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Conserved domains on  [gi|2209889639|ref|WP_241836147|]
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beta-ketoacyl synthase [Streptomyces sp. JS01]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase family protein( domain architecture ID 11416750)

beta-ketoacyl-[acyl-carrier-protein] synthase family protein similar to nodulation protein E (nodE), which is involved in the synthesis of a highly unsaturated fatty acid moiety that is part of a lipo-oligosaccharide responsible for host specificity, and to polyketide beta-ketoacyl synthases, which are involved in the synthesis of polyketide antibiotics and related compounds

CATH:  3.40.47.10
EC:  2.3.1.-
Gene Ontology:  GO:0006633|GO:0004315
PubMed:  25456814|11969206
SCOP:  3000122

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 10-412 2.37e-176

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: 497.70  E-value: 2.37e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  10 DVAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGL--EGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARL 87
Cdd:COG0304     2 RVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFdaSGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAARE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  88 AVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTAC 167
Cdd:COG0304    82 ALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTAC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 168 ASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLVLERV 247
Cdd:COG0304   162 ASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEEL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 248 ADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIG 327
Cdd:COG0304   242 EHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 328 DH---PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGFGGQN 404
Cdd:COG0304   322 DHaykVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGHN 401


                  ....*...
gi 2209889639 405 AAVVVTAA 412
Cdd:COG0304   402 ASLVFKRY 409
 
Name Accession Description Interval E-value
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 10-412 2.37e-176

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: 497.70  E-value: 2.37e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  10 DVAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGL--EGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARL 87
Cdd:COG0304     2 RVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFdaSGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAARE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  88 AVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTAC 167
Cdd:COG0304    82 ALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTAC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 168 ASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLVLERV 247
Cdd:COG0304   162 ASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEEL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 248 ADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIG 327
Cdd:COG0304   242 EHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 328 DH---PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGFGGQN 404
Cdd:COG0304   322 DHaykVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGHN 401


                  ....*...
gi 2209889639 405 AAVVVTAA 412
Cdd:COG0304   402 ASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 11-409 4.87e-167

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: 474.33  E-value: 4.87e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRSTASR--SPGLEGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARLA 88
Cdd:cd00834     3 VVITGLGAVTPLGNGVEEFWEALLAGRSGIRPitRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAEEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  89 VSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTACA 168
Cdd:cd00834    83 LADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 169 SGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLVLERVA 248
Cdd:cd00834   163 SGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLESLE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 249 DAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIGD 328
Cdd:cd00834   243 HAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGE 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 329 H---PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGFGGQNA 405
Cdd:cd00834   323 HakkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGHNA 402


                  ....
gi 2209889639 406 AVVV 409
Cdd:cd00834   403 SLVF 406
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 11-409 1.43e-157

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: 450.01  E-value: 1.43e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGL--EGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARLA 88
Cdd:TIGR03150   3 VVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFdaSDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAKEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  89 VSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTACA 168
Cdd:TIGR03150  83 VEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTACA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 169 SGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLVLERVA 248
Cdd:TIGR03150 163 TGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 249 DAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIGD 328
Cdd:TIGR03150 243 HAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVFGD 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 329 H---PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGFGGQNA 405
Cdd:TIGR03150 323 HaykLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGTNA 402


                  ....
gi 2209889639 406 AVVV 409
Cdd:TIGR03150 403 SLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
6-408 2.35e-143

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 414.19  E-value: 2.35e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639   6 RRRfdVAVTGLGLITPAGTGVKANVARIWDGRSTASR--SPGLEGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVT 83
Cdd:PRK07314    1 KRR--VVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPitHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  84 AARLAVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVV 163
Cdd:PRK07314   79 AAKQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 164 STACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLV 243
Cdd:PRK07314  159 VTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 244 LERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIR 323
Cdd:PRK07314  239 LEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIK 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 324 RVIGDHP---LVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGF 400
Cdd:PRK07314  319 RVFGEHAykvAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGF 398


                  ....*...
gi 2209889639 401 GGQNAAVV 408
Cdd:PRK07314  399 GGTNASLV 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 10-250 4.88e-39

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: 140.46  E-value: 4.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  10 DVAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGLEGMAVDFSC-----------------RVEDFDPAAE-LGRRTA 71
Cdd:pfam00109   2 PVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDppsriagkiytkwggldDIFDFDPLFFgISPREA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  72 LRMDRVSQLGVTAARLAVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREhetYLSSGPTVVSPqLMVTAPVNMTAGHIA 151
Cdd:pfam00109  82 ERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLL---DEDGGPRRGSP-FAVGTMPSVIAGRIS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 152 MDCQALGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRraEDPAAASRPFDahrD 231
Cdd:pfam00109 158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA---D 232

                         250
                  ....*....|....*....
gi 2209889639 232 GFVAGEGAGVLVLERVADA 250
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 57-409 3.13e-27

