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Conserved domains on  [gi|49244203|emb|CAG42629|]
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3-oxoacyl-[acyl-carrier-protein] synthase II [Staphylococcus aureus subsp. aureus MSSA476]

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 ...
 5-410 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: 741.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203     5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    85 EAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIES 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   244 LESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   324 GEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGGH 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400


                  ....*..
gi 49244203   404 NAVLVFK 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 ...
 5-410 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: 741.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203     5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    85 EAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIES 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   244 LESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   324 GEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGGH 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400


                  ....*..
gi 49244203   404 NAVLVFK 410
Cdd:TIGR03150 401 NASLVFK 407
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
4-413 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 704.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    4 NKRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAA 83
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   84 REAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVT 163
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  164 ACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGAGILVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  243 SLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNT 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  323 FGEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400

                        410
                 ....*....|.
gi 49244203  403 HNAVLVFKKFE 413
Cdd:PRK07314 401 TNASLVFKRYE 411
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: 688.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  85 EAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIES 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 244 LESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 324 GEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGGH 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400


                ....*....
gi 49244203 404 NAVLVFKKF 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 ...
 5-409 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: 637.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  85 EAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIES 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 244 LESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 324 GEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGGH 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400


                ....*.
gi 49244203 404 NAVLVF 409
Cdd:cd00834 401 NASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 5-247 2.66e-62

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: 201.32  E-value: 2.66e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203     5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKI--TRIDTEPY---SVHLAGELKN--------FNIEDH---IDKKE 68
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddiFDFDPLffgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    69 ARRMDRFTQYAIVAAREAVKDAQLDINENTADRIGVWIGSGIGGMETFEiahKQLMDKGPRRVSPFFVPMlIPDMATGQV 148
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALL---LLDEDGGPRRGSPFAVGT-MPSVIAGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   149 SIDLGAKGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTNDdietACRPFQEGRD 228
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDG----PCKAFDPFAD 232

                         250
                  ....*....|....*....
gi 49244203   229 GFVMGEGAGILVIESLESA 247
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 7-408 3.18e-19

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: 87.38  E-value: 3.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203      7 VVITGMGALSPIGNDVKTTWENALKGVNGIDKitridtepysvhlagelknFnieDH----IDKKEARRMD---RFtqyA 79
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVDL-------------------F---DAaffgISPREAEAMDpqqRL---L 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203     80 IVAAREAVKDAQLDINENTADRIGVWIGSGIGgmetfeiahkqlmdkgprrvspffvpmlipDMAtgqVSIDlgakgpng 159
Cdd:smart00825  56 LEVAWEALEDAGIDPESLRGSRTGVFVGVSSS------------------------------DYS---VTVD-------- 94

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    160 atvTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTNDdietACRPFQEGRDGFVMGEGAGIL 239
Cdd:smart00825  95 ---TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDG----RCKTFDASADGYVRGEGVGVV 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    240 VIESLESAQARGANIYAEIVGYGTT--GDAYHITAPAPEGeggsramqaamddagiepkdvqylnahgtstpvgdlnevk 317
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVNqdGRSNGITAPSGPA---------------------------------------- 207

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    318 aikntfgeaakHLKVSSTKSMTGHLLGATG--GIeaIFSALSIKDSKVAPTIHAVTPDPECDLD----IVPNEAQDLDIT 391
Cdd:smart00825 208 -----------QLLIGSVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPP 274

                          410       420
                   ....*....|....*....|.
gi 49244203    392 ----YAMSNSLGFGGHNAVLV 408
Cdd:smart00825 275 grprRAGVSSFGFGGTNAHVI 295
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 5-410 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: 741.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203     5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    85 EAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIES 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   244 LESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   324 GEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGGH 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400


                  ....*..
gi 49244203   404 NAVLVFK 410
Cdd:TIGR03150 401 NASLVFK 407
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
4-413 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 704.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    4 NKRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAA 83
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   84 REAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVT 163
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  164 ACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGAGILVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  243 SLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNT 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  323 FGEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400

                        410
                 ....*....|.
gi 49244203  403 HNAVLVFKKFE 413
Cdd:PRK07314 401 TNASLVFKRYE 411
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: 688.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  85 EAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIES 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 244 LESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 324 GEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGGH 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400


