NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|721831997|gb|KGZ91787|]
View 

3-oxoacyl-ACP synthase [Bacillus anthracis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
4-409 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: 728.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997    4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   84 MAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  164 CASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILEE 242
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALsTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  243 LEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETF 322
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  323 GEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGH 402
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400

                  ....*..
gi 721831997  403 NAVLVFK 409
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 ...
4-409 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: 728.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997    4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   84 MAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  164 CASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILEE 242
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALsTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  243 LEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETF 322
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  323 GEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGH 402
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400

                  ....*..
gi 721831997  403 NAVLVFK 409
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: 718.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   3 KKRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAA 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  83 KMAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 163 ACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILE 241
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALsTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 242 ELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKET 321
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 322 FGEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGG 401
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
                        410
                 ....*....|.
gi 721831997 402 HNAVLVFKSYK 412
Cdd:PRK07314 401 TNASLVFKRYE 411
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4-411 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: 691.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  84 MAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:COG0304   81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 164 CASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILEE 242
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALsTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 243 LEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETF 322
Cdd:COG0304  241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 323 GEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGH 402
Cdd:COG0304  321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400

                 ....*....
gi 721831997 403 NAVLVFKSY 411
Cdd:COG0304  401 NASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4-408 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: 638.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  84 MAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:cd00834   81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 164 CASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILEE 242
Cdd:cd00834  161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALsTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 243 LEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETF 322
Cdd:cd00834  241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 323 GEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGH 402
Cdd:cd00834  321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400

                 ....*.
gi 721831997 403 NAVLVF 408
Cdd:cd00834  401 NASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4-246 3.35e-55

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: 182.83  E-value: 3.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997    4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRL--TRIDPELF---PAKVAAEI--------NDFEVEKY---IDKKE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIytkwggldDIFDFDPLffgISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   68 ARRMDRFTQYAVAAAKMAVADAKLEITEENGPRIGVWIGSGIGGmetYEEQFKIFTEKGPRRVSPFFVPMMiPDMAAGQV 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGD---YAALLLLDEDGGPRRGSPFAVGTM-PSVIAGRI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  148 SIATGAKGINTCSVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALTFNEdpatACRPFDKNRS 227
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDG----PCKAFDPFAD 232
                         250
                  ....*....|....*....
gi 721831997  228 GFVMGEGSGILILEELEHA 246
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
162-407 2.84e-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: 104.33  E-value: 2.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   162 TACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALTfnedPATACRPFDKNRSGFVMGEGSGILILE 241
Cdd:smart00825  95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS----PDGRCKTFDASADGYVRGEGVGVVVLK 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   242 ELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGgvramrQaladaglqpedidyinahgtstdanekyetmaiket 321
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPA------Q------------------------------------ 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   322 fgehaykVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLD----YVPNNARHQEVN------A 391
Cdd:smart00825 209 -------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPgrprraG 281
                          250
                   ....*....|....*.
gi 721831997   392 VlsNSLGFGGHNAVLV 407
Cdd:smart00825 282 V--SSFGFGGTNAHVI 295
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
4-409 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: 728.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997    4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   84 MAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  164 CASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILEE 242
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALsTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  243 LEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETF 322
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  323 GEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGH 402
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400

                  ....*..
gi 721831997  403 NAVLVFK 409
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: 718.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   3 KKRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAA 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  83 KMAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 163 ACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILE 241
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALsTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 242 ELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKET 321
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 322 FGEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGG 401
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
                        410
                 ....*....|.
gi 721831997 402 HNAVLVFKSYK 412
Cdd:PRK07314 401 TNASLVFKRYE 411
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4-411 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: 691.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  84 MAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:COG0304   81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 164 CASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILEE 242
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALsTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 243 LEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETF 322
Cdd:COG0304  241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 323 GEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGH 402
Cdd:COG0304  321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400

                 ....*....
gi 721831997 403 NAVLVFKSY 411
Cdd:COG0304  401 NASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4-408 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: 638.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  84 MAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:cd00834   81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 164 CASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILEE 242
Cdd:cd00834  161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALsTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 243 LEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETF 322
Cdd:cd00834  241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 323 GEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGH 402
Cdd:cd00834  321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400

                 ....*.
gi 721831997 403 NAVLVF 408
Cdd:cd00834  401 NASLVF 406
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-412 0e+00