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: 109.73  E-value: 3.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639   57 VEDFDPAA-ELGRRTALRMD---RvsqLGVTAARLAVSDAGLDPQVWDGARVAVVIGTSFGGSAsferehetylssgptv 132
Cdd:smart00825  30 VDLFDAAFfGISPREAEAMDpqqR---LLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDYS---------------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  133 vspqlmvtapvnMTaghiamdcqalgpnqvVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGAL 212
Cdd:smart00825  91 ------------VT----------------VDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGML 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  213 SrraedPAAASRPFDAHRDGFVAGEGAGVLVLERVADAHARGARVRARISGFGASADGFHAS--APHPTGdgaeramraa 290
Cdd:smart00825 143 S-----PDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGitAPSGPA---------- 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  291 ladacldpaevahvnahgtstpkndvteaavirrvigdHPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLE 370
Cdd:smart00825 208 --------------------------------------QLLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFE 249

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2209889639  371 RVDPQVEID-----VV--------AGAPRTATIgaamsNSFGFGGQNAAVVV 409
Cdd:smart00825 250 TPNPHIDLEesplrVPteltpwppPGRPRRAGV-----SSFGFGGTNAHVIL 296
 
Name Accession Description Interval E-value
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 10-412 2.37e-176

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: 497.70  E-value: 2.37e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  10 DVAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGL--EGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARL 87
Cdd:COG0304     2 RVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFdaSGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAARE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  88 AVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTAC 167
Cdd:COG0304    82 ALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTAC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 168 ASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLVLERV 247
Cdd:COG0304   162 ASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEEL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 248 ADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIG 327
Cdd:COG0304   242 EHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 328 DH---PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGFGGQN 404
Cdd:COG0304   322 DHaykVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGHN 401


                  ....*...
gi 2209889639 405 AAVVVTAA 412
Cdd:COG0304   402 ASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 11-409 4.87e-167

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: 474.33  E-value: 4.87e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRSTASR--SPGLEGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARLA 88
Cdd:cd00834     3 VVITGLGAVTPLGNGVEEFWEALLAGRSGIRPitRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAEEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  89 VSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTACA 168
Cdd:cd00834    83 LADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 169 SGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLVLERVA 248
Cdd:cd00834   163 SGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLESLE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 249 DAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIGD 328
Cdd:cd00834   243 HAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGE 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 329 H---PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGFGGQNA 405
Cdd:cd00834   323 HakkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGHNA 402


                  ....
gi 2209889639 406 AVVV 409
Cdd:cd00834   403 SLVF 406
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 11-409 1.43e-157

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: 450.01  E-value: 1.43e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGL--EGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARLA 88
Cdd:TIGR03150   3 VVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFdaSDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAKEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  89 VSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTACA 168
Cdd:TIGR03150  83 VEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTACA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 169 SGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLVLERVA 248
Cdd:TIGR03150 163 TGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 249 DAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIGD 328
Cdd:TIGR03150 243 HAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVFGD 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 329 H---PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGFGGQNA 405
Cdd:TIGR03150 323 HaykLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGTNA 402


                  ....
gi 2209889639 406 AVVV 409
Cdd:TIGR03150 403 SLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
6-408 2.35e-143

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 414.19  E-value: 2.35e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639   6 RRRfdVAVTGLGLITPAGTGVKANVARIWDGRSTASR--SPGLEGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVT 83
Cdd:PRK07314    1 KRR--VVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPitHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  84 AARLAVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVV 163
Cdd:PRK07314   79 AAKQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 164 STACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLV 243
Cdd:PRK07314  159 VTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 244 LERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIR 323
Cdd:PRK07314  239 LEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIK 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 324 RVIGDHP---LVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGF 400
Cdd:PRK07314  319 RVFGEHAykvAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGF 398


                  ....*...
gi 2209889639 401 GGQNAAVV 408
Cdd:PRK07314  399 GGTNASLV 406
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
6-408 9.73e-111

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 331.58  E-value: 9.73e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639   6 RRRfdVAVTGLGLITPAGTGVKANVARIWDGRSTASRSPG--LEGMAVDFSCRVED--------FDPAAELGRRTALRMD 75
Cdd:PRK06333    3 KKR--IVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDfpVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  76 RVSQLGVTAARLAVSDAGLDPQ-VWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPqlmVTAP---VNMTAGHIA 151
Cdd:PRK06333   81 RFILFAMAAAKEALAQAGWDPDtLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSP---FTIPsflTNMAAGHVS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 152 MDCQALGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRR-AEDPAAASRPFDAHR 230
Cdd:PRK06333  158 IRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 231 DGFVAGEGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTS 310
Cdd:PRK06333  238 DGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 311 TPKNDVTEAAVIRRVIGD--HPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVE-IDVVAGAPRT 387
Cdd:PRK06333  318 TPVGDLGEVAAIKKVFGHvsGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARP 397

                         410       420
                  ....*....|....*....|.
gi 2209889639 388 ATIGAAMSNSFGFGGQNAAVV 408
Cdd:PRK06333  398 MDMDYALSNGFGFGGVNASIL 418
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 11-408 2.98e-108

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 324.76  E-value: 2.98e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRSTASR--SPGLEGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARLA 88
Cdd:PRK08439    4 VVVTGIGMINSLGLNKESSFKAICNGECGIKKitLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAREA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  89 VSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTACA 168
Cdd:PRK08439   84 MKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTACA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 169 SGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLVLERVA 248
Cdd:PRK08439  164 AGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEEYE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 249 DAHARGARVRARISGFGASADGFHASAPHPtgDGAERAMRAALADAclDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIGD 328
Cdd:PRK08439  244 SAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMA--GNPKIDYINAHGTSTPYNDKNETAALKELFGS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 329 H---PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGFGGQNA 405
Cdd:PRK08439  320 KekvPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGTNG 399