                ....*....
gi 49244203 404 NAVLVFKKF 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 ...
 5-409 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: 637.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  85 EAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIES 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 244 LESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 324 GEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGGH 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400


                ....*.
gi 49244203 404 NAVLVF 409
Cdd:cd00834 401 NASLVF 406
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
5-414 0e+00

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 561.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKN--------FNIEDHIDKKEARRMDRFT 76
Cdd:PRK06333   4 KRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMDRFI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   77 QYAIVAAREAVKDAQLDI-NENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAK 155
Cdd:PRK06333  84 LFAMAAAKEALAQAGWDPdTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGFK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  156 GPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST--NDDIETACRPFQEGRDGFVMG 233
Cdd:PRK06333 164 GPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTrfNDAPEQASRPFDRDRDGFVMG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  234 EGAGILVIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDL 313
Cdd:PRK06333 244 EGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  314 NEVKAIKNTFGEAAKhLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECD-LDIVPNEAQDLDITY 392
Cdd:PRK06333 324 GEVAAIKKVFGHVSG-LAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMDY 402

                        410       420
                 ....*....|....*....|..
gi 49244203  393 AMSNSLGFGGHNAVLVFKKFEA 414
Cdd:PRK06333 403 ALSNGFGFGGVNASILFRRWEP 424
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 5-412 7.50e-167

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 473.84  E-value: 7.50e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   85 EAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:PRK08439  82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIES 243
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  244 LESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEggSRAMQAAMDDAGiEPKdVQYLNAHGTSTPVGDLNEVKAIKNTF 323
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAPEGP--LRAMKAALEMAG-NPK-IDYINAHGTSTPYNDKNETAALKELF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  324 GEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGGH 403
Cdd:PRK08439 318 GSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGT 397


                 ....*....
gi 49244203  404 NAVLVFKKF 412
Cdd:PRK08439 398 NGVVIFKKV 406
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 14-412 1.11e-162

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 463.78  E-value: 1.11e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   14 ALSPIGNDVKTTWENALKGVNGIDKITRID-TEPYSVHLAGELKNFN------IEDHIDKKE--------ARRMDRFTQY 78
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPkFLPDCIPEQKALENLVaampcqIAAEVDQSEfdpsdfapTKRESRATHF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   79 AIVAAREAVKDAQLDINENT-ADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGP 157
Cdd:PTZ00050  81 AMAAAREALADAKLDILSEKdQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  158 NGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST--NDDIETACRPFQEGRDGFVMGEG 235
Cdd:PTZ00050 161 SGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkyNDDPQRASRPFDKDRAGFVMGEG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  236 AGILVIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAG-IEPKDVQYLNAHGTSTPVGDLN 314
Cdd:PTZ00050 241 AGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIGDKI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  315 EVKAIKNTFGE-AAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQ--DLDIT 391
Cdd:PTZ00050 321 ELKAIKKVFGDsGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAhpLQSID 400

                        410       420
                 ....*....|....*....|.
gi 49244203  392 YAMSNSLGFGGHNAVLVFKKF 412
Cdd:PTZ00050 401 AVLSTSFGFGGVNTALLFTKY 421
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
5-412 6.89e-157

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 449.07  E-value: 6.89e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:PRK08722   4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   85 EAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:PRK08722  84 QALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILVIES 243
Cdd:PRK08722 164 CTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLGDGAGMMVLEE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  244 LESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTF 323
Cdd:PRK08722 244 YEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRAL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  324 GEA-AKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLD-ITYAMSNSLGFG 401
Cdd:PRK08722 324 GEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNSFGFG 403

                        410
                 ....*....|.
gi 49244203  402 GHNAVLVFKKF 412
Cdd:PRK08722 404 GTNGSLIFKKM 414
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 5-409 3.13e-139