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 515.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   1 MEKKRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEIND--------FEVEKYIDKKEARRMD 72
Cdd:PRK06333   1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  73 RFTQYAVAAAKMAVADAKLEITEENGP-RIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIAT 151
Cdd:PRK06333  81 RFILFAMAAAKEALAQAGWDPDTLEDReRTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 152 GAKGINTCSVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALT--FNEDPATACRPFDKNRSGF 229
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALStrFNDAPEQASRPFDRDRDGF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 230 VMGEGSGILILEELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDA 309
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 310 NEKYETMAIKETFGeHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECD-LDYVPNNARHQE 388
Cdd:PRK06333 321 GDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
                        410       420
                 ....*....|....*....|....
gi 721831997 389 VNAVLSNSLGFGGHNAVLVFKSYK 412
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRRWE 423
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
4-411 2.97e-171

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 485.01  E-value: 2.97e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  84 MAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:PRK08439  82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 164 CASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILILEE 242
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALsTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 243 LEHALARGAHIYAEIAGYGATGDAFHITMPAPggEGGVRAMRQALADAGLQPedIDYINAHGTSTDANEKYETMAIKETF 322
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKELF 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 323 GEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGH 402
Cdd:PRK08439 318 GSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGT 397

                 ....*....
gi 721831997 403 NAVLVFKSY 411
Cdd:PRK08439 398 NGVVIFKKV 406
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
13-411 9.52e-166

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 471.48  E-value: 9.52e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  13 AVTPVGTDVETAWENIKKGVSGIGRLTRID----------------PELFPAKVAAEInDFEVEKYIDKKEARRMDRFTQ 76
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPkflpdcipeqkalenlVAAMPCQIAAEV-DQSEFDPSDFAPTKRESRATH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  77 YAVAAAKMAVADAKLEITEENGP-RIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKG 155
Cdd:PTZ00050  80 FAMAAAREALADAKLDILSEKDQeRIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 156 INTCSVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALT--FNEDPATACRPFDKNRSGFVMGE 233
Cdd:PTZ00050 160 PSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkYNDDPQRASRPFDKDRAGFVMGE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 234 GSGILILEELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQP-EDIDYINAHGTSTDANEK 312
Cdd:PTZ00050 240 GAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINiNDVDYVNAHATSTPIGDK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 313 YETMAIKETFGEH-AYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARH--QEV 389
Cdd:PTZ00050 320 IELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHplQSI 399
                        410       420
                 ....*....|....*....|..
gi 721831997 390 NAVLSNSLGFGGHNAVLVFKSY 411
Cdd:PTZ00050 400 DAVLSTSFGFGGVNTALLFTKY 421
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
1-409 1.61e-148

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 427.50  E-value: 1.61e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   1 MEKKRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVA 80
Cdd:PRK08722   1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  81 AAKMAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCS 160
Cdd:PRK08722  81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 161 VTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGEGSGILI 239
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALsTRNDEPQKASRPWDKDRDGFVLGDGAGMMV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 240 LEELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIK 319
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 320 ETFGEH-AYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQE-VNAVLSNSL 397
Cdd:PRK08722 321 RALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNSF 400
                        410
                 ....*....|..
gi 721831997 398 GFGGHNAVLVFK 409
Cdd:PRK08722 401 GFGGTNGSLIFK 412
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
4-410 2.94e-146

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 422.66  E-value: 2.94e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPEL--------------FPAKVAAEI------NDFEVEKYI 63
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKMksedeetqlytldqLPSRVAALVprgtgpGDFDEELWL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  64 dkkEARRMDRFTQYAVAAAKMAVADAKLEITE-ENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDM 142
Cdd:PLN02836  86 ---NSRSSSRFIGYALCAADEALSDARWLPSEdEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 143 AAGQVSIATGAKGINTCSVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALT--FNEDPATACR 220
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStkFNSCPTEASR 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 221 PFDKNRSGFVMGEGSGILILEELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYI 300
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYV 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 301 NAHGTSTDANEKYETMAIKETFGEHAY--KVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLD 378
Cdd:PLN02836 323 NAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDG 402
                        410       420       430
                 ....*....|....*....|....*....|...
gi 721831997 379 YVP-NNARHQEVNAVLSNSLGFGGHNAVLVFKS 410
Cdd:PLN02836 403 FVPlTASKAMLIRAALSNSFGFGGTNASLLFTS 435
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
1-412 9.05e-115