                  ...
gi 2209889639 406 AVV 408
Cdd:PRK08439  400 VVI 402
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 18-410 6.75e-100

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 303.92  E-value: 6.75e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  18 LITPAGTGVKANVARIWDGRS--------------TASRSPGLEGMAVDFSCRV------EDFDPAAelgRRTALRMDRV 77
Cdd:PTZ00050    1 VVTPLGVGAESTWEALIAGKSgirkltefpkflpdCIPEQKALENLVAAMPCQIaaevdqSEFDPSD---FAPTKRESRA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  78 SQLGVTAARLAVSDAGLDP-QVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQA 156
Cdd:PTZ00050   78 THFAMAAAREALADAKLDIlSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 157 LGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAED-PAAASRPFDAHRDGFVA 235
Cdd:PTZ00050  158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDdPQRASRPFDKDRAGFVM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 236 GEGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALAD-ACLDPAEVAHVNAHGTSTPKN 314
Cdd:PTZ00050  238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANININDVDYVNAHATSTPIG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 315 DVTEAAVIRRVIGDHP----LVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTA-- 388
Cdd:PTZ00050  318 DKIELKAIKKVFGDSGapklYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPlq 397

                         410       420
                  ....*....|....*....|..
gi 2209889639 389 TIGAAMSNSFGFGGQNAAVVVT 410
Cdd:PTZ00050  398 SIDAVLSTSFGFGGVNTALLFT 419
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
6-408 1.27e-91

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 282.28  E-value: 1.27e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639   6 RRRfdVAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGLEgmAVDFSCR----VEDFDPAAELGRRTALRMDRVSQLG 81
Cdd:PRK08722    3 KRR--VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFD--TTNFSTRfaglVKDFNCEEYMSKKDARKMDLFIQYG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  82 VTAARLAVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQ 161
Cdd:PRK08722   79 IAAGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 162 VVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGV 241
Cdd:PRK08722  159 AISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 242 LVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAV 321
Cdd:PRK08722  239 MVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 322 IRRVIG----DHPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPR-TATIGAAMSN 396
Cdd:PRK08722  319 IKRALGeagsKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARkVESMEYAICN 398

                         410
                  ....*....|..
gi 2209889639 397 SFGFGGQNAAVV 408
Cdd:PRK08722  399 SFGFGGTNGSLI 410
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 11-412 1.15e-89

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 277.83  E-value: 1.15e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRStasrspGLEGMAVD------------------FSCRV----------EDFDP 62
Cdd:PLN02836    8 VVVTGLGLVTPLGCGVETTWRRLIAGEC------GVRALTQDdlkmksedeetqlytldqLPSRVaalvprgtgpGDFDE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  63 AAELGRRtalRMDRVSQLGVTAARLAVSDAGLDPQVWDGA-RVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTA 141
Cdd:PLN02836   82 ELWLNSR---SSSRFIGYALCAADEALSDARWLPSEDEAKeRTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 142 PVNMTAGHIAMDCQALGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAED-PA 220
Cdd:PLN02836  159 LINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKFNScPT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 221 AASRPFDAHRDGFVAGEGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAE 300
Cdd:PLN02836  239 EASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 301 VAHVNAHGTSTPKNDVTEAAVIRRVIGDHPL-----VTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQ 375
Cdd:PLN02836  319 VDYVNAHATSTPLGDAVEARAIKTVFSEHATsgglaFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI 398

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 2209889639 376 VEIDVVA-GAPRTATIGAAMSNSFGFGGQNAAVVVTAA 412
Cdd:PLN02836  399 FDDGFVPlTASKAMLIRAALSNSFGFGGTNASLLFTSP 436
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
10-408 9.96e-81

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 254.27  E-value: 9.96e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  10 DVAVTGLGLITPAGTGVKANVARIWDGRStasrspGLEGMAVDFscrVEDFD------------PAAELGRRTALRMDRV 77
Cdd:PRK07910   13 NVVVTGIAMTTALATDAETTWKLLLDGQS------GIRTLDDPF---VEEFDlpvrigghlleeFDHQLTRVELRRMSYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  78 SQLGVTAARLAVSDAGlDPQVwDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQAL 157
Cdd:PRK07910   84 QRMSTVLGRRVWENAG-SPEV-DTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 158 GPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGA-LSRRAEDPAAASRPFDAHRDGFVAG 236
Cdd:PRK07910  162 AGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 237 EGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDV 316
Cdd:PRK07910  242 EGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDV 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 317 TEAAVIRRVIGDH-PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMS 395
Cdd:PRK07910  322 AEGKAINNALGGHrPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAIN 401

                         410
                  ....*....|...
gi 2209889639 396 NSFGFGGQNAAVV 408
Cdd:PRK07910  402 NSFGFGGHNVALA 414
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 2-408 1.59e-78