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 404.94  E-value: 3.13e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRID---------TEPYSV-----HLAGELKNFNIEDHIDKK--- 67
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDlkmksedeeTQLYTLdqlpsRVAALVPRGTGPGDFDEElwl 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   68 EARRMDRFTQYAIVAAREAVKDAQ-LDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATG 146
Cdd:PLN02836  86 NSRSSSRFIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAAG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  147 QVSIDLGAKGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST--NDDIETACRPFQ 224
Cdd:PLN02836 166 HVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfNSCPTEASRPFD 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  225 EGRDGFVMGEGAGILVIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAH 304
Cdd:PLN02836 246 CDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAH 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  305 GTSTPVGDLNEVKAIKNTFGE--AAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVP 382
Cdd:PLN02836 326 ATSTPLGDAVEARAIKTVFSEhaTSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVP 405

                        410       420
                 ....*....|....*....|....*...
gi 49244203  383 -NEAQDLDITYAMSNSLGFGGHNAVLVF 409
Cdd:PLN02836 406 lTASKAMLIRAALSNSFGFGGTNASLLF 433
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 5-412 2.05e-125

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 373.16  E-value: 2.05e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGK 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   85 EAVKDAQLD---INENTADRIGVWIGSGIGGMETFEIAHKQLMdKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGAT 161
Cdd:PLN02787 209 KALADGGITedvMKELDKTKCGVLIGSAMGGMKVFNDAIEALR-ISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSI 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  162 VTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILV 240
Cdd:PLN02787 288 STACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMGEGAGVLL 367

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  241 IESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIK 320
Cdd:PLN02787 368 LEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALM 447

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  321 NTFGEAAKhLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLD-IVPNEAQDLDITYAMSNSLG 399
Cdd:PLN02787 448 RCFGQNPE-LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKvLVGPKKERLDIKVALSNSFG 526

                        410
                 ....*....|...
gi 49244203  400 FGGHNAVLVFKKF 412
Cdd:PLN02787 527 FGGHNSSILFAPY 539
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
7-412 5.04e-111

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 332.08  E-value: 5.04e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    7 VVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYS--VHLAGELKNfNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFDlpVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLGR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   85 EAVKDAqlDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTA 164
Cdd:PRK07910  93 RVWENA--GSPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  165 CATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRA-LST-NDDIETACRPFQEGRDGFVMGEGAGILVIE 242
Cdd:PRK07910 171 CASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTnNDDPAGACRPFDKDRDGFVFGEGGALMVIE 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  243 SLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNT 322
Cdd:PRK07910 251 TEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  323 FGeaAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGG 402
Cdd:PRK07910 331 LG--GHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFGG 408

                        410
                 ....*....|
gi 49244203  403 HNAVLVFKKF 412
Cdd:PRK07910 409 HNVALAFGRY 418
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 72-412 5.09e-110

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 327.07  E-value: 5.09e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   72 MDRFTQYAIVAAREAVKDAQldiNENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSID 151
Cdd:PRK14691   1 MGRWWRYKWITFHPSLTHAD---NTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  152 LGAKGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST--NDDIETACRPFQEGRDG 229
Cdd:PRK14691  78 HHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfNSTPEKASRPFDTARDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  230 FVMGEGAGILVIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTP 309
Cdd:PRK14691 158 FVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  310 VGDLNEVKAIKNTFGEaAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECD-LDIVPNEAQDL 388
Cdd:PRK14691 238 VGDLGEINAIKHLFGE-SNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPH 316

                        330       340
                 ....*....|....*....|....
gi 49244203  389 DITYAMSNSLGFGGHNAVLVFKKF 412
Cdd:PRK14691 317 DMTYALSNGFGFAGVNASILLKRW 340
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
5-414 1.59e-104

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 315.07  E-value: 1.59e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKnFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   85 EAVKDAQLDINENTADRIGVWIGSGIGG----METFEIAHKqlmDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGA 160
Cdd:PRK07967  81 QAIADAGLSEEQVSNPRTGLIAGSGGGStrnqVEAADAMRG---PRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  161 TVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAgFSASRALST--NDDIETACRPFQEGRDGFVMGEGAGI 238
Cdd:PRK07967 158 ISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTkyNDTPEKASRAYDANRDGFVIAGGGGV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  239 LVIESLESAQARGANIYAEIVGYGTTGDAYHITAPApeGEGGSRAMQAAMddAGIEpKDVQYLNAHGTSTPVGDLNEVKA 318
Cdd:PRK07967 237 VVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPS--GEGAVRCMQMAL--ATVD-TPIDYINTHGTSTPVGDVKELGA 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  319 IKNTFGEAAKHlkVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPE-CDLDIVPNEAQDLDITYAMSNS 397
Cdd:PRK07967 312 IREVFGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNS 389