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 345.81  E-value: 9.05e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   1 MEKKRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVA 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  81 AAKMAVADAKleITEE-----NGPRIGVWIGSGIGGMETYEEQFKIFtEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKG 155
Cdd:PLN02787 206 AGKKALADGG--ITEDvmkelDKTKCGVLIGSAMGGMKVFNDAIEAL-RISYRKMNPFCVPFATTNMGSAMLAMDLGWMG 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 156 INTCSVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALT-FNEDPATACRPFDKNRSGFVMGEG 234
Cdd:PLN02787 283 PNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSqRNDDPTKASRPWDMNRDGFVMGEG 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 235 SGILILEELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYE 314
Cdd:PLN02787 363 AGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKE 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 315 TMAIKETFGEHAyKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLD-YVPNNARHQEVNAVL 393
Cdd:PLN02787 443 YQALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKvLVGPKKERLDIKVAL 521
                        410
                 ....*....|....*....
gi 721831997 394 SNSLGFGGHNAVLVFKSYK 412
Cdd:PLN02787 522 SNSFGFGGHNSSILFAPYK 540
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
6-411 3.03e-107

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 322.45  E-value: 3.03e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   6 VVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELF--PAKVAAEINDfEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFdlPVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLGR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  84 MAVADAKLEITEENgpRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:PRK07910  93 RVWENAGSPEVDTN--RLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 164 CASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL--TFNEDPATACRPFDKNRSGFVMGEGSGILILE 241
Cdd:PRK07910 171 CASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVmsTNNDDPAGACRPFDKDRDGFVFGEGGALMVIE 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 242 ELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKET 321
Cdd:PRK07910 251 TEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNA 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 322 FGEHayKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGG 401
Cdd:PRK07910 331 LGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFGG 408
                        410
                 ....*....|
gi 721831997 402 HNAVLVFKSY 411
Cdd:PRK07910 409 HNVALAFGRY 418
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
6-412 1.76e-106

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 320.81  E-value: 1.76e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   6 VVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTqyavaaAKMA 85
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPESPFGASALSEALARLA------AEEA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  86 VADAKLEITEENGP--------------RIGVWIGSGIGGMETYEEQFKIfteKGPRRVSPFFVPMMIPDMAAgQVSIAT 151
Cdd:PRK06501  87 LAQAGIGKGDFPGPlflaappvelewpaRFALAAAVGDNDAPSYDRLLRA---ARGGRFDALHERFQFGSIAD-RLADRF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 152 GAKGINTCSVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFV 230
Cdd:PRK06501 163 GTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALsTQNDPPEKASKPFSKDRDGFV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 231 MGEGSGILILEELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDAN 310
Cdd:PRK06501 243 MAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPEN 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 311 EKYETMAIKETFGEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVN 390
Cdd:PRK06501 323 DKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARVT 402
                        410       420
                 ....*....|....*....|..
gi 721831997 391 AVLSNSLGFGGHNAVLVFKSYK 412
Cdd:PRK06501 403 AVLSNSFGFGGQNASLVLTAEP 424
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
4-412 1.23e-105

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 317.77  E-value: 1.23e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIgrltRIDPEL----FPAKVAAEInDFEVEKYIDKKEARRMDRFTQYAV 79
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGI----TFSPEFaemgMRSQVWGNV-KLDPTGLIDRKVMRFMGDASAYAY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  80 AAAKMAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIF-TEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINT 158
Cdd:PRK07967  77 LAMEQAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMrGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 159 CSVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAgFSSAKALT--FNEDPATACRPFDKNRSGFVMGEGSG 236
Cdd:PRK07967 157 SISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALStkYNDTPEKASRAYDANRDGFVIAGGGG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 237 ILILEELEHALARGAHIYAEIAGYGATGDAFhiTMPAPGGEGGVRAMRQALADAGlqpEDIDYINAHGTSTDANEKYETM 316
Cdd:PRK07967 236 VVVVEELEHALARGAKIYAEIVGYGATSDGY--DMVAPSGEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVKELG 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 317 AIKETFGEHAykVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPE-CDLDYVPNNARHQEVNAVLSN 395
Cdd:PRK07967 311 AIREVFGDKS--PAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSN 388
                        410
                 ....*....|....*..
gi 721831997 396 SLGFGGHNAVLVFKSYK 412
Cdd:PRK07967 389 SFGFGGTNATLVFRRYK 405
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
4-409 8.86e-104