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 252.21  E-value: 1.59e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639   2 TAVRRRRfdVAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGLEgmAVDFSCR----VEDFDPAAELGRRTALRMDRV 77
Cdd:PLN02787  124 PLTKQRR--VVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFD--CSQFPTRiageIKSFSTDGWVAPKLSKRMDKF 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  78 SQLGVTAARLAVSDAGLDPQV---WDGARVAVVIGTSFGGSASFEREHETyLSSGPTVVSPQLMVTAPVNMTAGHIAMDC 154
Cdd:PLN02787  200 MLYLLTAGKKALADGGITEDVmkeLDKTKCGVLIGSAMGGMKVFNDAIEA-LRISYRKMNPFCVPFATTNMGSAMLAMDL 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 155 QALGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFV 234
Cdd:PLN02787  279 GWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFV 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 235 AGEGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKN 314
Cdd:PLN02787  359 MGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAG 438

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 315 DVTEAAVIRRVIGDHP--LVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRT-ATIG 391
Cdd:PLN02787  439 DLKEYQALMRCFGQNPelRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKErLDIK 518

                         410
                  ....*....|....*..
gi 2209889639 392 AAMSNSFGFGGQNAAVV 408
Cdd:PLN02787  519 VALSNSFGFGGHNSSIL 535
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
11-411 5.88e-78

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 247.24  E-value: 5.88e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRS---TASRSPgLEGMAVDFSCRVeDFDPAAELGRrtalrMDRVSQLGVTAARL 87
Cdd:PRK06501   13 VAVTGMGVVTSLGQGKADNWAALTAGESgihTITRFP-TEGLRTRIAGTV-DFLPESPFGA-----SALSEALARLAAEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  88 AVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVS----------PQLMVTAPVNMTAGHIAMDCQAL 157
Cdd:PRK06501   86 ALAQAGIGKGDFPGPLFLAAPPVELEWPARFALAAAVGDNDAPSYDRllraarggrfDALHERFQFGSIADRLADRFGTR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 158 GPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGE 237
Cdd:PRK06501  166 GLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGFVMAE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 238 GAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVT 317
Cdd:PRK06501  246 GAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKM 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 318 EAAVIRRVIGDH----PlVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAA 393
Cdd:PRK06501  326 EYLGLSAVFGERlasiP-VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARVTAV 404

                         410
                  ....*....|....*...
gi 2209889639 394 MSNSFGFGGQNAAVVVTA 411
Cdd:PRK06501  405 LSNSFGFGGQNASLVLTA 422
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
11-408 1.64e-74

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 237.43  E-value: 1.64e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRSTasrspgleGMAVdfsCRVEDFDPAAELGRRTAL--------------RMDR 76
Cdd:PRK09185    4 VYISAFGATSALGRGLDAILAALRAGRAS--------GMRP---CDFWLVDLPTWVGEVVGVelpalpaalaafdcRNNR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  77 VSQLGVTAARLAVSDAgldPQVWDGARVAVVIGTSFGG----SASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAM 152
Cdd:PRK09185   73 LALLALQQIEPAVEAA---IARYGADRIGVVLGTSTSGilegELAYRRRDPAHGALPADYHYAQQELGSLADFLRAYLGL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 153 DcqalGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGG--SEAALTRTGMASLhkmGALSRRAedpaaaSRPFDAHR 230
Cdd:PRK09185  150 S----GPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGvdSLCRLTLNGFNSL---ESLSPQP------CRPFSANR 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 231 DGFVAGEGAGVLVLERVADAhargarvRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTS 310
Cdd:PRK09185  217 DGINIGEAAAFFLLEREDDA-------AVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTA 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 311 TPKNDVTEAAVIRRVIGDHPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATI 390
Cdd:PRK09185  290 TPLNDAMESRAVAAVFGDGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAI 369

                         410
                  ....*....|....*...
gi 2209889639 391 GAAMSNSFGFGGQNAAVV 408
Cdd:PRK09185  370 RYVLSNSFAFGGNNCSLI 387
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
11-408 4.38e-73

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 234.18  E-value: 4.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGLEGMAvdFSCRVE---DFDPAAELGRRTALRMDRVSQLGVTAARL 87
Cdd:PRK07967    4 VVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMG--MRSQVWgnvKLDPTGLIDRKVMRFMGDASAYAYLAMEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  88 AVSDAGLDPQVWDGARVAVVIGtSFGGSASFEREHE--TYLSSGPTVVSPqLMVTAPVNMTAGH-IAMDCQALGPNQVVS 164
Cdd:PRK07967   82 AIADAGLSEEQVSNPRTGLIAG-SGGGSTRNQVEAAdaMRGPRGPKRVGP-YAVTKAMASTVSAcLATPFKIKGVNYSIS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 165 TACASGTTAIGIGRMLLEAGLCDVVLAGGSEAaLTRTGMASLHKMGALS-RRAEDPAAASRPFDAHRDGFVAGEGAGVLV 243
Cdd:PRK07967  160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEE-LDWEMSCLFDAMGALStKYNDTPEKASRAYDANRDGFVIAGGGGVVV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 244 LERVADAHARGARVRARISGFGASADGFHASAphPTGDGAERAMRAALADAcldPAEVAHVNAHGTSTPKNDVTEAAVIR 323
Cdd:PRK07967  239 VEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMALATV---DTPIDYINTHGTSTPVGDVKELGAIR 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 324 RVIGDH-PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVE-IDVVAGAPRTATIGAAMSNSFGFG 401
Cdd:PRK07967  314 EVFGDKsPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAgMPIVTETTDNAELTTVMSNSFGFG 393


                  ....*..
gi 2209889639 402 GQNAAVV 408
Cdd:PRK07967  394 GTNATLV 400
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
10-409 6.53e-73