                        410
                 ....*....|....*..
gi 49244203  398 LGFGGHNAVLVFKKFEA 414
Cdd:PRK07967 390 FGFGGTNATLVFRRYKG 406
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
5-410 1.01e-93

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 287.27  E-value: 1.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEP-YSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAA 83
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDgLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   84 REAVKDAQLDINENTAD-RIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSP-FFVPMLiPDMATGQVSIDLGAKGPNGAT 161
Cdd:PRK09116  82 ELALEDAGLLGDPILTDgRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITAtTYVRMM-PHTTAVNVGLFFGLKGRVIPT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  162 VTACATGTNSIGEAFKIVQRGDADAMITGGTEApITHMAIAGFSASRALST-NDDIETACRPFQEGRDGFVMGEGAGILV 240
Cdd:PRK09116 161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTrNDAPELTPRPFDANRDGLVIGEGAGTLV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  241 IESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGgsRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIK 320
Cdd:PRK09116 240 LEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  321 NTFGEaakHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPEC-DLDIVPNEAQDLDITYAMSNSLG 399
Cdd:PRK09116 318 AVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYVMSNNFA 394

                        410
                 ....*....|.
gi 49244203  400 FGGHNAVLVFK 410
Cdd:PRK09116 395 FGGINTSLIFK 405
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
7-409 1.68e-91

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 282.29  E-value: 1.68e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    7 VVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELknfnieDHIDKKEARRMDRFTQYAIVAAREA 86
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------DFLPESPFGASALSEALARLAAEEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   87 VKDAQLDinentadrigvwiGSGIGG--------METFEIAHKQLMDKGPRRVSPFFVPML-------IPDMAT----GQ 147
Cdd:PRK06501  87 LAQAGIG-------------KGDFPGplflaappVELEWPARFALAAAVGDNDAPSYDRLLraarggrFDALHErfqfGS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  148 VSIDL----GAKGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALST-NDDIETACRP 222
Cdd:PRK06501 154 IADRLadrfGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTqNDPPEKASKP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  223 FQEGRDGFVMGEGAGILVIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLN 302
Cdd:PRK06501 234 FSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYIN 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  303 AHGTSTPVGDLNEVKAIKNTFGEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVP 382
Cdd:PRK06501 314 AHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVP 393

                        410       420
                 ....*....|....*....|....*..
gi 49244203  383 NEAQDLDITYAMSNSLGFGGHNAVLVF 409
Cdd:PRK06501 394 NVARDARVTAVLSNSFGFGGQNASLVL 420
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 6-408 1.30e-86

"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: 269.31  E-value: 1.30e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   6 RVVITGMGALSPIGNDVKTT---WENALKGVNGIDKITRIdTEPYSVHLAGELKNFNIEDHIDKKEaRRMDRFTQYAIVA 82
Cdd:cd00828   2 RVVITGIGVVSPHGEGCDEVeefWEALREGRSGIAPVARL-KSRFDRGVAGQIPTGDIPGWDAKRT-GIVDRTTLLALVA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  83 AREAVKDAQL-DINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFvpMLIPDMATGQVSIDL-GAKGPNGA 160
Cdd:cd00828  80 TEEALADAGItDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKW--MLSPNTVAGWVNILLlSSHGPIKT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 161 TVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIaGFSASRALSTNDDI-ETACRPFQEGRDGFVMGEGAGIL 239
Cdd:cd00828 158 PVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLS-GFANMGALSTAEEEpEEMSRPFDETRDGFVEAEGAGVL 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 240 VIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPeGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAI 319
Cdd:cd00828 237 VLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAI 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 320 KNTFGEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDL--DITYAMSNS 397
Cdd:cd00828 316 AEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLnlKVRAALVNA 395

                       410
                ....*....|.
gi 49244203 398 LGFGGHNAVLV 408
Cdd:cd00828 396 FGFGGSNAALV 406
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 5-408 1.57e-83

