79e-05

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 45.01  E-value: 4.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454    6 RVAVTGLGIVCPVGVDvegSWANLLAGKSGIgpiTGFDVTNFPVR-FGGAVKGFEIGDYLPLKDARKMdpfihygIAAAR 84
Cdd:PRK06147   4 ALAIVGSGMVTAVGLD---APSSCAAIRARL---DNFQETRFIDPpGGEWLIGAPVPLPPPWRGPERL-------AEMAA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454   85 QALEDSGLEINEANATQVGVAIGSGIGGLHGIELGHNAYLQGGPRRISPFFVP--SNIINmiAGNLSilygmkgpniaiv 162
Cdd:PRK06147  71 PAIAEALEGLPALDASEAPLLLCVAEEERPGRPPDLEERLLRELEARLGLRLEpgSAVIA--RGRVS------------- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  163 tacttGTHNIGEAVR-IIQRGEAKVMIAGGAEMATSPTGLGGFASARALSTRNEEpetasrpwdkdrdGFVLSDGAGVLV 241
Cdd:PRK06147 136 -----GAVALAQARRlIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNSN-------------GFIPGEAAAAVL 197

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76883454  242 LEELEHAKRRGAQIYAevVGFGM-SADAYHMTQPPRNGEGAARCMMNALKDAHINGEEIDYI 302
Cdd:PRK06147 198 LGRPAGGEAPGLPLLG--LGLGRePAPVGESEDLPLRGDGLTQAIRAALAEAGCGLEDMDYR 257
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
 222-361 4.50e-03

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 38.92  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76883454  222 RPWDKDRDGFV-------LSDGAGVLVLEELEHAKRRGAQIYAEVVGFgmsADAyhmTQPPRNGEGA-ARCMMNALKDAH 293
Cdd:PLN02644 232 RPSFKEDGGSVtagnassISDGAAALVLVSGEKALELGLQVIAKIRGY---ADA---AQAPELFTTApALAIPKALKHAG 305

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76883454  294 INGEEIDY--INAHGTSTpagdraeTLAIKAVLGSHAQKTPVSSTKSMTGHLLGAAGG--IEAIFSVLAIRD 361
Cdd:PLN02644 306 LEASQVDYyeINEAFSVV-------ALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGAriLVTLLGVLRSKN 370
 
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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