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 233.02  E-value: 6.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  10 DVAVTGLGLITPAGTgVKANVARIWDGRS-TASRSPGLEGMAVdfscrvedfdPAAELGRRTAlRMDRVSQLGVTAArla 88
Cdd:PRK05952    3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSgIKLHQPFPELPPL----------PLGLIGNQPS-SLEDLTKTVVTAA--- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  89 VSDAGLDPQVWDgarVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMV----TAPvNMTAGHIAMDCQALGPNQVVS 164
Cdd:PRK05952   68 LKDAGLTPPLTD---CGVVIGSSRGCQGQWEKLARQMYQGDDSPDEELDLEnwldTLP-HQAAIAAARQIGTQGPVLAPM 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 165 TACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALsrrAEDPAAasrPFDAHRDGFVAGEGAGVLVL 244
Cdd:PRK05952  144 AACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGAL---AKTGAY---PFDRQREGLVLGEGGAILVL 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 245 ERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRR 324
Cdd:PRK05952  218 ESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQA 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 325 VIGDHPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLErvDPQVEIDVVAgAPRTATIGAAMSNSFGFGGQN 404
Cdd:PRK05952  298 LFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQ--EPEFDLNFVR-QAQQSPLQNVLCLSFGFGGQN 374


                  ....*
gi 2209889639 405 AAVVV 409
Cdd:PRK05952  375 AAIAL 379
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
11-408 2.02e-71

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 229.87  E-value: 2.02e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGLE---GMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARL 87
Cdd:PRK09116    4 VVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDrydGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRASEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  88 AVSDAGL--DPQVWDGaRVAVVIGTSFGGSA---SFEREHETYLSSGPTVVS-PQLMV-TAPVNMT-----AGHIAmdcq 155
Cdd:PRK09116   84 ALEDAGLlgDPILTDG-RMGIAYGSSTGSTDpigAFGTMLLEGSMSGITATTyVRMMPhTTAVNVGlffglKGRVI---- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 156 algpnqVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAaLTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVA 235
Cdd:PRK09116  159 ------PTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 236 GEGAGVLVLERVADAHARGARVRARISGFGASADGFHASapHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKND 315
Cdd:PRK09116  232 GEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVT--QPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGD 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 316 VTEAAVIRRVIGDHPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQV-EIDVVAGAPRTATIGAAM 394
Cdd:PRK09116  310 IAESQATAAVFGARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYVM 389

                         410
                  ....*....|....
gi 2209889639 395 SNSFGFGGQNAAVV 408
Cdd:PRK09116  390 SNNFAFGGINTSLI 403
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 11-409 7.18e-71

"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: 228.48  E-value: 7.18e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTG---VKANVARIWDGRST-ASRSPGLEGMAVDFSCRVEDFDPAAELGRRTaLRMDRVSQLGVTAAR 86
Cdd:cd00828     3 VVITGIGVVSPHGEGcdeVEEFWEALREGRSGiAPVARLKSRFDRGVAGQIPTGDIPGWDAKRT-GIVDRTTLLALVATE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  87 LAVSDAGL-DPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTApvNMTAGHIAMDCQ-ALGPNQVVS 164
Cdd:cd00828    82 EALADAGItDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLSP--NTVAGWVNILLLsSHGPIKTPV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 165 TACASGTTAIGIGRMLLEAGLCDVVLAGGSEAaLTRTGMASLHKMGALSRRAEDPAAASRPFDAHRDGFVAGEGAGVLVL 244
Cdd:cd00828   160 GACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGAGVLVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 245 ERVADAHARGARVRARISGFGASADGFHASAPhPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRR 324
Cdd:cd00828   239 ERAELALARGAPIYGRVAGTASTTDGAGRSVP-AGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 325 VIGDHPL---VTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTA--TIGAAMSNSFG 399
Cdd:cd00828   318 VAGALGAplpVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLnlKVRAALVNAFG 397

                         410
                  ....*....|
gi 2209889639 400 FGGQNAAVVV 409
Cdd:cd00828   398 FGGSNAALVL 407
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 53-409 1.16e-69

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: 225.90  E-value: 1.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  53 FSCRVEDFDPAA-ELGRRTALRMDRVSQLGVTAARLAVSDAGLDPQVWDGARVAVVIGTSFggsasfeREHETYLSSGPT 131
Cdd:cd00833    62 FLDDVDAFDAAFfGISPREAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASS-------SDYLELLARDPD 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 132 VVSPQLMVTAPVNMTAGHIA--MDCQalGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKM 209
Cdd:cd00833   135 EIDAYAATGTSRAFLANRISyfFDLR--GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKA 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 210 GALSrraedPAAASRPFDAHRDGFVAGEGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRA 289
Cdd:cd00833   213 GMLS-----PDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRR 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 290 ALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIGDHP------LVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSV 363
Cdd:cd00833   288 AYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRsadqplLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVI 367

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2209889639 364 PPTANLERVDPQVEID-------------VVAGAPRTATIgaamsNSFGFGGQNAAVVV 409
Cdd:cd00833   368 PPNLHFETPNPKIDFEesplrvptearpwPAPAGPRRAGV-----SSFGFGGTNAHVIL 421
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 103-409 3.69e-69

