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Conserved domains on  [gi|56314587|emb|CAI09232|]
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Beta-ketoacyl-(acyl-carrier-protein) synthase [Aromatoleum aromaticum EbN1]

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 ...
 4-410 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: 767.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587     4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    84 QAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   164 CTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   244 YEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRCF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   324 GDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGGT 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400


                  ....*..
gi 56314587   404 NGTLAFR 410
Cdd:TIGR03150 401 NASLVFK 407
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 4-410 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: 767.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587     4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    84 QAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   164 CTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   244 YEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRCF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   324 GDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGGT 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400


                  ....*..
gi 56314587   404 NGTLAFR 410
Cdd:TIGR03150 401 NASLVFK 407
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-412 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 764.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    3 RRRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAG 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   83 IQAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  163 ACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  243 EYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRC 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  323 FGDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400

                        410
                 ....*....|
gi 56314587  403 TNGTLAFRRI 412
Cdd:PRK07314 401 TNASLVFKRY 410
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 4-412 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: 701.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  84 QAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVTA 163
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 164 CTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 244 YEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRCF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 324 GDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGGT 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400


                ....*....
gi 56314587 404 NGTLAFRRI 412
Cdd:COG0304 401 NASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 4-409 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: 644.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  84 QAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVTA 163
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 164 CTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 244 YEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRCF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 324 GDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGGT 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400


                ....*.
gi 56314587 404 NGTLAF 409
Cdd:cd00834 401 NASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 4-247 1.21e-64

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: 207.10  E-value: 1.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587     4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEI--TRFDASSF---PVRIAGEVRG----------FDIGAY-LSPKE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddifdFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    68 ARRMDVFIHYGLAAGIQAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEAThddFLKGGARKISPFFIpGTIINMIAGNL 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLL---DEDGGPRRGSPFAV-GTMPSVIAGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   148 SIMLGLKGPCLAMVTACTTAtHCIGEAA-RLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTrnDDPLTASRPWDkg 226
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSS-LVAIHAAvQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA-- 231

                         250       260
                  ....*....|....*....|.
gi 56314587   227 rDGFVLGEGAGVLVLEEYEHA 247
Cdd:pfam00109 232 -DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 6-404 5.06e-25

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: 103.56  E-value: 5.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587      6 VVITGLGIISPVGNTVPEAWDNIvngRSGIGEITRFDASsFpvriagevrgFDIgaylSPKEARRMD----VFihygLAA 81
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLL---LAGLDDVDLFDAA-F----------FGI----SPREAEAMDpqqrLL----LEV 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587     82 GIQAFRDAGLDVTASNAERIGVNLGsgigglpmieATHDDFlkggarkispffipgtiinmiagnlsimlglkgpCLAMV 161
Cdd:smart00825  59 AWEALEDAGIDPESLRGSRTGVFVG----------VSSSDY----------------------------------SVTVD 94

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    162 TACT---TATHcigEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALStrnddPLTASRPWDKGRDGFVLGEGAGV 238
Cdd:smart00825  95 TACSsslVALH---LACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGV 166

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    239 LVLEEYEHAKARGARIYAEISGYGMSADAYH--MTAPaedgDGAARCmanamrdarmtveeidyvnahgtstPLGdlaet 316
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAP----SGPAQL-------------------------LIG----- 212

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    317 tavkrcfgdrarsivvnSTKSMTGHLLGAAgGVEAVF-TALALHNQIAPPTINIFEQDERCDLD----YVANKARPME-- 389
Cdd:smart00825 213 -----------------SVKSNIGHLEAAA-GVAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPpp 274

                          410
                   ....*....|....*..
gi 56314587    390 --IRAALSNSFGFGGTN 404
Cdd:smart00825 275 grPRRAGVSSFGFGGTN 291
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 4-410 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: 767.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587     4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    84 QAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   164 CTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   244 YEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRCF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   324 GDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGGT 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400


                  ....*..
gi 56314587   404 NGTLAFR 410
Cdd:TIGR03150 401 NASLVFK 407
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-412 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 764.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    3 RRRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAG 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   83 IQAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  163 ACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  243 EYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRC 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  323 FGDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400