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: 261.14  E-value: 1.57e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAR 84
Cdd:cd00832   1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  85 EAVKDAQLDINENTADRIGVWIGSGIGGmetFEIAHKQ---LMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGAT 161
Cdd:cd00832  81 WALADAGVDPAALPPYDMGVVTASAAGG---FEFGQRElqkLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 162 VTACATGTNSIGEAFKIVQRGdADAMITGGTEAPITHMAIAGFSASRALSTNDDIETACRPFQEGRDGFVMGEGAGILVI 241
Cdd:cd00832 158 VAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEGGAILVL 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 242 ESLESAQARGANIYAEIVGYGTTGDAyhitAPAP-EGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIK 320
Cdd:cd00832 237 EDAAAARERGARVYGEIAGYAATFDP----PPGSgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALA 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 321 NTFGeaAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGF 400
Cdd:cd00832 313 AVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGR 390


                ....*...
gi 49244203 401 GGHNAVLV 408
Cdd:cd00832 391 GGFNSALV 398
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 5-411 2.96e-82

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 258.04  E-value: 2.96e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITR--------IDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFT 76
Cdd:PRK07103   2 DEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRpgrqvpddAGAGLASAFIGAELDSLALPERLDAKLLRRASLSA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   77 QYAIVAAREAVKDAQLDinENTADRIGVWI-GSGIGGMETFEIaHKQLMDKgPRRVSPFFVPMLIPDMATGQVSIDLGAK 155
Cdd:PRK07103  82 QAALAAAREAWRDAALG--PVDPDRIGLVVgGSNLQQREQALV-HETYRDR-PAFLRPSYGLSFMDTDLVGLCSEQFGIR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  156 GPnGATV-TACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTN---DDIETACRPFQEGRDGFV 231
Cdd:PRK07103 158 GE-GFTVgGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDrfaDEPEAACRPFDQDRDGFI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  232 MGEGAGILVIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEggSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVG 311
Cdd:PRK07103 237 YGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGSPLG 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  312 DLNEVKAIkntFGEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTP-DPECDLdiVPNEAQDLDI 390
Cdd:PRK07103 315 DETELAAL---FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERFRW--VGSTAESARI 389

                        410       420
                 ....*....|....*....|.
gi 49244203  391 TYAMSNSLGFGGHNAVLVFKK 411
Cdd:PRK07103 390 RYALSLSFGFGGINTALVLER 410
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
6-411 7.17e-82

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 256.13  E-value: 7.17e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    6 RVVITGMGALSPIGnDVKTTWENALKGVNGID-KITRIDTEPYSVHLAGelknfniedhidkKEARRMDRFTQYAIVAar 84
Cdd:PRK05952   3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKlHQPFPELPPLPLGLIG-------------NQPSSLEDLTKTVVTA-- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   85 eAVKDAQLDINENTAdriGVWIGSGIGGMETFE-IAHKQLMDKGPRRVSPFFVPML--IPDMATGQVSIDLGAKGPNGAT 161
Cdd:PRK05952  67 -ALKDAGLTPPLTDC---GVVIGSSRGCQGQWEkLARQMYQGDDSPDEELDLENWLdtLPHQAAIAAARQIGTQGPVLAP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  162 VTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTnddieTACRPFQEGRDGFVMGEGAGILVI 241
Cdd:PRK05952 143 MAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK-----TGAYPFDRQREGLVLGEGGAILVL 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  242 ESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKN 321
Cdd:PRK05952 218 ESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQA 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  322 TFGEAakhLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTpdPECDLDIVpNEAQDLDITYAMSNSLGFG 401
Cdd:PRK05952 298 LFPHR---VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNFV-RQAQQSPLQNVLCLSFGFG 371

                        410
                 ....*....|
gi 49244203  402 GHNAVLVFKK 411
Cdd:PRK05952 372 GQNAAIALGK 381
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 6-408 3.45e-70