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 313.08  E-value: 8.86e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRID--PELfPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAA 81
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDryDGL-NTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  82 AKMAVADAKL----EITeeNGpRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSP-FFVPMMiPDMAAGQVSIATGAKG- 155
Cdd:PRK09116  81 SELALEDAGLlgdpILT--DG-RMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITAtTYVRMM-PHTTAVNVGLFFGLKGr 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 156 -INTCSvtACASGANSIGDAFKAIQRGDADAMITGGAEApLTSMAFAGFSSAKAL-TFNEDPATACRPFDKNRSGFVMGE 233
Cdd:PRK09116 157 vIPTSS--ACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATsTRNDAPELTPRPFDANRDGLVIGE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 234 GSGILILEELEHALARGAHIYAEIAGYGATGDAFHITMPAPggEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKY 313
Cdd:PRK09116 234 GAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQA--ETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIA 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 314 ETMAIKETFGEhayKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPEC-DLDYVPNNARHQEVNAV 392
Cdd:PRK09116 312 ESQATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYV 388
                        410
                 ....*....|....*..
gi 721831997 393 LSNSLGFGGHNAVLVFK 409
Cdd:PRK09116 389 MSNNFAFGGINTSLIFK 405
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
96-411 1.49e-99

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 300.11  E-value: 1.49e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  96 ENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTACASGANSIGDAF 175
Cdd:PRK14691  23 EKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 176 KAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALT--FNEDPATACRPFDKNRSGFVMGEGSGILILEELEHALARGAHI 253
Cdd:PRK14691 103 RMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSthFNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 254 YAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETFGEhAYKVAISS 333
Cdd:PRK14691 183 LAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITS 261
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 721831997 334 TKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECD-LDYVPNNARHQEVNAVLSNSLGFGGHNAVLVFKSY 411
Cdd:PRK14691 262 TKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKRW 340
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
5-407 3.12e-84

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 262.30  E-value: 3.12e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   5 RVVITGLGAVTPVGtDVETAWENIKKGVSGIgRLTRIDPELfPAKVAAEINDFEVEkyidkkearrmdrFTQYAVAAAKM 84
Cdd:PRK05952   3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGI-KLHQPFPEL-PPLPLGLIGNQPSS-------------LEDLTKTVVTA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  85 AVADAKLEITEengPRIGVWIGSGIGGMETYEEQFK-IFTEKGPRRVSPFFVPMM--IPDMAAGQVSIATGAKGINTCSV 161
Cdd:PRK05952  67 ALKDAGLTPPL---TDCGVVIGSSRGCQGQWEKLARqMYQGDDSPDEELDLENWLdtLPHQAAIAAARQIGTQGPVLAPM 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 162 TACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALTfnedpATACRPFDKNRSGFVMGEGSGILILE 241
Cdd:PRK05952 144 AACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAYPFDRQREGLVLGEGGAILVLE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 242 ELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKET 321
Cdd:PRK05952 219 SAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQAL 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 322 FGEhayKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETpdPECDLDYVpNNARHQEVNAVLSNSLGFGG 401
Cdd:PRK05952 299 FPH---RVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNFV-RQAQQSPLQNVLCLSFGFGG 372

                 ....*.
gi 721831997 402 HNAVLV 407
Cdd:PRK05952 373 QNAAIA 378
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
4-407 6.11e-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: 259.60  E-value: 6.11e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELFPAKVAAEINDFEVEKYIDKKEARRMDRFTQYAVAAAK 83
Cdd:cd00832    1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  84 MAVADAKLEITEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTA 163
Cdd:cd00832   81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 164 CASGANSIGDAFKAIQRGdADAMITGGAEAPLTSMAFAGFSSAKALTFNEDPATACRPFDKNRSGFVMGEGSGILILEEL 243
Cdd:cd00832  161 QAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEGGAILVLEDA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 244 EHALARGAHIYAEIAGYGATGDAfhitMPAPGGEGG-VRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETF 322
Cdd:cd00832  240 AAARERGARVYGEIAGYAATFDP----PPGSGRPPGlARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVF 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 323 GEHAykVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGH 402
Cdd:cd00832  316 GPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGGF 393

                 ....*
gi 721831997 403 NAVLV 407
Cdd:cd00832  394 NSALV 398
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
5-407 6.35e-83