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 222.30  E-value: 3.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 103 RVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTACASGTTAIGIGRMLLE 182
Cdd:PRK14691   27 RTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 183 AGLCDVVLAGGSEAALTRTGMASLHKMGALSRR-AEDPAAASRPFDAHRDGFVAGEGAGVLVLERVADAHARGARVRARI 261
Cdd:PRK14691  107 NNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEI 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 262 SGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIGDHP--LVTSTKGVI 339
Cdd:PRK14691  187 VGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNalAITSTKSAT 266

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2209889639 340 GHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVE-IDVVAGAPRTATIGAAMSNSFGFGGQNAAVVV 409
Cdd:PRK14691  267 GHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILL 337
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 8-409 1.58e-68

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 222.60  E-value: 1.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639   8 RFDVAVTGLGLITPAGTGVKANVARIWDGRST---ASRSPGLEGMAVD-------FSCRVEDFDPAAELGRRTALRMDRV 77
Cdd:PRK07103    1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAfgvMRRPGRQVPDDAGaglasafIGAELDSLALPERLDAKLLRRASLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  78 SQLGVTAARLAVSDAGLDPQvwDGARVAVVIGtsfgGSASFERE----HETYLSSgPTVVSPQLMVTAPVNMTAGHIAMD 153
Cdd:PRK07103   81 AQAALAAAREAWRDAALGPV--DPDRIGLVVG----GSNLQQREqalvHETYRDR-PAFLRPSYGLSFMDTDLVGLCSEQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 154 CQALGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGAL--SRRAEDPAAASRPFDAHRD 231
Cdd:PRK07103  154 FGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMgsDRFADEPEAACRPFDQDRD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 232 GFVAGEGAGVLVLERVADAHARGARVRARISGFGASADGfhASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTST 311
Cdd:PRK07103  234 GFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA--NRGPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGS 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 312 PKNDVTEAAVIRRVIGDHPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLER-VDPQveIDVVAGAPRTATI 390
Cdd:PRK07103  312 PLGDETELAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEpIDER--FRWVGSTAESARI 389

                         410
                  ....*....|....*....
gi 2209889639 391 GAAMSNSFGFGGQNAAVVV 409
Cdd:PRK07103  390 RYALSLSFGFGGINTALVL 408
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 11-409 4.09e-66

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: 216.07  E-value: 4.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  11 VAVTGLGLITPAGTGVKANVARIWDGRSTASRSP--GLEGMAVDFSCRVEDFDPAAELGRRTALRMDRVSQLGVTAARLA 88
Cdd:cd00832     3 AVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITrfDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAADWA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  89 VSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTAPVNMTAGHIAMDCQALGPNQVVSTACA 168
Cdd:cd00832    83 LADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAEQA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 169 SGTTAIGIGRMLLEAGLCdVVLAGGSEAALTRTGMASLHKMGALSRrAEDPAAASRPFDAHRDGFVAGEGAGVLVLERVA 248
Cdd:cd00832   163 GGLDALAQARRLVRRGTP-LVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGAILVLEDAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 249 DAHARGARVRARISGFGASADGFHASAPHPtgdGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIGD 328
Cdd:cd00832   241 AARERGARVYGEIAGYAATFDPPPGSGRPP---GLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVFGP 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 329 HPL-VTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVEIDVVAGAPRTATIGAAMSNSFGFGGQNAAV 407
Cdd:cd00832   318 RGVpVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGGFNSAL 397


                  ..
gi 2209889639 408 VV 409
Cdd:cd00832   398 VV 399
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 76-409 5.45e-53

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: 179.75  E-value: 5.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  76 RVSQLGVTAARLAVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREHETYLSSGPTVVSPQLMVTApvnmtAGHIAMDCQ 155
Cdd:cd00825    10 YVSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGA-----SGQIATPLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 156 ALGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALtrtgmASLHKMGALSRRAEDPAAASRPFDAHRDGFVA 235
Cdd:cd00825    85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELA-----APMDCEFDAMGALSTPEKASRTFDAAADGFVF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 236 GEGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKND 315
Cdd:cd00825   160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 316 VTEAAVIRRVIGDHPL-VTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPqvEIDVVAGAPRTATIGAAM 394
Cdd:cd00825   240 VKELKLLRSEFGDKSPaVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTAL 317

                         330
                  ....*....|....*
gi 2209889639 395 SNSFGFGGQNAAVVV 409
Cdd:cd00825   318 LNGFGLGGTNATLVL 332
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 57-412 9.79e-46

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 169.28  E-value: 9.79e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639   57 VEDFDPAA-ELGRRTALRMDRVSQLGVTAARLAVSDAGLDPQVWDGARVAVVIGTSFGgsasferEHETYLSSGPTVVSP 135
Cdd:COG3321     70 VDEFDALFfGISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSN-------DYALLLLADPEAIDA 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  136 QLMVTAPVNMTAGHIA--MDCQalGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALS 213
Cdd:COG3321    143 YALTGNAKSVLAGRISykLDLR--GPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  214 rraedPAAASRPFDAHRDGFVAGEGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALAD 293
Cdd:COG3321    221 -----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALAD 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  294 ACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIG-----DHPL-VTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTA 367
Cdd:COG3321    296 AGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGqgrpaDQPCaIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTL 375