                        410
                 ....*....|
gi 56314587  403 TNGTLAFRRI 412
Cdd:PRK07314 401 TNASLVFKRY 410
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 4-412 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: 701.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  84 QAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVTA 163
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 164 CTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 244 YEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRCF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 324 GDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGGT 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400


                ....*....
gi 56314587 404 NGTLAFRRI 412
Cdd:COG0304 401 NASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 4-409 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: 644.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  84 QAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVTA 163
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 164 CTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 244 YEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRCF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 324 GDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGGT 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400


                ....*.
gi 56314587 404 NGTLAF 409
Cdd:cd00834 401 NASLVF 406
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
1-412 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 548.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    1 MTRRRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLA 80
Cdd:PRK08722   1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   81 AGIQAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAM 160
Cdd:PRK08722  81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  161 VTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLV 240
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  241 LEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVK 320
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  321 RCFGDR-ARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPME-IRAALSNSF 398
Cdd:PRK08722 321 RALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNSF 400

                        410
                 ....*....|....
gi 56314587  399 GFGGTNGTLAFRRI 412
Cdd:PRK08722 401 GFGGTNGSLIFKKM 414
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-411 0e+00

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 547.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    1 MTRRRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVR--------GFDIGAYLSPKEARRMD 72
Cdd:PRK06333   1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlaedaeaGFDPDRYLDPKDQRKMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   73 VFIHYGLAAGIQAFRDAGLD-VTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIML 151
Cdd:PRK06333  81 RFILFAMAAAKEALAQAGWDpDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  152 GLKGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTR-NDDPLTASRPWDKGRDGF 230
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  231 VLGEGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPL 310
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  311 GDLAETTAVKRCFGdRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCD-LDYVANKARPME 389
Cdd:PRK06333 321 GDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399

                        410       420
                 ....*....|....*....|..
gi 56314587  390 IRAALSNSFGFGGTNGTLAFRR 411
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRR 421
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 4-412 0e+00

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 515.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   84 QAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVTA 163
Cdd:PRK08439  82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  164 CTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGAGVLVLEE 243
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  244 YEHAKARGARIYAEISGYGMSADAYHMTAPAEdgDGAARCMANAMRDARMTveEIDYVNAHGTSTPLGDLAETTAVKRCF 323
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAALKELF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  324 GDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNSFGFGGT 403
Cdd:PRK08439 318 GSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGT 397


                 ....*....
gi 56314587  404 NGTLAFRRI 412
Cdd:PRK08439 398 NGVVIFKKV 406
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 13-412 3.56e-166

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 472.64  E-value: 3.56e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   13 IISPVGNTVPEAWDNIVNGRSGIGEITRFDA----------------SSFPVRIAGEVRG--FDIGAYLSPKearRMDVF 74
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDQseFDPSDFAPTK---RESRA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   75 IHYGLAAGIQAFRDAGLDVTAS-NAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGL 153
Cdd:PTZ00050  78 THFAMAAAREALADAKLDILSEkDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  154 KGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTR-NDDPLTASRPWDKGRDGFVL 232
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  233 GEGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRD-ARMTVEEIDYVNAHGTSTPLG 311
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANININDVDYVNAHATSTPIG 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  312 DLAETTAVKRCFGDR-ARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKAR--PM 388
Cdd:PTZ00050 318 DKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAhpLQ 397

                        410       420
                 ....*....|....*....|....
gi 56314587  389 EIRAALSNSFGFGGTNGTLAFRRI 412
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 4-412 5.34e-149

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 429.60  E-value: 5.34e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDA--------------SSFPVRIAGEV-RGFDIGAYLSPK-- 66
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLkmksedeetqlytlDQLPSRVAALVpRGTGPGDFDEELwl 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   67 EARRMDVFIHYGLAAGIQAFRDAG-LDVTASNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAG 145
Cdd:PLN02836  86 NSRSSSRFIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAAG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  146 NLSIMLGLKGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTR-NDDPLTASRPWD 224
Cdd:PLN02836 166 HVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPFD 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  225 KGRDGFVLGEGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAH 304
Cdd:PLN02836 246 CDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAH 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  305 GTSTPLGDLAETTAVKRCFGDRARS--IVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVA 382
Cdd:PLN02836 326 ATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVP 405