"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: 259.68  E-value: 6.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   5 RVVITGLGAVTPVGT---DVETAWENIKKGVSGIGRLTRIDPElFPAKVAAEINDFEVEKYIDKKEaRRMDRFTQYAVAA 81
Cdd:cd00828    2 RVVITGIGVVSPHGEgcdEVEEFWEALREGRSGIAPVARLKSR-FDRGVAGQIPTGDIPGWDAKRT-GIVDRTTLLALVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  82 AKMAVADAKLEI-TEENGPRIGVWIGSGIGGMETYEEQFKIFTEKGPRRVSPFFvpMMIPDMAAGQVSIA-TGAKGINTC 159
Cdd:cd00828   80 TEEALADAGITDpYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKW--MLSPNTVAGWVNILlLSSHGPIKT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 160 SVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFaGFSSAKALTFNED-PATACRPFDKNRSGFVMGEGSGIL 238
Cdd:cd00828  158 PVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLS-GFANMGALSTAEEePEEMSRPFDETRDGFVEAEGAGVL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 239 ILEELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGeGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAI 318
Cdd:cd00828  237 VLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGK-GIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAI 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 319 KETFGEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNAR--HQEVNAVLSNS 396
Cdd:cd00828  316 AEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRdlNLKVRAALVNA 395
                        410
                 ....*....|.
gi 721831997 397 LGFGGHNAVLV 407
Cdd:cd00828  396 FGFGGSNAALV 406
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
100-408 2.57e-75

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 239.36  E-value: 2.57e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 100 RIGVWIG---SGIGGMETYEEQFKIFTEKGPrrvSPFFVPMMIPDMAAGQVSIATGAKG-INTCSvTACASGANSIGDAF 175
Cdd:PRK09185  96 RIGVVLGtstSGILEGELAYRRRDPAHGALP---ADYHYAQQELGSLADFLRAYLGLSGpAYTIS-TACSSSAKVFASAR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 176 KAIQRGDADAMITGGAEApLTSMAFAGFSSAKALTfnedpATACRPFDKNRSGFVMGEGSGILILE-ELEHALArgahiy 254
Cdd:PRK09185 172 RLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLS-----PQPCRPFSANRDGINIGEAAAFFLLErEDDAAVA------ 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 255 aeIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETFGEHaykVAISST 334
Cdd:PRK09185 240 --LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDG---VPCSST 314
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 721831997 335 KSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLDYVPNNARHQEVNAVLSNSLGFGGHNAVLVF 408
Cdd:PRK09185 315 KGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIRYVLSNSFAFGGNNCSLIF 388
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
3-407 5.04e-75

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 239.16  E-value: 5.04e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   3 KKRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLTRIDPELF--------PAKVAAEINDFEVEKYIDKKEARRMDRF 74
Cdd:PRK07103   1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPddagaglaSAFIGAELDSLALPERLDAKLLRRASLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  75 TQYAVAAAKMAVADAKLEitEENGPRIGVWI-GSGIGGMETYEeQFKIFTEKgPRRVSP-FFVPMMIPDmAAGQVSIATG 152
Cdd:PRK07103  81 AQAALAAAREAWRDAALG--PVDPDRIGLVVgGSNLQQREQAL-VHETYRDR-PAFLRPsYGLSFMDTD-LVGLCSEQFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 153 AKGInTCSV-TACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKAL---TFNEDPATACRPFDKNRSG 228
Cdd:PRK07103 156 IRGE-GFTVgGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMgsdRFADEPEAACRPFDQDRDG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 229 FVMGEGSGILILEELEHALARGAHIYAEIAGYGATGDAFHitMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTD 308
Cdd:PRK07103 235 FIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANR--GPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSP 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 309 ANEKYETMAIketFGEHAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETP-DPECdlDYVPNNARHQ 387
Cdd:PRK07103 313 LGDETELAAL---FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTAESA 387
                        410       420
                 ....*....|....*....|
gi 721831997 388 EVNAVLSNSLGFGGHNAVLV 407
Cdd:PRK07103 388 RIRYALSLSFGFGGINTALV 407
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
5-407 1.51e-66