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 227.06  E-value: 3.45e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   6 RVVITGMGALSPIGNDVKTTWENALKGVNGIDKIT--RIDTEPYS----------VHLAGELKNFNIEDH----IDKKEA 69
Cdd:cd00833   2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedRWDADGYYpdpgkpgktyTRRGGFLDDVDAFDAaffgISPREA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  70 RRMDRFTQYAIVAAREAVKDAQLDINENTADRIGVWIGSGigGMETFEIAHKQlmdkgPRRVSPFFVPMLIPDMATGQVS 149
Cdd:cd00833  82 EAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGAS--SSDYLELLARD-----PDEIDAYAATGTSRAFLANRIS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 150 IDLGAKGPNgATV-TACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTNDdietACRPFQEGRD 228
Cdd:cd00833 155 YFFDLRGPS-LTVdTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDG----RCRPFDADAD 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 229 GFVMGEGAGILVIESLESAQARGANIYAEIVGYGTTGDAY--HITAPAPEGEggSRAMQAAMDDAGIEPKDVQYLNAHGT 306
Cdd:cd00833 230 GYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEAQ--AALIRRAYARAGVDPSDIDYVEAHGT 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 307 STPVGDLNEVKAIKNTFGE---AAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLD---- 379
Cdd:cd00833 308 GTPLGDPIEVEALAKVFGGsrsADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEespl 387

                       410       420       430
                ....*....|....*....|....*....|...
gi 49244203 380 IVPNEAQDLDIT----YAMSNSLGFGGHNAVLV 408
Cdd:cd00833 388 RVPTEARPWPAPagprRAGVSSFGFGGTNAHVI 420
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
7-409 4.81e-68

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 220.87  E-value: 4.81e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    7 VVITGMGALSPIGNDVKTTWENALKGVNG---------------IDKITRIDTEPysvhLAGELKNFNIedhidkkearR 71
Cdd:PRK09185   4 VYISAFGATSALGRGLDAILAALRAGRASgmrpcdfwlvdlptwVGEVVGVELPA----LPAALAAFDC----------R 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   72 MDRFTQYAIVAAREAVKDAqldINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSID 151
Cdd:PRK09185  70 NNRLALLALQQIEPAVEAA---IARYGADRIGVVLGTSTSGILEGELAYRRRDPAHGALPADYHYAQQELGSLADFLRAY 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  152 LGAKGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEApITHMAIAGFSASRALStnddiETACRPFQEGRDGFV 231
Cdd:PRK09185 147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLS-----PQPCRPFSANRDGIN 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  232 MGEGAGILVIESLESAQARganiyaeIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVG 311
Cdd:PRK09185 221 IGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLN 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  312 DLNEVKAIKNTFGEaakHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDIT 391
Cdd:PRK09185 294 DAMESRAVAAVFGD---GVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIR 370

                        410
                 ....*....|....*...
gi 49244203  392 YAMSNSLGFGGHNAVLVF 409
Cdd:PRK09185 371 YVLSNSFAFGGNNCSLIF 388
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 5-247 2.66e-62

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: 201.32  E-value: 2.66e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203     5 KRVVITGMGALSPIGNDVKTTWENALKGVNGIDKI--TRIDTEPY---SVHLAGELKN--------FNIEDH---IDKKE 68
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddiFDFDPLffgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    69 ARRMDRFTQYAIVAAREAVKDAQLDINENTADRIGVWIGSGIGGMETFEiahKQLMDKGPRRVSPFFVPMlIPDMATGQV 148
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALL---LLDEDGGPRRGSPFAVGT-MPSVIAGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   149 SIDLGAKGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTNDdietACRPFQEGRD 228
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDG----PCKAFDPFAD 232

                         250
                  ....*....|....*....
gi 49244203   229 GFVMGEGAGILVIESLESA 247
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 74-408 1.22e-58

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: 194.39  E-value: 1.22e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  74 RFTQYAIVAAREAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMlipdmATGQVSIDLG 153
Cdd:cd00825  10 YVSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG-----ASGQIATPLG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 154 AKGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTnddiETACRPFQEGRDGFVMG 233
Cdd:cd00825  85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTP----EKASRTFDAAADGFVFG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 234 EGAGILVIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDL 313
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 314 NEVKAIKNTFGEaaKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPecDLDIVPNEAQDLDITYA 393
Cdd:cd00825 241 KELKLLRSEFGD--KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTA 316

                       330
                ....*....|....*
gi 49244203 394 MSNSLGFGGHNAVLV 408
Cdd:cd00825 317 LLNGFGLGGTNATLV 331
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 3-408 5.80e-50