                        410       420       430
                 ....*....|....*....|....*....|.
gi 56314587  383 NKARP-MEIRAALSNSFGFGGTNGTLAFRRI 412
Cdd:PLN02836 406 LTASKaMLIRAALSNSFGFGGTNASLLFTSP 436
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 1-409 3.41e-134

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 395.50  E-value: 3.41e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    1 MTRRRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLA 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   81 AGIQAFRDAGL--DVTAS-NAERIGVNLGSGIGGLPM----IEAthddfLKGGARKISPFFIPGTIINMIAGNLSIMLGL 153
Cdd:PLN02787 206 AGKKALADGGIteDVMKElDKTKCGVLIGSAMGGMKVfndaIEA-----LRISYRKMNPFCVPFATTNMGSAMLAMDLGW 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  154 KGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLG 233
Cdd:PLN02787 281 MGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMG 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  234 EGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDL 313
Cdd:PLN02787 361 EGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDL 440

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  314 AETTAVKRCFGDRARsIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLD-YVANKARPMEIRA 392
Cdd:PLN02787 441 KEYQALMRCFGQNPE-LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKvLVGPKKERLDIKV 519

                        410
                 ....*....|....*..
gi 56314587  393 ALSNSFGFGGTNGTLAF 409
Cdd:PLN02787 520 ALSNSFGFGGHNSSILF 536
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
4-411 2.25e-109

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 327.40  E-value: 2.25e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRgFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   84 QAFRDAGLDVTASNAERIGVNLGSGIG-GLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVT 162
Cdd:PRK07967  81 QAIADAGLSEEQVSNPRTGLIAGSGGGsTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  163 ACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGgFASAKALSTR-NDDPLTASRPWDKGRDGFVLGEGAGVLVL 241
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVVV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  242 EEYEHAKARGARIYAEISGYGMSADAYHMTAPAedGDGAARCMANAMRdarmTVE-EIDYVNAHGTSTPLGDLAETTAVK 320
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYDMVAPS--GEGAVRCMQMALA----TVDtPIDYINTHGTSTPVGDVKELGAIR 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  321 RCFGDRARSIvvNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDER-CDLDYVANKARPMEIRAALSNSFG 399
Cdd:PRK07967 314 EVFGDKSPAI--SATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNSFG 391

                        410
                 ....*....|..
gi 56314587  400 FGGTNGTLAFRR 411
Cdd:PRK07967 392 FGGTNATLVFRR 403
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 99-411 3.29e-105

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 314.74  E-value: 3.29e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   99 ERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCLAMVTACTTATHCIGEAARLI 178
Cdd:PRK14691  26 ERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  179 QYGDVDVMVAGGAESTVTPLAVGGFASAKALSTR-NDDPLTASRPWDKGRDGFVLGEGAGVLVLEEYEHAKARGARIYAE 257
Cdd:PRK14691 106 RNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAE 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  258 ISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRCFGDrARSIVVNSTKS 337
Cdd:PRK14691 186 IVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITSTKS 264

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56314587  338 MTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCD-LDYVANKARPMEIRAALSNSFGFGGTNGTLAFRR 411
Cdd:PRK14691 265 ATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
6-411 9.54e-101

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 305.89  E-value: 9.54e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    6 VVITGLGIISPVGNTVPEAWDNIVNGRSGIGE-----ITRFDassFPVRIAGE-VRGFDigAYLSPKEARRMDVFIHYGL 79
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTlddpfVEEFD---LPVRIGGHlLEEFD--HQLTRVELRRMSYLQRMST 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   80 AAGIQAFRDAGL-DVtasNAERIGVNLGSGIGGLPMIEATHDDFLKGGARKISPFFIPGTIINMIAGNLSIMLGLKGPCL 158
Cdd:PRK07910  89 VLGRRVWENAGSpEV---DTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  159 AMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKA-LSTRNDDPLTASRPWDKGRDGFVLGEGAG 237
Cdd:PRK07910 166 TPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGA 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  238 VLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETT 317
Cdd:PRK07910 246 LMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGK 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  318 AVKRCFGDRARSivVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAALSNS 397
Cdd:PRK07910 326 AINNALGGHRPA--VYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNS 403