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2209889639  368 NLERVDPQVEID-------------VVAGAPRTATIgaamsNSFGFGGQNAAVVVTAA 412
Cdd:COG3321    376 HFETPNPHIDFEnspfyvntelrpwPAGGGPRRAGV-----SSFGFGGTNAHVVLEEA 428
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 10-250 4.88e-39

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: 140.46  E-value: 4.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  10 DVAVTGLGLITPAGTGVKANVARIWDGRSTASRSPGLEGMAVDFSC-----------------RVEDFDPAAE-LGRRTA 71
Cdd:pfam00109   2 PVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDppsriagkiytkwggldDIFDFDPLFFgISPREA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  72 LRMDRVSQLGVTAARLAVSDAGLDPQVWDGARVAVVIGTSFGGSASFEREhetYLSSGPTVVSPqLMVTAPVNMTAGHIA 151
Cdd:pfam00109  82 ERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLL---DEDGGPRRGSP-FAVGTMPSVIAGRIS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 152 MDCQALGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRraEDPAAASRPFDahrD 231
Cdd:pfam00109 158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA---D 232

                         250
                  ....*....|....*....
gi 2209889639 232 GFVAGEGAGVLVLERVADA 250
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 259-370 1.13e-35

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: 127.30  E-value: 1.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 259 ARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVTEAAVIRRVIGDHP-----LVT 333
Cdd:pfam02801   2 AVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkqplAIG 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2209889639 334 STKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLE 370
Cdd:pfam02801  82 SVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 144-409 5.56e-29

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: 120.11  E-value: 5.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  144 NMTAGHIAMDCQALGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGALSRRAEdpaaaS 223
Cdd:TIGR02813  183 NVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED-----I 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  224 RPFDAHRDGFVAGEGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHPTGDGAERAMRAALADACLDPAEVAH 303
Cdd:TIGR02813  258 QPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGL 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  304 VNAHGTSTPKNDVTEAAVIRRVIGD------HPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLERVDPQVE 377
Cdd:TIGR02813  338 IEAHGTGTAAGDVAEFGGLVSVFSQdndqkqHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLD 417

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2209889639  378 ID---------------VVAGAPRTATIgaamsNSFGFGGQNAAVVV 409
Cdd:TIGR02813  418 IEnspfylntetrpwmqREDGTPRRAGI-----SSFGFGGTNFHMVL 459
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 57-409 3.13e-27

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: 109.73  E-value: 3.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639   57 VEDFDPAA-ELGRRTALRMD---RvsqLGVTAARLAVSDAGLDPQVWDGARVAVVIGTSFGGSAsferehetylssgptv 132
Cdd:smart00825  30 VDLFDAAFfGISPREAEAMDpqqR---LLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDYS---------------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  133 vspqlmvtapvnMTaghiamdcqalgpnqvVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLHKMGAL 212
Cdd:smart00825  91 ------------VT----------------VDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGML 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  213 SrraedPAAASRPFDAHRDGFVAGEGAGVLVLERVADAHARGARVRARISGFGASADGFHAS--APHPTGdgaeramraa 290
Cdd:smart00825 143 S-----PDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGitAPSGPA---------- 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  291 ladacldpaevahvnahgtstpkndvteaavirrvigdHPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTANLE 370
Cdd:smart00825 208 --------------------------------------QLLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFE 249

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2209889639  371 RVDPQVEID-----VV--------AGAPRTATIgaamsNSFGFGGQNAAVVV 409
Cdd:smart00825 250 TPNPHIDLEesplrVPteltpwppPGRPRRAGV-----SSFGFGGTNAHVIL 296
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 158-409 1.09e-25

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: 104.45  E-value: 1.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 158 GPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAaltrtgmaslhkmgalsrraedpaaasrpfdahrdgFVAGE 237
Cdd:cd00327    59 GPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 238 GAGVLVLERVADAHARGARVRARISGFGASADGFHAsAPHPTGDGAERAMRAALADACLDPAEVAHVNAHGTSTPKNDVT 317
Cdd:cd00327   103 GAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 318 EAAVIRRVIGDH-PLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTAnlervdpqveidvvagaprtATIGAAMSN 396
Cdd:cd00327   182 ELALGLDPDGVRsPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTP--------------------REPRTVLLL 241

                         250
                  ....*....|...
gi 2209889639 397 SFGFGGQNAAVVV 409
Cdd:cd00327   242 GFGLGGTNAAVVL 254
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
10-392 3.25e-09

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 58.43  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  10 DVAVTGLGLITPAGTGVKANvariWDGRSTASRSPGLEgmavdfscrVEDFDP-----------AAELGRRTALR-MDRV 77
Cdd:PRK06519    7 DVVITGIGLVSSLGEGLDAH----WNALSAGRPQPNVD---------TETFAPypvhplpeidwSQQIPKRGDQRqMETW 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  78 SQLGVTAARLAVSDAGL--DPQVWDGARVAVVIGtsfGGsasfER----------------EHETYLSSG-PTVVSPQLM 138
Cdd:PRK06519   74 QRLGTYAAGLALDDAGIkgNEELLSTMDMIVAAG---GG----ERdiavdtailnearkrnDRGVLLNERlMTELRPTLF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 139 VTAPVNMTAGHIAMDCQALGPNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAAlTRTGMASLHKMGALSRRAED 218
Cdd:PRK06519  147 LAQLSNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNA-ERPDMLLLYELGGLLLKGGW 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 219 PAAASRPFDAHrDGFVAGEGAGVLVLERVADAHARGARVRARISGFGAsadgfhASAPHPTGDGAERaMRAALADACLDP 298
Cdd:PRK06519  226 APVWSRGGEDG-GGFILGSGGAFLVLESREHAEARGARPYARISGVES------DRARRAPGDLEAS-LERLLKPAGGLA 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 299 AEVAHVNAhgtSTPKNDVT--EAAVIRRVigDHPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSVPPTAnlervDPQV 376
Cdd:PRK06519  298 APTAVISG---ATGAHPATaeEKAALEAA--LAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPPF-----DASG 367