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: 217.81  E-value: 1.51e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   5 RVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLT--RIDPELFPAKVAA-------------EINDFEVEKY-IDKKEA 68
Cdd:cd00833    2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedRWDADGYYPDPGKpgktytrrggfldDVDAFDAAFFgISPREA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  69 RRMD---RFtqyavaaakmavadaKLEITEE------------NGPRIGVWIGSGiggMETYEEQFKifteKGPRRVSPF 133
Cdd:cd00833   82 EAMDpqqRL---------------LLEVAWEaledagyspeslAGSRTGVFVGAS---SSDYLELLA----RDPDEIDAY 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 134 FVPMMIPDMAAGQVSIATGAKGiNTCSV-TACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALTfn 212
Cdd:cd00833  140 AATGTSRAFLANRISYFFDLRG-PSLTVdTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 213 edPATACRPFDKNRSGFVMGEGSGILILEELEHALARGAHIYAEIAGYGAT--GDAFHITmpAPGGEGGVRAMRQALADA 290
Cdd:cd00833  217 --PDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRTKGIT--APSGEAQAALIRRAYARA 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 291 GLQPEDIDYINAHGTSTDANEKYETMAIKETFGEHAYK---VAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTIN 367
Cdd:cd00833  293 GVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLH 372
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 721831997 368 YETPDPECDLD----YVPNNARHQEVNAVLS----NSLGFGGHNAVLV 407
Cdd:cd00833  373 FETPNPKIDFEesplRVPTEARPWPAPAGPRragvSSFGFGGTNAHVI 420
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
91-407 2.60e-57

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: 190.92  E-value: 2.60e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  91 LEITEENGPRIGVWIGSGIGGMEtyeeqFKIFTEKGPRRVSPFFVPMMIPDMAAGQVSIATGAKGINTCSVTACASGANS 170
Cdd:cd00825   28 LSREYQKNPIVGVVVGTGGGSPR-----FQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAYDVSAACAGSLHA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 171 IGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALTfnedPATACRPFDKNRSGFVMGEGSGILILEELEHALARG 250
Cdd:cd00825  103 LSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST----PEKASRTFDAAADGFVFGDGAGALVVEELEHALARG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 251 AHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETFGEHayKVA 330
Cdd:cd00825  179 AHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDK--SPA 256
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 721831997 331 ISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPecDLDYVPNNARHQEVNAVLSNSLGFGGHNAVLV 407
Cdd:cd00825  257 VSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTALLNGFGLGGTNATLV 331
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4-246 3.35e-55

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: 182.83  E-value: 3.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997    4 KRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRL--TRIDPELF---PAKVAAEI--------NDFEVEKY---IDKKE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIytkwggldDIFDFDPLffgISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   68 ARRMDRFTQYAVAAAKMAVADAKLEITEENGPRIGVWIGSGIGGmetYEEQFKIFTEKGPRRVSPFFVPMMiPDMAAGQV 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGD---YAALLLLDEDGGPRRGSPFAVGTM-PSVIAGRI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  148 SIATGAKGINTCSVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALTFNEdpatACRPFDKNRS 227
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDG----PCKAFDPFAD 232
                         250
                  ....*....|....*....
gi 721831997  228 GFVMGEGSGILILEELEHA 246
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1-407 1.85e-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: 183.15  E-value: 1.85e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997    1 MEKKRVVITGLGAVTPVGTDVETAWENIKKGVSGIGRLT--RIDPELF--PAKVAA------------EINDFEVEKY-I 63
Cdd:COG3321     1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPadRWDADAYydPDPDAPgktyvrwggfldDVDEFDALFFgI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   64 DKKEARRMD---RFtqyavaaakmavadaKLEITEE------------NGPRIGVWIGSGiggMETYEeqfkIFTEKGPR 128
Cdd:COG3321    81 SPREAEAMDpqqRL---------------LLEVAWEaledagydpeslAGSRTGVFVGAS---SNDYA----LLLLADPE 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  129 RVSPFFVPMMIPDMAAGQVSIATGAKGINtCSV-TACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAK 207
Cdd:COG3321   139 AIDAYALTGNAKSVLAGRISYKLDLRGPS-VTVdTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  208 ALTfnedPATACRPFDKNRSGFVMGEGSGILILEELEHALARGAHIYAEIAGY-----GAT-GdafhITmpAPGGEGGVR 281
Cdd:COG3321   218 MLS----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSavnqdGRSnG----LT--APNGPAQAA 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  282 AMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETFGEHAYK---VAISSTKSMTGHLLGAAGA---VEAIFSIK 355
Cdd:COG3321   288 VIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVaglIKAVLALR 367
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 721831997  356 SitdGVIPPTINYETPDPECDLD----YVPNNARHQEVN------AVlsNSLGFGGHNAVLV 407
Cdd:COG3321   368 H---GVLPPTLHFETPNPHIDFEnspfYVNTELRPWPAGggprraGV--SSFGFGGTNAHVV 424
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
254-369 1.93e-50