                        410
                 ....*....|....
gi 56314587  398 FGFGGTNGTLAFRR 411
Cdd:PRK07910 404 FGFGGHNVALAFGR 417
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
6-411 7.88e-100

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 303.86  E-value: 7.88e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    6 VVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMdvfihyGLAAGIQA 85
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPESPFGASALSEAL------ARLAAEEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   86 FRDAGLDVTASN--------------------AERIGVNlgsgigglpmIEATHDDFLKGGARKISPFFIPGTIINMIAG 145
Cdd:PRK06501  87 LAQAGIGKGDFPgplflaappvelewparfalAAAVGDN----------DAPSYDRLLRAARGGRFDALHERFQFGSIAD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  146 NLSIMLGLKGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDDPLTASRPWDK 225
Cdd:PRK06501 157 RLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  226 GRDGFVLGEGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHG 305
Cdd:PRK06501 237 DRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  306 TSTPLGDLAETTAVKRCFGDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKA 385
Cdd:PRK06501 317 TSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVA 396

                        410       420
                 ....*....|....*....|....*.
gi 56314587  386 RPMEIRAALSNSFGFGGTNGTLAFRR 411
Cdd:PRK06501 397 RDARVTAVLSNSFGFGGQNASLVLTA 422
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
4-410 8.69e-100

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 303.06  E-value: 8.69e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGI---GEITRFDasSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLA 80
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVrrmPEWDRYD--GLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   81 AGIQAFRDAGL--DVTASNAeRIGVNLGSGIGGLPMIEATHDDFLKGGARKISPffipGTIINMI----AGNLSIMLGLK 154
Cdd:PRK09116  80 ASELALEDAGLlgDPILTDG-RMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITA----TTYVRMMphttAVNVGLFFGLK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  155 GPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAEStVTPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGE 234
Cdd:PRK09116 155 GRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  235 GAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPaeDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLA 314
Cdd:PRK09116 234 GAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQP--QAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIA 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  315 ETTAVKRCFGDRarsIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERC-DLDYVANKARPMEIRAA 393
Cdd:PRK09116 312 ESQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYV 388

                        410
                 ....*....|....*..
gi 56314587  394 LSNSFGFGGTNGTLAFR 410
Cdd:PRK09116 389 MSNNFAFGGINTSLIFK 405
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 4-407 6.72e-90

"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: 277.78  E-value: 6.72e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   4 RRVVITGLGIISPVGN---TVPEAWDNIVNGRSGIGEITRFDaSSFPVRIAGEVRGFDIGAYlSPKEARRMDVFIHYGLA 80
Cdd:cd00828   1 SRVVITGIGVVSPHGEgcdEVEEFWEALREGRSGIAPVARLK-SRFDRGVAGQIPTGDIPGW-DAKRTGIVDRTTLLALV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  81 AGIQAFRDAGL-DVTASNAERIGVNLGSGIGGLPMIEathdDFLKGGARKISPFFIPGTI--INMIAGNLSIMLGLK-GP 156
Cdd:cd00828  79 ATEEALADAGItDPYEVHPSEVGVVVGSGMGGLRFLR----RGGKLDARAVNPYVSPKWMlsPNTVAGWVNILLLSShGP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 157 CLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVtPLAVGGFASAKALSTRNDDPLTASRPWDKGRDGFVLGEGA 236
Cdd:cd00828 155 IKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL-EEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 237 GVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAeDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAET 316
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 317 TAVKRCFGDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKAR--PMEIRAAL 394
Cdd:cd00828 313 RAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRdlNLKVRAAL 392

                       410
                ....*....|...
gi 56314587 395 SNSFGFGGTNGTL 407
Cdd:cd00828 393 VNAFGFGGSNAAL 405
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 4-407 3.32e-79