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 181.61  E-value: 5.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    3 QNKRVVITGMGALSPIGNDVKTTWENALKGVNGIDKIT--RIDTEPYS-----------VHLAGELknfnieDHIDK--- 66
Cdd:COG3321    2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPadRWDADAYYdpdpdapgktyVRWGGFL------DDVDEfda 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   67 -------KEARRMD---RFtqyAIVAAREAVKDAQLDINENTADRIGVWIGSGIGGmetfeiaHKQLMDKGPRRVSPFFV 136
Cdd:COG3321   76 lffgispREAEAMDpqqRL---LLEVAWEALEDAGYDPESLAGSRTGVFVGASSND-------YALLLLADPEAIDAYAL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  137 PMLIPDMATGQVSIDLGAKGPNgATV-TACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTNDD 215
Cdd:COG3321  146 TGNAKSVLAGRISYKLDLRGPS-VTVdTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGR 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  216 ietaCRPFQEGRDGFVMGEGAGILVIESLESAQARGANIYAEIVGYG------TTGdayhITAPAPEGEggSRAMQAAMD 289
Cdd:COG3321  225 ----CRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAvnqdgrSNG----LTAPNGPAQ--AAVIRRALA 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  290 DAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTFGE---AAKHLKVSSTKSMTGHLLGATG--GIeaIFSALSIKDSKVA 364
Cdd:COG3321  295 DAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQgrpADQPCAIGSVKSNIGHLEAAAGvaGL--IKAVLALRHGVLP 372

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 49244203  365 PTIHAVTPDPECDLD----IVPNEAQDLDIT----YAMSNSLGFGGHNAVLV 408
Cdd:COG3321  373 PTLHFETPNPHIDFEnspfYVNTELRPWPAGggprRAGVSSFGFGGTNAHVV 424
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 255-368 1.63e-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: 155.80  E-value: 1.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203   255 YAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTFGEAA--KHLKV 332
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkQPLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 49244203   333 SSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIH 368
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLN 116
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 151-412 4.42e-34

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: 135.13  E-value: 4.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    151 DLGakGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGT---EAPITHMAiagFSASRALSTNDDIetacRPFQEGR 227
Cdd:TIGR02813  194 DLG--GMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVctdNSPFMYMS---FSKTPAFTTNEDI----QPFDIDS 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    228 DGFVMGEGAGILVIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTS 307
Cdd:TIGR02813  265 KGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTG 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    308 TPVGDLNEVKAIKNTFGE---AAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVP-- 382
Cdd:TIGR02813  345 TAAGDVAEFGGLVSVFSQdndQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPfy 424

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 49244203    383 --NEA----QDLDIT--YAMSNSLGFGGHNAVLVFKKF 412
Cdd:TIGR02813  425 lnTETrpwmQREDGTprRAGISSFGFGGTNFHMVLEEY 462
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 144-408 4.56e-29

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: 113.69  E-value: 4.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 144 ATGQVSIDLG-AKGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEApithmaiagfsasralstnddietacrp 222
Cdd:cd00327  46 AAGQLAYHLGiSGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 223 fqegrdgFVMGEGAGILVIESLESAQARGANIYAEIVGYGTTGD-AYHITAPApeGEGGSRAMQAAMDDAGIEPKDVQYL 301
Cdd:cd00327  98 -------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVS--GEGLARAARKALEGAGLTPSDIDYV 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203 302 NAHGTSTPVGDLNEVKAIKNTFGEaaKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTihavtpdpecdldiv 381
Cdd:cd00327 169 EAHGTGTPIGDAVELALGLDPDGV--RSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT--------------- 231

                       250       260
                ....*....|....*....|....*..
gi 49244203 382 PNEAQdlditYAMSNSLGFGGHNAVLV 408
Cdd:cd00327 232 PREPR-----TVLLLGFGLGGTNAAVV 253
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 7-408 3.18e-19

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: 87.38  E-value: 3.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203      7 VVITGMGALSPIGNDVKTTWENALKGVNGIDKitridtepysvhlagelknFnieDH----IDKKEARRMD---RFtqyA 79
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVDL-------------------F---DAaffgISPREAEAMDpqqRL---L 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203     80 IVAAREAVKDAQLDINENTADRIGVWIGSGIGgmetfeiahkqlmdkgprrvspffvpmlipDMAtgqVSIDlgakgpng 159
Cdd:smart00825  56 LEVAWEALEDAGIDPESLRGSRTGVFVGVSSS------------------------------DYS---VTVD-------- 94

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    160 atvTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTNDdietACRPFQEGRDGFVMGEGAGIL 239
Cdd:smart00825  95 ---TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDG----RCKTFDASADGYVRGEGVGVV 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    240 VIESLESAQARGANIYAEIVGYGTT--GDAYHITAPAPEGeggsramqaamddagiepkdvqylnahgtstpvgdlnevk 317
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVNqdGRSNGITAPSGPA---------------------------------------- 207

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203    318 aikntfgeaakHLKVSSTKSMTGHLLGATG--GIeaIFSALSIKDSKVAPTIHAVTPDPECDLD----IVPNEAQDLDIT 391
Cdd:smart00825 208 -----------QLLIGSVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPP 274

                          410       420
                   ....*....|....*....|.
gi 49244203    392 ----YAMSNSLGFGGHNAVLV 408
Cdd:smart00825 275 grprRAGVSSFGFGGTNAHVI 295
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 171-314 2.70e-05

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 45.78  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  171 SIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTNDDietacrpfqegRDGFVMGEGAGILVIESLESAQAR 250
Cdd:PRK06147 139 ALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQN-----------SNGFIPGEAAAAVLLGRPAGGEAP 207

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49244203  251 GANIYAeiVGYGTTGDAYHITAPAP-EGEGGSRAMQAAMDDAGIEPKDVQYLnahgtstpVGDLN 314
Cdd:PRK06147 208 GLPLLG--LGLGREPAPVGESEDLPlRGDGLTQAIRAALAEAGCGLEDMDYR--------IADLN 262
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
225-385 5.54e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 44.94  E-value: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  225 EGRDGFVMGEGAGILVIESLESAQARGANIYAEIVGYGT----------TGDAYHITAPAPEGEGGSRAMQAAmddAGIE 294
Cdd:PRK06519 234 EDGGGFILGSGGAFLVLESREHAEARGARPYARISGVESdrarrapgdlEASLERLLKPAGGLAAPTAVISGA---TGAH 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  295 PkdvqylnahgtstpvgdlneVKAIKNTFGEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPtihAVTPDP 374
Cdd:PRK06519 311 P--------------------ATAEEKAALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFP---PFDASG 367

                        170
                 ....*....|.
gi 49244203  375 ECDLDIVPNEA 385
Cdd:PRK06519 368 EKPMSGAAREA 378
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 235-298 2.58e-03

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: 39.66  E-value: 2.58e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49244203 235 GAGILVIESLESAQARGANIYAEIVGYGTTGDAYHI--TAPAPegeggsrAMQAAMDDAGIEPKDV 298
Cdd:COG0183 251 GAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEImgIGPVP-------ATRKALARAGLTLDDI 309
PRK05790 PRK05790
putative acyltransferase; Provisional
 235-298 6.99e-03

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 38.21  E-value: 6.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49244203  235 GAGILVIESLESAQARGANIYAEIVGYGTTGdayhiTAPAPEGEGGSRAMQAAMDDAGIEPKDV 298
Cdd:PRK05790 253 GAAAVVVMSEAKAKELGLTPLARIVSYAVAG-----VDPAIMGIGPVPAIRKALEKAGWSLADL 311
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
 232-363 8.73e-03

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 38.15  E-value: 8.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49244203  232 MGEGAGILVIESLESAQARGANIYAEIVGYgttGDAyhitAPAPE--GEGGSRAMQAAMDDAGIEPKDVQYLnahgtstp 309
Cdd:PLN02644 250 ISDGAAALVLVSGEKALELGLQVIAKIRGY---ADA----AQAPElfTTAPALAIPKALKHAGLEASQVDYY-------- 314

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49244203  310 vgDLNE---VKAIKNT--FGEAAKHLKVSSTKSMTGHLLGATGG--IEAIFSALSIKDSKV 363
Cdd:PLN02644 315 --EINEafsVVALANQklLGLDPEKVNVHGGAVSLGHPIGCSGAriLVTLLGVLRSKNGKY 373
 
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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