                         410
                  ....*....|....*.
gi 2209889639 377 EIDVVAGAPRTATIGA 392
Cdd:PRK06519  368 EKPMSGAAREAVVTTV 383
FabG2 COG4982
3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and ...
 218-409 1.48e-06

3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and metabolism];


Pssm-ID: 444006 [Multi-domain]  Cd Length: 3088  Bit Score: 50.84  E-value: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  218 DPAAASRPFDAHRDGFVAGEGAGVLVLERVADAHARGARVRARISGFGASADGFHASAPHP-------TGDGAERAMRAA 290
Cdd:COG4982   2787 DDRFFSRANDRRRGGFVEAQGGGTILLARGDVAAKLGLPVLGVVAFAQSFADGAHTSIPAPglgalaaARGGKDSKLARD 2866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  291 LADACLDPAEVAHVNAHGTSTPKNDVTE-------AAVIRRVIGDHPLVTSTKGVIGHLIGAAGAVEAAYTVLAVEQGSV 363
Cdd:COG4982   2867 LAKLGVTADDIAVVSKHDTSTNANDPNEselherlAHAIGRTDGNPLFVVSQKSLTGHAKGGAAAFQLIGLCQVLRSGVI 2946

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2209889639  364 PPTANLERVDPQVEID---VVAGAPR----TATIGAAMSNSFGFGGQNAAVVV 409
Cdd:COG4982   2947 PPNRSLDCVDDKLAGDdhlVWLREPLrlgaKGPLKAGLLTSLGFGHVSGLLAV 2999
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 161-294 3.01e-05

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 45.78  E-value: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 161 QVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAALTRTGMASLhkmgalsrraedpAAASRPFDAHR-DGFVAGEGA 239
Cdd:PRK06147  127 AVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHY-------------EARDRLLTSQNsNGFIPGEAA 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2209889639 240 GVLVLERVADAHARGARVRARisGFGASADGFHASAPHP-TGDGAERAMRAALADA 294
Cdd:PRK06147  194 AAVLLGRPAGGEAPGLPLLGL--GLGREPAPVGESEDLPlRGDGLTQAIRAALAEA 247
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
72-203 1.34e-04

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 43.94  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  72 LRMDrvsQLGVTAARLAVSDAGLDPQVWDgarvAVVIGTSFGGSasferehETYLSSGPTVVspqLMVTAPVNMTAGHIA 151
Cdd:PRK06445   30 IRPE---ELAAMLINRLIEKTGIKPEEID----DIITGCALQVG-------ENWLYGGRHPI---FLARLPYNIPAMAVD 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2209889639 152 MdcqalgpnqvvstACASGTTAIGIGRMLLEAGLCDVVLAGGSEaALTRTGM 203
Cdd:PRK06445   93 R-------------QCASSLTTVSIGAMEIATGMADIVIAGGVE-HMTRTPM 130
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 79-222 1.99e-04

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 43.41  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  79 QLGVTAARLAVSDAGLDPQVWDGARVAVVIGTSFGGsasferehetylssgptvvspqlmvtAPVNMTAGHIAMDCqalG 158
Cdd:cd00829    18 ELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQS--------------------------FPGALIAEYLGLLG---K 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2209889639 159 PNQVVSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAalTRTGMASLHKMGALSRRAEDPAAA 222
Cdd:cd00829    69 PATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEK--MSDVPTGDEAGGRASDLEWEGPEP 130
PRK06059 PRK06059
lipid-transfer protein; Provisional
 79-197 1.03e-03

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 40.90  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639  79 QLGVTAARLAVSDAGLDpqvWDGARVAVVIGTSFGGSASFerehetylssgptvvspqlmvtapvnmTAGhiAMDCQALG 158
Cdd:PRK06059   25 EYGVVAARAALADAGLD---WRDVQLVVGADTIRNGYPGF---------------------------VAG--ATFAQALG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2209889639 159 PNQV----VSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEAA 197
Cdd:PRK06059   73 WNGApvssSYAACASGSQALQSARAQILAGLCDVALVVGADTT 115
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 163-251 4.66e-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: 38.89  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209889639 163 VSTACASGTTAIGIGRMLLEAGLCDVVLAGGSEaALTRTGMASLHKMGALSRRAE--DPAAASRPFDAHrDGFVAGEGAg 240
Cdd:COG0183    84 VNRVCGSGLQAVALAAQAIAAGDADVVIAGGVE-SMSRAPMLLPKARWGYRMNAKlvDPMINPGLTDPY-TGLSMGETA- 160

                          90
                  ....*....|.
gi 2209889639 241 vlvlERVADAH 251
Cdd:COG0183   161 ----ENVAERY 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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