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: 249.97  E-value: 3.32e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIHYGLAAGI 83
Cdd:cd00832   1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  84 QAFRDAGLDVTASNAERIGVNLGSGIGGLpmiEATHDDFLK---GGARKISP------FFIPGTiinmiaGNLSIMLGLK 154
Cdd:cd00832  81 WALADAGVDPAALPPYDMGVVTASAAGGF---EFGQRELQKlwsKGPRHVSAyqsfawFYAVNT------GQISIRHGMR 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 155 GPCLAMVTACTTATHCIGEAARLIQYGdVDVMVAGGAESTVTPLAVGGFASAKALSTrNDDPLTASRPWDKGRDGFVLGE 234
Cdd:cd00832 152 GPSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGE 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 235 GAGVLVLEEYEHAKARGARIYAEISGYGMSADAyhmtAPAED-GDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDL 313
Cdd:cd00832 230 GGAILVLEDAAAARERGARVYGEIAGYAATFDP----PPGSGrPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDR 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 314 AETTAVKRCFGdrARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRAA 393
Cdd:cd00832 306 AEAAALAAVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTA 383

                       410
                ....*....|....
gi 56314587 394 LSNSFGFGGTNGTL 407
Cdd:cd00832 384 LVLARGRGGFNSAL 397
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
5-411 2.19e-77

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 244.58  E-value: 2.19e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    5 RVVITGLGIISPVGNtVPEAWDNIVNGRSGIGEITRF-DASSFPVRIagevrgfdIGAYLSPKEA-RRMDVfihyglaag 82
Cdd:PRK05952   3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQPFpELPPLPLGL--------IGNQPSSLEDlTKTVV--------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   83 IQAFRDAGLDVTASNAeriGVNLGSGIGGLPMIEAthddflkgGARKISPFFIPG-----------TIINMIAGNLSIML 151
Cdd:PRK05952  65 TAALKDAGLTPPLTDC---GVVIGSSRGCQGQWEK--------LARQMYQGDDSPdeeldlenwldTLPHQAAIAAARQI 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  152 GLKGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTrnddplTASRPWDKGRDGFV 231
Cdd:PRK05952 134 GTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGLV 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  232 LGEGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLG 311
Cdd:PRK05952 208 LGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLN 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  312 DLAETTAVKRCFGDRarsIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIfeQDERCDLDYVaNKARPMEIR 391
Cdd:PRK05952 288 DQREANLIQALFPHR---VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGL--QEPEFDLNFV-RQAQQSPLQ 361

                        410       420
                 ....*....|....*....|
gi 56314587  392 AALSNSFGFGGTNGTLAFRR 411
Cdd:PRK05952 362 NVLCLSFGFGGQNAAIALGK 381
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 5-404 3.22e-76

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: 242.85  E-value: 3.22e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   5 RVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEIT--RFDASSFP----------VRIAGEVRGFDIGA----YLSPKEA 68
Cdd:cd00833   2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedRWDADGYYpdpgkpgktyTRRGGFLDDVDAFDaaffGISPREA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  69 RRMD----VFihygLAAGIQAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDflkggarKISPFFIPGTIINMIA 144
Cdd:cd00833  82 EAMDpqqrLL----LEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPD-------EIDAYAATGTSRAFLA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 145 GNLSIMLGLKGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALStrnddPLTASRPWD 224
Cdd:cd00833 151 NRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCRPFD 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 225 KGRDGFVLGEGAGVLVLEEYEHAKARGARIYAEISGYGMSADAY--HMTAPaeDGDGAARCMANAMRDARMTVEEIDYVN 302
Cdd:cd00833 226 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVDPSDIDYVE 303

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 303 AHGTSTPLGDLAETTAVKRCFG---DRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLD 379
Cdd:cd00833 304 AHGTGTPLGDPIEVEALAKVFGgsrSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFE 383

                       410       420       430
                ....*....|....*....|....*....|....
gi 56314587 380 ----YVANKARPME-----IRAALsNSFGFGGTN 404
Cdd:cd00833 384 esplRVPTEARPWPapagpRRAGV-SSFGFGGTN 416
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 5-411 3.01e-75

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 239.93  E-value: 3.01e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    5 RVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITR--------FDASSFPVRIAGEVRGFDIGAYLSPKEARRMDVFIH 76
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRpgrqvpddAGAGLASAFIGAELDSLALPERLDAKLLRRASLSAQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   77 YGLAAGIQAFRDAGLDVTASNaeRIG-VNLGSGIGGLPMIEAtHDDFlKGGARKISPFFIPGTIINMIAGNLSIMLGLKG 155
Cdd:PRK07103  83 AALAAAREAWRDAALGPVDPD--RIGlVVGGSNLQQREQALV-HETY-RDRPAFLRPSYGLSFMDTDLVGLCSEQFGIRG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  156 PCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRN--DDPLTASRPWDKGRDGFVLG 233
Cdd:PRK07103 159 EGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGFIYG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  234 EGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPaeDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDL 313
Cdd:PRK07103 239 EACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDE 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  314 AETTAVKRCFGDRARsivVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQ-DERCdlDYVANKARPMEIRA 392
Cdd:PRK07103 317 TELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTAESARIRY 391