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: 165.82  E-value: 1.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997  254 YAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPEDIDYINAHGTSTDANEKYETMAIKETFGEHAYK--VAI 331
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 721831997  332 SSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYE 369
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
136-412 4.97e-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: 137.83  E-value: 4.97e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   136 PMMIPDMAAGQVSIATGAKGINTCSVTACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALTFNEDp 215
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   216 ataCRPFDKNRSGFVMGEGSGILILEELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGGVRAMRQALADAGLQPE 295
Cdd:TIGR02813  257 ---IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPH 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   296 DIDYINAHGTSTDANEKYETMAIKETFGE---HAYKVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPD 372
Cdd:TIGR02813  334 TCGLIEAHGTGTAAGDVAEFGGLVSVFSQdndQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPN 413
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 721831997   373 PECDLD----YVPNNAR--HQEVNAVLS----NSLGFGGHNAVLVFKSYK 412
Cdd:TIGR02813  414 PKLDIEnspfYLNTETRpwMQREDGTPRragiSSFGFGGTNFHMVLEEYS 463
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
143-407 1.00e-31

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: 121.01  E-value: 1.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 143 AAGQVSIATGAKGINTCSVT-ACASGANSIGDAFKAIQRGDADAMITGGAEApltsmafagfssakaltfnedpatacrp 221
Cdd:cd00327   46 AAGQLAYHLGISGGPAYSVNqACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 222 fdknrsgFVMGEGSGILILEELEHALARGAHIYAEIAGYGATGDAFHItMPAPGGEGGVRAMRQALADAGLQPEDIDYIN 301
Cdd:cd00327   98 -------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 302 AHGTSTDANEKYETMAIKETFGEHAykVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTinyetpdpecdldyvp 381
Cdd:cd00327  170 AHGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------- 231
                        250       260
                 ....*....|....*....|....*.
gi 721831997 382 nnarHQEVNAVLSNSLGFGGHNAVLV 407
Cdd:cd00327  232 ----PREPRTVLLLGFGLGGTNAAVV 253
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
162-407 2.84e-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: 104.33  E-value: 2.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   162 TACASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALTfnedPATACRPFDKNRSGFVMGEGSGILILE 241
Cdd:smart00825  95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS----PDGRCKTFDASADGYVRGEGVGVVVLK 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   242 ELEHALARGAHIYAEIAGYGATGDAFHITMPAPGGEGgvramrQaladaglqpedidyinahgtstdanekyetmaiket 321
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPA------Q------------------------------------ 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997   322 fgehaykVAISSTKSMTGHLLGAAGAVEAIFSIKSITDGVIPPTINYETPDPECDLD----YVPNNARHQEVN------A 391
Cdd:smart00825 209 -------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPgrprraG 281
                          250
                   ....*....|....*.
gi 721831997   392 VlsNSLGFGGHNAVLV 407
Cdd:smart00825 282 V--SSFGFGGTNAHVI 295
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
165-300 4.83e-06

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 48.09  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 165 ASGANSIGDAFKAIQRGDADAMITGGAEAPLTSMAFAGFSSAKALTFNEdpatacrpfdkNRSGFVMGEGSGILILEELE 244
Cdd:PRK06147 134 VSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQ-----------NSNGFIPGEAAAAVLLGRPA 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 721831997 245 HALARGAHIYA-----EIAGYGATGDAfhitmpaPG-GEGGVRAMRQALADAGLQPEDIDYI 300
Cdd:PRK06147 203 GGEAPGLPLLGlglgrEPAPVGESEDL-------PLrGDGLTQAIRAALAEAGCGLEDMDYR 257
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
144-345 1.61e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 46.87  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 144 AGQVSIATGAKGINTCSVTACASGANSIGDAFKAIQRGDADAMITGG---AEAP--LTSMAFAGFSSAKALTfnedPATA 218
Cdd:PRK06519 155 AGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGaynAERPdmLLLYELGGLLLKGGWA----PVWS 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 219 CRPFDKnrSGFVMGEGSGILILEELEHALARGAHIYAEIAGYgatgdafhITMPAPGGEGGVRA-MRQALADAGLQPEDI 297
Cdd:PRK06519 231 RGGEDG--GGFILGSGGAFLVLESREHAEARGARPYARISGV--------ESDRARRAPGDLEAsLERLLKPAGGLAAPT 300
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 721831997 298 DYINAhgtstdANEKYETMAIKETFGEHAYKVAISSTKSMTGHLLGAA 345
Cdd:PRK06519 301 AVISG------ATGAHPATAEEKAALEAALAGPVRGIGTLFGHTMEAQ 342
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
211-347 1.67e-04