                        410
                 ....*....|....*....
gi 56314587  393 ALSNSFGFGGTNGTLAFRR 411
Cdd:PRK07103 392 ALSLSFGFGGINTALVLER 410
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
6-411 1.91e-72

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 232.04  E-value: 1.91e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    6 VVITGLGIISPVGNTVPEAWDNIVNGRSGIGEITRFDASSFPVRIaGEVRGFD---IGAYLSPKEAR--RMdvfihygLA 80
Cdd:PRK09185   4 VYISAFGATSALGRGLDAILAALRAGRASGMRPCDFWLVDLPTWV-GEVVGVElpaLPAALAAFDCRnnRL-------AL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   81 AGIQAFRDAGLDVTAS-NAERIGVNLG---SGIG----GLPMIEATHDDFLKGgarkispFFIPGTIINMIAGNLSIMLG 152
Cdd:PRK09185  76 LALQQIEPAVEAAIARyGADRIGVVLGtstSGILegelAYRRRDPAHGALPAD-------YHYAQQELGSLADFLRAYLG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  153 LKGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAEStVTPLAVGGFASAKALSTrnddplTASRPWDKGRDGFVL 232
Cdd:PRK09185 149 LSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSP------QPCRPFSANRDGINI 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  233 GEGAGVLVLEeyehaKARGARIYaeISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGD 312
Cdd:PRK09185 222 GEAAAFFLLE-----REDDAAVA--LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLND 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  313 LAETTAVKRCFGDRarsIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDERCDLDYVANKARPMEIRA 392
Cdd:PRK09185 295 AMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIRY 371

                        410
                 ....*....|....*....
gi 56314587  393 ALSNSFGFGGTNGTLAFRR 411
Cdd:PRK09185 372 VLSNSFAFGGNNCSLIFGR 390
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 4-247 1.21e-64

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: 207.10  E-value: 1.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587     4 RRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEI--TRFDASSF---PVRIAGEVRG----------FDIGAY-LSPKE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddifdFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    68 ARRMDVFIHYGLAAGIQAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEAThddFLKGGARKISPFFIpGTIINMIAGNL 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLL---DEDGGPRRGSPFAV-GTMPSVIAGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   148 SIMLGLKGPCLAMVTACTTAtHCIGEAA-RLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTrnDDPLTASRPWDkg 226
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSS-LVAIHAAvQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA-- 231

                         250       260
                  ....*....|....*....|.
gi 56314587   227 rDGFVLGEGAGVLVLEEYEHA 247
Cdd:pfam00109 232 -DGFVRGEGVGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 73-408 9.03e-62

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: 202.48  E-value: 9.03e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  73 VFIHYGLAAGIQAFRDAGLDVTASNAERIGVNLGSGIGGlpmIEATHddFLKGGARKISPFFIPGTIINMIAGNLSIMLG 152
Cdd:cd00825  10 YVSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGS---PRFQV--FGADAMRAVGPYVVTKAMFPGASGQIATPLG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 153 LKGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALStrnddPLTASRPWDKGRDGFVL 232
Cdd:cd00825  85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVF 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 233 GEGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGD 312
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 313 LAETTAVKRCFGDRARsiVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQDErcDLDYVANKARPMEIRA 392
Cdd:cd00825 240 VKELKLLRSEFGDKSP--AVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRT 315

                       330
                ....*....|....*.
gi 56314587 393 ALSNSFGFGGTNGTLA 408
Cdd:cd00825 316 ALLNGFGLGGTNATLV 331
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-404 5.16e-60

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 210.88  E-value: 5.16e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    1 MTRRRVVITGLGIISPVGNTVPEAWDNIVNGRSGIGEIT--RFDASSF-----------PVRIAG---EVRGFDIGAY-L 63
Cdd:COG3321    1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPadRWDADAYydpdpdapgktYVRWGGfldDVDEFDALFFgI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   64 SPKEARRMD----VFihygLAAGIQAFRDAGLDVTASNAERIGVNLGSGIGGLPMIEATHDDflkggarKISPFFIPGTI 139
Cdd:COG3321   81 SPREAEAMDpqqrLL----LEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPE-------AIDAYALTGNA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  140 INMIAGNLSIMLGLKGPCLAMVTACTT---ATHcigEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDdp 216
Cdd:COG3321  150 KSVLAGRISYKLDLRGPSVTVDTACSSslvAVH---LACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGR-- 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  217 ltaSRPWDKGRDGFVLGEGAGVLVLEEYEHAKARGARIYAEISGYGMSAD-AYH-MTAPaeDGDGAARCMANAMRDARMT 294
Cdd:COG3321  225 ---CRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgRSNgLTAP--NGPAQAAVIRRALADAGVD 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  295 VEEIDYVNAHGTSTPLGDLAETTAVKRCFG---DRARSIVVNSTKSMTGHLLGAAG--GVeaVFTALALHNQIAPPTINi 369
Cdd:COG3321  300 PATVDYVEAHGTGTPLGDPIEAAALTAAFGqgrPADQPCAIGSVKSNIGHLEAAAGvaGL--IKAVLALRHGVLPPTLH- 376

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 56314587  370 FEQ-DERCDLD----YVANKARPMEI-----RAALSnSFGFGGTN 404
Cdd:COG3321  377 FETpNPHIDFEnspfYVNTELRPWPAgggprRAGVS-SFGFGGTN 420
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 255-369 1.11e-46

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 156.19  E-value: 1.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   255 YAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTVEEIDYVNAHGTSTPLGDLAETTAVKRCFGDRARS--IVV 332
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 56314587   333 NSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINI 369
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 136-404 3.00e-35

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: 138.60  E-value: 3.00e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    136 PGTIINMIAGNLSIMLGLKGPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTRNDd 215
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    216 pltaSRPWDKGRDGFVLGEGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMTAPAEDGDGAARCMANAMRDARMTV 295
Cdd:TIGR02813  257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAP 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    296 EEIDYVNAHGTSTPLGDLAETTAVKRCFG---DRARSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTINIFEQ 372
Cdd:TIGR02813  333 HTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP 412

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 56314587    373 DERCDLD----YVANKARP-------MEIRAALSnSFGFGGTN 404
Cdd:TIGR02813  413 NPKLDIEnspfYLNTETRPwmqredgTPRRAGIS-SFGFGGTN 454
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 144-407 3.16e-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: 122.55  E-value: 3.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 144 AGNLSIMLGLK-GPCLAMVTACTTATHCIGEAARLIQYGDVDVMVAGGAEStvtplavggfasakalstrnddpltasrp 222
Cdd:cd00327  47 AGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE----------------------------- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 223 wdkgrdgFVLGEGAGVLVLEEYEHAKARGARIYAEISGYGMSADAYHMtAPAEDGDGAARCMANAMRDARMTVEEIDYVN 302
Cdd:cd00327  98 -------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVE 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587 303 AHGTSTPLGDLAETTAVKRCFGDraRSIVVNSTKSMTGHLLGAAGGVEAVFTALALHNQIAPPTinifeqdercdldyva 382
Cdd:cd00327 170 AHGTGTPIGDAVELALGLDPDGV--RSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------- 231

                       250       260
                ....*....|....*....|....*
gi 56314587 383 nkarPMEIRAALSNSFGFGGTNGTL 407
Cdd:cd00327 232 ----PREPRTVLLLGFGLGGTNAAV 252
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 6-404 5.06e-25

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: 103.56  E-value: 5.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587      6 VVITGLGIISPVGNTVPEAWDNIvngRSGIGEITRFDASsFpvriagevrgFDIgaylSPKEARRMD----VFihygLAA 81
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLL---LAGLDDVDLFDAA-F----------FGI----SPREAEAMDpqqrLL----LEV 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587     82 GIQAFRDAGLDVTASNAERIGVNLGsgigglpmieATHDDFlkggarkispffipgtiinmiagnlsimlglkgpCLAMV 161
Cdd:smart00825  59 AWEALEDAGIDPESLRGSRTGVFVG----------VSSSDY----------------------------------SVTVD 94

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    162 TACT---TATHcigEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALStrnddPLTASRPWDKGRDGFVLGEGAGV 238
Cdd:smart00825  95 TACSsslVALH---LACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGV 166

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    239 LVLEEYEHAKARGARIYAEISGYGMSADAYH--MTAPaedgDGAARCmanamrdarmtveeidyvnahgtstPLGdlaet 316
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAP----SGPAQL-------------------------LIG----- 212

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    317 tavkrcfgdrarsivvnSTKSMTGHLLGAAgGVEAVF-TALALHNQIAPPTINIFEQDERCDLD----YVANKARPME-- 389
Cdd:smart00825 213 -----------------SVKSNIGHLEAAA-GVAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPpp 274

                          410
                   ....*....|....*..
gi 56314587    390 --IRAALSNSFGFGGTN 404
Cdd:smart00825 275 grPRRAGVSSFGFGGTN 291
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
1-358 6.26e-12

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 66.52  E-value: 6.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587    1 MTRRRVVITGLGIISPVGNTVPEAWDNIVNGRSGigeiTRFDASSF---PVRIAGEVrgfDIGAYLsPKEA--RRMDVFI 75
Cdd:PRK06519   3 MQPNDVVITGIGLVSSLGEGLDAHWNALSAGRPQ----PNVDTETFapyPVHPLPEI---DWSQQI-PKRGdqRQMETWQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587   76 HYGL-AAGIqAFRDAGLdvtASNAERIG-----VNLGSGIGGLPMIEATHDDFLKGGAR----------KISPFFIPGTI 139
Cdd:PRK06519  75 RLGTyAAGL-ALDDAGI---KGNEELLStmdmiVAAGGGERDIAVDTAILNEARKRNDRgvllnerlmtELRPTLFLAQL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  140 INMIAGNLSIMLGLKGPC-------LAMVTACTTAthcigeAARlIQYGDVDVMVAGGAESTVTPLAVGGFASAKALSTR 212
Cdd:PRK06519 151 SNLLAGNISIVHKVTGSSrtfmgeeSAGVSAIEIA------FAR-IASGQSDHALVGGAYNAERPDMLLLYELGGLLLKG 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  213 NDDPLTASRPWDKGrdGFVLGEGAGVLVLEEYEHAKARGARIYAEISgyGMSADayhmTAPAEDGDGAARcmANAMRDAR 292
Cdd:PRK06519 224 GWAPVWSRGGEDGG--GFILGSGGAFLVLESREHAEARGARPYARIS--GVESD----RARRAPGDLEAS--LERLLKPA 293

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56314587  293 MTVEEIDYVNAhGTStplgDLAETTAVKRCFGDRARSIVVNSTKSMTGHLLGAAGGVEAVFTALAL 358
Cdd:PRK06519 294 GGLAAPTAVIS-GAT----GAHPATAEEKAALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSV 354
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 169-301 3.21e-06

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 48.86  E-value: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56314587  169 HCIGEAARLIQYGDVDVMVAGGAESTVTPLAVGGFASAKALstrnddpLTASRPwdkgrDGFVLGEGAGVLVLEEYEHAK 248
Cdd:PRK06147 138 VALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRL-------LTSQNS-----NGFIPGEAAAAVLLGRPAGGE 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 56314587  249 ARGARIYaeisGYGMSADAYHMTAPAE---DGDGAARCMANAMRDARMTVEEIDYV 301
Cdd:PRK06147 206 APGLPLL----GLGLGREPAPVGESEDlplRGDGLTQAIRAALAEAGCGLEDMDYR 257
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 163-236 8.86e-04

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 41.21  E-value: 8.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56314587 163 ACTTATHCIGEAARLIQYGDVDVMVAGGAES-TVTPLAVGGFASAKALSTRNDDPLTASRPWDKgRDGFVLGEGA 236
Cdd:COG0183  87 VCGSGLQAVALAAQAIAAGDADVVIAGGVESmSRAPMLLPKARWGYRMNAKLVDPMINPGLTDP-YTGLSMGETA 160
 
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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