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 43.54  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 211 FNEDPATACRPFDKNRSGFV-------MGEGSGILILEELEHALARGAHIYAEIAGYG--ATGDAFHITMPApggeggvR 281
Cdd:PLN02644 223 FDPAKLRKLRPSFKEDGGSVtagnassISDGAAALVLVSGEKALELGLQVIAKIRGYAdaAQAPELFTTAPA-------L 295
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 721831997 282 AMRQALADAGLQPEDIDYInahgtstDANEKYETMAI--KETFGEHAYKVAISSTKSMTGHLLGAAGA 347
Cdd:PLN02644 296 AIPKALKHAGLEASQVDYY-------EINEAFSVVALanQKLLGLDPEKVNVHGGAVSLGHPIGCSGA 356
PRK09051 PRK09051
beta-ketothiolase BktB;
222-357 8.37e-04

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 41.48  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 222 FDKNRSGFVMGEGSGI------LILEELEHALARGAHIYAEIAGYGATGdafhiTMPAPGGEGGVRAMRQALADAGLQPE 295
Cdd:PRK09051 236 FKKENGTVTAGNASGIndgaaaVVLAEADAAEARGLKPLARLVGYAHAG-----VDPEYMGIGPVPATQKALERAGLTVA 310
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 721831997 296 DIDYInahgtstDANEKY--ETMAIKETFGEHAYKV-----AISstksmTGHLLGAAGaveAIFSIKSI 357
Cdd:PRK09051 311 DLDVI-------EANEAFaaQACAVTRELGLDPAKVnpngsGIS-----LGHPVGATG---AIITVKAL 364
PRK05790 PRK05790
putative acyltransferase; Provisional
220-347 1.20e-03

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 40.91  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 220 RP-FDKNrsGFVM-GEGSGI------LILEELEHALARGAHIYAEIAGYG-ATGDafhitmPAPGGEGGVRAMRQALADA 290
Cdd:PRK05790 233 RPaFDKD--GTVTaGNASGIndgaaaVVVMSEAKAKELGLTPLARIVSYAvAGVD------PAIMGIGPVPAIRKALEKA 304
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721831997 291 GLQPEDIDYInahgtstDANEKYETMAI---KEtFGEHAYKV-----AISstksmTGHLLGAAGA 347
Cdd:PRK05790 305 GWSLADLDLI-------EINEAFAAQALaveKE-LGLDPEKVnvnggAIA-----LGHPIGASGA 356
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
234-300 1.62e-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: 40.43  E-value: 1.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 721831997 234 GSGILILEELEHALARGAHIYAEIAGYGATGDAFHItMpapgGEGGVRAMRQALADAGLQPEDIDYI 300
Cdd:COG0183  251 GAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEI-M----GIGPVPATRKALARAGLTLDDIDLI 312
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
163-209 1.90e-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: 40.05  E-value: 1.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 721831997 163 ACASGANSIGDAFKAIQRGDADAMITGGAEapltSMAFAGFSSAKAL 209
Cdd:COG0183   87 VCGSGLQAVALAAQAIAAGDADVVIAGGVE----SMSRAPMLLPKAR 129
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
234-300 3.94e-03

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 39.00  E-value: 3.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 721831997 234 GSGILILEELEHALARGAHIYAEIAGYGATGDAFHItMpapgGEGGVRAMRQALADAGLQPEDIDYI 300
Cdd:cd00751  247 GAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAI-M----GIGPVPAIPKALKRAGLTLDDIDLI 308
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
225-348 6.60e-03

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 38.60  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721831997 225 NRSGFVmgEGSGILILEELEHALARGAHIYAEIAGYGATGDAFHITMPAPggeggVRAMRQALADAGLQPEDIDYInahg 304
Cdd:PRK06025 270 NSSGVV--DGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAP-----VPAAKKVLAKAGLTKDDIDLW---- 338
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 721831997 305 tstDANEKYETMAIK--ETFGEHAYKVAISSTKSMTGHLLGAAGAV 348
Cdd:PRK06025 339 ---EINEAFAVVAEKfiRDLDLDRDKVNVNGGAIALGHPIGATGSI 381
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
279-305 8.80e-03

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


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 37.78  E-value: 8.80e-03
                         10        20
                 ....*....|....*....|....*...
gi 721831997 279 GVRAMRQALADAGLQPEDIDY-INAHGT 305
Cdd:COG0332   55 AVEAARKALEAAGIDPEDIDLiIVATVT 82
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH