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Conserved domains on  [gi|1443441168|emb|SUW23399|]
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3-oxoacyl-ACP synthase [Brucella abortus]

Protein Classification

beta-ketoacyl-ACP synthase I( domain architecture ID 11483011)

beta-ketoacyl-ACP synthase I catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP

CATH:  3.40.47.10
EC:  2.3.1.41
Gene Ontology:  GO:0004315|GO:0006633
PubMed:  11286890|11969206

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
1-407 0e+00

beta-ketoacyl-ACP synthase I;


:

Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 842.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGAPDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:PRK07967    1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAME 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITRE-KGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSISS 159
Cdd:PRK07967   81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGpRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 160 ACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVLFDAMGAMSSKYNDTPSTASRAYDKNRDGFVIAGGAGVLVLE 239
Cdd:PRK07967  161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVVE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 240 DLETALARGAKIYGEIVGYGATSDGYDMVAPSGEGAIRCMKMALSTVTSKIDYINPHATSTPAGDAPEIEAIRQIFgaGD 319
Cdd:PRK07967  241 ELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATVDTPIDYINTHGTSTPVGDVKELGAIREVF--GD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 320 VCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFADMPIVRKRIDNVQLNTVLSNSFGFGGTNAT 399
Cdd:PRK07967  319 KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSNSFGFGGTNAT 398


                  ....*...
gi 1443441168 400 LVFQRYQG 407
Cdd:PRK07967  399 LVFRRYKG 406
 
Name Accession Description Interval E-value
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
1-407 0e+00

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 842.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGAPDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:PRK07967    1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAME 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITRE-KGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSISS 159
Cdd:PRK07967   81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGpRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 160 ACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVLFDAMGAMSSKYNDTPSTASRAYDKNRDGFVIAGGAGVLVLE 239
Cdd:PRK07967  161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVVE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 240 DLETALARGAKIYGEIVGYGATSDGYDMVAPSGEGAIRCMKMALSTVTSKIDYINPHATSTPAGDAPEIEAIRQIFgaGD 319
Cdd:PRK07967  241 ELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATVDTPIDYINTHGTSTPVGDVKELGAIREVF--GD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 320 VCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFADMPIVRKRIDNVQLNTVLSNSFGFGGTNAT 399
Cdd:PRK07967  319 KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSNSFGFGGTNAT 398


                  ....*...
gi 1443441168 400 LVFQRYQG 407
Cdd:PRK07967  399 LVFRRYKG 406
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 2-405 0e+00

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 558.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG-APDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:COG0304     1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGeVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSISSA 160
Cdd:COG0304    81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 161 CATSNHCIGNAYEMIQYGKQDRMFAGGCE-DLDWTLSVLFDAMGAMSSKyNDTPSTASRAYDKNRDGFVIAGGAGVLVLE 239
Cdd:COG0304   161 CASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 240 DLETALARGAKIYGEIVGYGATSDGYDMVA--PSGEGAIRCMKMALSTV---TSKIDYINPHATSTPAGDAPEIEAIRQI 314
Cdd:COG0304   240 ELEHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALKDAglsPEDIDYINAHGTSTPLGDAAETKAIKRV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 315 FGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFaDMPIVRKRIDNVQLNTVLSNSFGFG 394
Cdd:COG0304   320 FGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPEC-DLDYVPNEAREAKIDYALSNSFGFG 398

                         410
                  ....*....|.
gi 1443441168 395 GTNATLVFQRY 405
Cdd:COG0304   399 GHNASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 2-402 4.81e-175

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: 494.36  E-value: 4.81e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG-APDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:cd00834     1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGeVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSISSA 160
Cdd:cd00834    81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 161 CATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKYNDtPSTASRAYDKNRDGFVIAGGAGVLVLE 239
Cdd:cd00834   161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAgFAALRALSTRNDD-PEKASRPFDKDRDGFVLGEGAGVLVLE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 240 DLETALARGAKIYGEIVGYGATSDGYDMVAPS--GEGAIRCMKMAL--STVT-SKIDYINPHATSTPAGDAPEIEAIRQI 314
Cdd:cd00834   240 SLEHAKARGAKIYAEILGYGASSDAYHITAPDpdGEGAARAMRAALadAGLSpEDIDYINAHGTSTPLNDAAESKAIKRV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 315 FGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFaDMPIVRKRIDNVQLNTVLSNSFGFG 394
Cdd:cd00834   320 FGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPEC-DLDYVPNEAREAPIRYALSNSFGFG 398


                  ....*...
gi 1443441168 395 GTNATLVF 402
Cdd:cd00834   399 GHNASLVF 406
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 2-402 9.52e-142

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: 409.57  E-value: 9.52e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGA-PDIDIESLVD----RRAMRFHGRGTAwnh 76
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEvKDFDPEDYIDkkeaRRMDRFIQYALA--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  77 iAMDQAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYS 156
Cdd:TIGR03150  78 -AAKEAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 157 ISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSsKYNDTPSTASRAYDKNRDGFVIAGGAGV 235
Cdd:TIGR03150 157 VVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAgFAAMKALS-TRNDDPEKASRPFDKDRDGFVMGEGAGV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 236 LVLEDLETALARGAKIYGEIVGYGATSDGYDMVAPS--GEGAIRCMKMALSTV---TSKIDYINPHATSTPAGDAPEIEA 310
Cdd:TIGR03150 236 LVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPApeGEGAARAMRAALKDAginPEDVDYINAHGTSTPLGDKAETKA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 311 IRQIFGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAfADMPIVRKRIDNVQLNTVLSNS 390
Cdd:TIGR03150 316 IKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPE-CDLDYVPNEAREAKIDYALSNS 394

                         410
                  ....*....|..
gi 1443441168 391 FGFGGTNATLVF 402
Cdd:TIGR03150 395 FGFGGTNASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 2-244 2.02e-37

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: 136.23  E-value: 2.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAelgFRCQVHGAPDIDIESLVDRRAMRFHGRGTAWNHI---- 77
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADR---WDPDKLYDPPSRIAGKIYTKWGGLDDIFDFDPLFfgis 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  78 -----AMD-----------QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADitrEKGPKRVGPFAVPkAMSSTAS 141
Cdd:pfam00109  78 preaeRMDpqqrllleaawEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDE---DGGPRRGSPFAVG-TMPSVIA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 142 ATLATFFKIKGINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCE-DLDWTLSVLFDAMGAMSSkynDTPSTASRAY 220
Cdd:pfam00109 154 GRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSP---DGPCKAFDPF 230

                         250       260
                  ....*....|....*....|....
gi 1443441168 221 DknrDGFVIAGGAGVLVLEDLETA 244
Cdd:pfam00109 231 A---DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 72-401 1.55e-15

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: 76.60  E-value: 1.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   72 TAWnhiamdQAIADAGLTEEEVSNERTGIIMGsggpstrtivdsaditrekgpkrvgpfavpkAMSSTASATLATffkik 151
Cdd:smart00825  58 VAW------EALEDAGIDPESLRGSRTGVFVG-------------------------------VSSSDYSVTVDT----- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  152 ginysissACATSNHCIGNAYEMIQYGKQDRMFAGGCE-DLDWTLSVLFDAMGAMSskyndtPSTASRAYDKNRDGFVIA 230
Cdd:smart00825  96 --------ACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  231 GGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYD--MVAPSGEGaircmkmalstvtskidyinphatstpagdapei 308
Cdd:smart00825 162 EGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGPA---------------------------------- 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  309 eairQIfgagdvcpPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDP--AFADMPIV------------ 374
Cdd:smart00825 208 ----QL--------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPhiDLEESPLRvpteltpwpppg 275

                          330       340
                   ....*....|....*....|....*..
gi 1443441168  375 RKRIDNVqlntvlsNSFGFGGTNATLV 401
Cdd:smart00825 276 RPRRAGV-------SSFGFGGTNAHVI 295
 
Name Accession Description Interval E-value
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
1-407 0e+00

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 842.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGAPDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:PRK07967    1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAME 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITRE-KGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSISS 159
Cdd:PRK07967   81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGpRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 160 ACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVLFDAMGAMSSKYNDTPSTASRAYDKNRDGFVIAGGAGVLVLE 239
Cdd:PRK07967  161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVVE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 240 DLETALARGAKIYGEIVGYGATSDGYDMVAPSGEGAIRCMKMALSTVTSKIDYINPHATSTPAGDAPEIEAIRQIFgaGD 319
Cdd:PRK07967  241 ELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATVDTPIDYINTHGTSTPVGDVKELGAIREVF--GD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 320 VCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFADMPIVRKRIDNVQLNTVLSNSFGFGGTNAT 399
Cdd:PRK07967  319 KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSNSFGFGGTNAT 398


                  ....*...
gi 1443441168 400 LVFQRYQG 407
Cdd:PRK07967  399 LVFRRYKG 406
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 2-405 0e+00

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 558.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG-APDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:COG0304     1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGeVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSISSA 160
Cdd:COG0304    81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 161 CATSNHCIGNAYEMIQYGKQDRMFAGGCE-DLDWTLSVLFDAMGAMSSKyNDTPSTASRAYDKNRDGFVIAGGAGVLVLE 239
Cdd:COG0304   161 CASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 240 DLETALARGAKIYGEIVGYGATSDGYDMVA--PSGEGAIRCMKMALSTV---TSKIDYINPHATSTPAGDAPEIEAIRQI 314
Cdd:COG0304   240 ELEHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALKDAglsPEDIDYINAHGTSTPLGDAAETKAIKRV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 315 FGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFaDMPIVRKRIDNVQLNTVLSNSFGFG 394
Cdd:COG0304   320 FGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPEC-DLDYVPNEAREAKIDYALSNSFGFG 398

                         410
                  ....*....|.
gi 1443441168 395 GTNATLVFQRY 405
Cdd:COG0304   399 GHNASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 2-402 4.81e-175

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: 494.36  E-value: 4.81e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG-APDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:cd00834     1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGeVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSISSA 160
Cdd:cd00834    81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 161 CATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKYNDtPSTASRAYDKNRDGFVIAGGAGVLVLE 239
Cdd:cd00834   161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAgFAALRALSTRNDD-PEKASRPFDKDRDGFVLGEGAGVLVLE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 240 DLETALARGAKIYGEIVGYGATSDGYDMVAPS--GEGAIRCMKMAL--STVT-SKIDYINPHATSTPAGDAPEIEAIRQI 314
Cdd:cd00834   240 SLEHAKARGAKIYAEILGYGASSDAYHITAPDpdGEGAARAMRAALadAGLSpEDIDYINAHGTSTPLNDAAESKAIKRV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 315 FGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFaDMPIVRKRIDNVQLNTVLSNSFGFG 394
Cdd:cd00834   320 FGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPEC-DLDYVPNEAREAPIRYALSNSFGFG 398


                  ....*...
gi 1443441168 395 GTNATLVF 402
Cdd:cd00834   399 GHNASLVF 406
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 2-402 9.52e-142

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: 409.57  E-value: 9.52e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGA-PDIDIESLVD----RRAMRFHGRGTAwnh 76
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEvKDFDPEDYIDkkeaRRMDRFIQYALA--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  77 iAMDQAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYS 156
Cdd:TIGR03150  78 -AAKEAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 157 ISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSsKYNDTPSTASRAYDKNRDGFVIAGGAGV 235
Cdd:TIGR03150 157 VVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAgFAAMKALS-TRNDDPEKASRPFDKDRDGFVMGEGAGV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 236 LVLEDLETALARGAKIYGEIVGYGATSDGYDMVAPS--GEGAIRCMKMALSTV---TSKIDYINPHATSTPAGDAPEIEA 310
Cdd:TIGR03150 236 LVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPApeGEGAARAMRAALKDAginPEDVDYINAHGTSTPLGDKAETKA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 311 IRQIFGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAfADMPIVRKRIDNVQLNTVLSNS 390
Cdd:TIGR03150 316 IKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPE-CDLDYVPNEAREAKIDYALSNS 394

                         410
                  ....*....|..
gi 1443441168 391 FGFGGTNATLVF 402
Cdd:TIGR03150 395 FGFGGTNASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
1-406 1.73e-141

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 409.18  E-value: 1.73e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG-APDIDIESLVDRRAMRfhgRGTAWNHIAM 79
Cdd:PRK07314    1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGeVKDFNPDDYMSRKEAR---RMDRFIQYGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  80 ---DQAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYS 156
Cdd:PRK07314   78 aaaKQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 157 ISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKyNDTPSTASRAYDKNRDGFVIAGGAGV 235
Cdd:PRK07314  158 IVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAgFAAARALSTR-NDDPERASRPFDKDRDGFVMGEGAGI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 236 LVLEDLETALARGAKIYGEIVGYGATSDGYDMVAPS--GEGAIRCMKMALSTV---TSKIDYINPHATSTPAGDAPEIEA 310
Cdd:PRK07314  237 LVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPApdGEGAARAMKLALKDAginPEDIDYINAHGTSTPAGDKAETQA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 311 IRQIFGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAfADMPIVRKRIDNVQLNTVLSNS 390
Cdd:PRK07314  317 IKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEE-CDLDYVPNEARERKIDYALSNS 395

                         410
                  ....*....|....*.
gi 1443441168 391 FGFGGTNATLVFQRYQ 406
Cdd:PRK07314  396 FGFGGTNASLVFKRYE 411
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-407 1.74e-115

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 343.52  E-value: 1.74e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG-APDI--------DIESLVDRRAMRFHGRG 71
Cdd:PRK06333    3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGqVPDLaedaeagfDPDRYLDPKDQRKMDRF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  72 TAWNHIAMDQAIADAGLTEEEVSN-ERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKI 150
Cdd:PRK06333   83 ILFAMAAAKEALAQAGWDPDTLEDrERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 151 KGINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKYNDTPSTASRAYDKNRDGFVI 229
Cdd:PRK06333  163 KGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAgFAAARALSTRFNDAPEQASRPFDRDRDGFVM 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 230 AGGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYDMVAP--SGEGAIRCMKMALSTV---TSKIDYINPHATSTPAGD 304
Cdd:PRK06333  243 GEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGpeDGEGARRAMLIALRQAgipPEEVQHLNAHATSTPVGD 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 305 APEIEAIRQIFGAGDvCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFADMPIVRKRIDNVQLN 384
Cdd:PRK06333  323 LGEVAAIKKVFGHVS-GLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVANKARPMDMD 401

                         410       420
                  ....*....|....*....|...
gi 1443441168 385 TVLSNSFGFGGTNATLVFQRYQG 407
Cdd:PRK06333  402 YALSNGFGFGGVNASILFRRWEP 424
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 11-405 9.09e-112

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 333.97  E-value: 9.09e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  11 IVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGAPDIDIESLV-------------DRRAMRFHGRGTAWNHI 77
Cdd:PTZ00050    1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAMpcqiaaevdqsefDPSDFAPTKRESRATHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  78 AM---DQAIADAGLTE-EEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGI 153
Cdd:PTZ00050   81 AMaaaREALADAKLDIlSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 154 NYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKYNDTPSTASRAYDKNRDGFVIAGG 232
Cdd:PTZ00050  161 SGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAgFSRMRALCTKYNDDPQRASRPFDKDRAGFVMGEG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 233 AGVLVLEDLETALARGAKIYGEIVGYGATSDGYDMVAP--SGEGAIRCMKMALSTV----TSKIDYINPHATSTPAGDAP 306
Cdd:PTZ00050  241 AGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPhpDGRGARRCMENALKDGaninINDVDYVNAHATSTPIGDKI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 307 EIEAIRQIFGaGDVCPP--IAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDP-AFADMPIVRKRIDNVQL 383
Cdd:PTZ00050  321 ELKAIKKVFG-DSGAPKlyVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAeCDLNLVQGKTAHPLQSI 399

                         410       420
                  ....*....|....*....|..
gi 1443441168 384 NTVLSNSFGFGGTNATLVFQRY 405
Cdd:PTZ00050  400 DAVLSTSFGFGGVNTALLFTKY 421
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 1-405 2.23e-108

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 324.76  E-value: 2.23e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG-APDIDIESLVD----RRAMRFHGRGTAwn 75
Cdd:PRK08439    1 MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGeITDFDPTEVMDpkevKKADRFIQLGLK-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  76 hiAMDQAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINY 155
Cdd:PRK08439   79 --AAREAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 156 SISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKyNDTPSTASRAYDKNRDGFVIAGGAG 234
Cdd:PRK08439  157 SSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGgFAAMKALSTR-NDDPKKASRPFDKDRDGFVMGEGAG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 235 VLVLEDLETALARGAKIYGEIVGYGATSDGYDMVAPSGEGAIRCMKMALSTVTS-KIDYINPHATSTPAGDAPEIEAIRQ 313
Cdd:PRK08439  236 ALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAGNpKIDYINAHGTSTPYNDKNETAALKE 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 314 IFGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAfADMPIVRKRIDNVQLNTVLSNSFGF 393
Cdd:PRK08439  316 LFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPE-CDLDYIPNVARKAELNVVMSNSFGF 394

                         410
                  ....*....|..
gi 1443441168 394 GGTNATLVFQRY 405
Cdd:PRK08439  395 GGTNGVVIFKKV 406
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
1-402 1.05e-99

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 302.68  E-value: 1.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEE---YAELGFRCqvhGAP--DIDIESLVDRRAMRFHGRGTAWN 75
Cdd:PRK09116    1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEwdrYDGLNTRL---AAPidDFELPAHYTRKKIRSMGRVSLMA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  76 HIAMDQAIADAGLTEEEV-SNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGIN 154
Cdd:PRK09116   78 TRASELALEDAGLLGDPIlTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 155 YSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVLFDAMGAMSSKyNDTPSTASRAYDKNRDGFVIAGGAG 234
Cdd:PRK09116  158 IPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTR-NDAPELTPRPFDANRDGLVIGEGAG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 235 VLVLEDLETALARGAKIYGEIVGYGATSDGYDMVAPSGEGAIRCMKMALSTVT---SKIDYINPHATSTPAGDAPEIEAI 311
Cdd:PRK09116  237 TLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGlapEDIGYVNAHGTATDRGDIAESQAT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 312 RQIFGAGdvcPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFADMPIVRKRIDNVQLNTVLSNSF 391
Cdd:PRK09116  317 AAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMSNNF 393

                         410
                  ....*....|.
gi 1443441168 392 GFGGTNATLVF 402
Cdd:PRK09116  394 AFGGINTSLIF 404
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 2-402 6.13e-99

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 301.71  E-value: 6.13e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGIS--RAEEYAELGFR------------CQVHGA-------PDIDIESLV 60
Cdd:PLN02836    6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRalTQDDLKMKSEDeetqlytldqlpSRVAALvprgtgpGDFDEELWL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  61 -DRRAMRFhgrgTAWNHIAMDQAIADA--GLTEEEVSnERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMS 137
Cdd:PLN02836   86 nSRSSSRF----IGYALCAADEALSDArwLPSEDEAK-ERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 138 STASATLATFFKIKGINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKYNDTPSTA 216
Cdd:PLN02836  161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAgFSRSRALSTKFNSCPTEA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 217 SRAYDKNRDGFVIAGGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYDMVAPS--GEGAIRCMKMALSTV---TSKID 291
Cdd:PLN02836  241 SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHedGRGAVLAMTRALQQSglhPNQVD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 292 YINPHATSTPAGDAPEIEAIRQIFGAGDVCPPIA--ATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFA 369
Cdd:PLN02836  321 YVNAHATSTPLGDAVEARAIKTVFSEHATSGGLAfsSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFD 400

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1443441168 370 D--MPIVRKRIDNVQlnTVLSNSFGFGGTNATLVF 402
Cdd:PLN02836  401 DgfVPLTASKAMLIR--AALSNSFGFGGTNASLLF 433
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
2-404 6.25e-82

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 257.24  E-value: 6.25e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG-APDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:PRK08722    4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGlVKDFNCEEYMSKKDARKMDLFIQYGIAAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSISSA 160
Cdd:PRK08722   84 QALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 161 CATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKyNDTPSTASRAYDKNRDGFVIAGGAGVLVLE 239
Cdd:PRK08722  164 CTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAgFGAAKALSTR-NDEPQKASRPWDKDRDGFVLGDGAGMMVLE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 240 DLETALARGAKIYGEIVGYGATSDGYDMVAPS--GEGAIRCMKMAL---STVTSKIDYINPHATSTPAGDAPEIEAIRQI 314
Cdd:PRK08722  243 EYEHAKARGAKIYAELVGFGMSGDAYHMTSPSedGSGGALAMEAAMrdaGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRA 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 315 FG-AGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFaDMPIVRKRIDNVQ-LNTVLSNSFG 392
Cdd:PRK08722  323 LGeAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGL-DIDLVPHTARKVEsMEYAICNSFG 401

                         410
                  ....*....|..
gi 1443441168 393 FGGTNATLVFQR 404
Cdd:PRK08722  402 FGGTNGSLIFKK 413
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-401 3.30e-81

"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: 255.06  E-value: 3.30e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNT---EEVTASLREAKSGISraeEYAELGFRCQVHGAPDIDIESLVDRRA--MRFHGRGTAWNH 76
Cdd:cd00828     1 SRVVITGIGVVSPHGEGCdevEEFWEALREGRSGIA---PVARLKSRFDRGVAGQIPTGDIPGWDAkrTGIVDRTTLLAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  77 IAMDQAIADAGLT-EEEVSNERTGIIMGSGGPSTRtivdSADITREKGPKRVGPFAVPKAM--SSTASATLATFFKIK-G 152
Cdd:cd00828    78 VATEEALADAGITdPYEVHPSEVGVVVGSGMGGLR----FLRRGGKLDARAVNPYVSPKWMlsPNTVAGWVNILLLSShG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 153 INYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVLFDAMGAMSSKYNDtPSTASRAYDKNRDGFVIAGG 232
Cdd:cd00828   154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAEEE-PEEMSRPFDETRDGFVEAEG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 233 AGVLVLEDLETALARGAKIYGEIVGYGATSDGYDMVAPS-GEGAIRCMKMALSTVTS---KIDYINPHATSTPAGDAPEI 308
Cdd:cd00828   233 AGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAgGKGIARAIRTALAKAGLsldDLDVISAHGTSTPANDVAES 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 309 EAIRQIFGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFADMPIVRK-RIDNVQLNTVL 387
Cdd:cd00828   313 RAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLsRDLNLKVRAAL 392

                         410
                  ....*....|....
gi 1443441168 388 SNSFGFGGTNATLV 401
Cdd:cd00828   393 VNAFGFGGSNAALV 406
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 78-401 2.90e-78

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: 245.24  E-value: 2.90e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  78 AMDQAIADAGLTEEEVSNERTGIIMGSGGPStrtivDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSI 157
Cdd:cd00825    18 AAERAIADAGLSREYQKNPIVGVVVGTGGGS-----PRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAYDV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 158 SSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVLFDAMGAMSskyndTPSTASRAYDKNRDGFVIAGGAGVLV 237
Cdd:cd00825    93 SAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALS-----TPEKASRTFDAAADGFVFGDGAGALV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 238 LEDLETALARGAKIYGEIVGYGATSDGYDMV--APSGEGAIRCMKMALS---TVTSKIDYINPHATSTPAGDAPEIEAIR 312
Cdd:cd00825   168 VEELEHALARGAHIYAEIVGTAATIDGAGMGafAPSAEGLARAAKEALAvagLTVWDIDYLVAHGTGTPIGDVKELKLLR 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 313 QIFgaGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAfADMPIVRKRIDnvQLNTVLSNSFG 392
Cdd:cd00825   248 SEF--GDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEA-GLNIVTETTPR--ELRTALLNGFG 322


                  ....*....
gi 1443441168 393 FGGTNATLV 401
Cdd:cd00825   323 LGGTNATLV 331
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 2-406 1.22e-77

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 249.90  E-value: 1.22e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGA-PDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:PLN02787  129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEiKSFSTDGWVAPKLSKRMDKFMLYLLTAGK 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEE---EVSNERTGIIMGSGGPSTRTIVDSADITReKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSI 157
Cdd:PLN02787  209 KALADGGITEDvmkELDKTKCGVLIGSAMGGMKVFNDAIEALR-ISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSI 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 158 SSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKyNDTPSTASRAYDKNRDGFVIAGGAGVL 236
Cdd:PLN02787  288 STACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGgFVACRALSQR-NDDPTKASRPWDMNRDGFVMGEGAGVL 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 237 VLEDLETALARGAKIYGEIVGYGATSDGYDMVAPSGEGA--IRCMKMALS---TVTSKIDYINPHATSTPAGDAPEIEAI 311
Cdd:PLN02787  367 LLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAgvILCIEKALAqsgVSKEDVNYINAHATSTKAGDLKEYQAL 446

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 312 RQIFGaGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFADMPIVRKRIDNVQLNTVLSNSF 391
Cdd:PLN02787  447 MRCFG-QNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIKVALSNSF 525

                         410
                  ....*....|....*
gi 1443441168 392 GFGGTNATLVFQRYQ 406
Cdd:PLN02787  526 GFGGHNSSILFAPYK 540
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
4-405 2.30e-72

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 232.70  E-value: 2.30e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   4 VVVTGMGIVSSIGSNTEEVTASLREAKSGISR-----AEEYaELGFRCQVHGAPDIDIE-SLVDRRAMRFHGRGTAwnhI 77
Cdd:PRK07910   14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTlddpfVEEF-DLPVRIGGHLLEEFDHQlTRVELRRMSYLQRMST---V 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  78 AMDQAIADAGltEEEVSNERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKIKGINYSI 157
Cdd:PRK07910   90 LGRRVWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 158 SSACATSNHCIGNAYEMIQYGKQDRMFAGGCED-LDWTLSVLFDAMGAMSSKYNDTPSTASRAYDKNRDGFVIAGGAGVL 236
Cdd:PRK07910  168 VSACASGSEAIAQAWRQIVLGEADIAICGGVETrIEAVPIAGFAQMRIVMSTNNDDPAGACRPFDKDRDGFVFGEGGALM 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 237 VLEDLETALARGAKIYGEIVGYGATSDGYDMVA--PSGEGAIRCMKMALSTV---TSKIDYINPHATSTPAGDAPEIEAI 311
Cdd:PRK07910  248 VIETEEHAKARGANILARIMGASITSDGFHMVApdPNGERAGHAMTRAIELAgltPGDIDHVNAHATGTSVGDVAEGKAI 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 312 RQIFGAGDvcPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFaDMPIVRKRIDNVQLNTVLSNSF 391
Cdd:PRK07910  328 NNALGGHR--PAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEI-DLDVVAGEPRPGNYRYAINNSF 404

                         410
                  ....*....|....
gi 1443441168 392 GFGGTNATLVFQRY 405
Cdd:PRK07910  405 GFGGHNVALAFGRY 418
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 1-404 2.45e-71

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 229.53  E-value: 2.45e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGA---------PDIDIESLVDRRAMR---FH 68
Cdd:PRK07103    1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAGAGLasafigaelDSLALPERLDAKLLRrasLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  69 GRGTAwnhIAMDQAIADAGLteEEVSNERTGIIMGSGGPSTRTIVDSADITREKgPKRVGPFAVPKAMSSTASATLATFF 148
Cdd:PRK07103   81 AQAAL---AAAREAWRDAAL--GPVDPDRIGLVVGGSNLQQREQALVHETYRDR-PAFLRPSYGLSFMDTDLVGLCSEQF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 149 KIKGINYSISSACATSNHCIGNAYEMIQYGKQDRMFA-GGCEDLDWTLSVLFDAMGAM-SSKYNDTPSTASRAYDKNRDG 226
Cdd:PRK07103  155 GIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAvGALMDLSYWECQALRSLGAMgSDRFADEPEAACRPFDQDRDG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 227 FVIAGGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYDMVAPSGEGAIRCMKMALSTV---TSKIDYINPHATSTPAG 303
Cdd:PRK07103  235 FIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALRRAglgPEDIDYVNPHGTGSPLG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 304 DAPEIEAirqIFGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEE-LDPAFAdmpIVRKRIDNVQ 382
Cdd:PRK07103  315 DETELAA---LFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEpIDERFR---WVGSTAESAR 388

                         410       420
                  ....*....|....*....|..
gi 1443441168 383 LNTVLSNSFGFGGTNATLVFQR 404
Cdd:PRK07103  389 IRYALSLSFGFGGINTALVLER 410
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 69-405 2.50e-71

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 227.69  E-value: 2.50e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  69 GRGTAWNHIAMDQAIADAGLTEEEvsnERTGIIMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFF 148
Cdd:PRK14691    2 GRWWRYKWITFHPSLTHADNTEKQ---ERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 149 KIKGINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSSKYNDTPSTASRAYDKNRDGF 227
Cdd:PRK14691   79 HFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAgFAAARALSTHFNSTPEKASRPFDTARDGF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 228 VIAGGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYDMV--APSGEGAIRCMKMAL---STVTSKIDYINPHATSTPA 302
Cdd:PRK14691  159 VMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTsgAEDGDGAYRAMKIALrqaGITPEQVQHLNAHATSTPV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 303 GDAPEIEAIRQIFGAGDVCpPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFADMPIVRKRIDNVQ 382
Cdd:PRK14691  239 GDLGEINAIKHLFGESNAL-AITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHD 317

                         330       340
                  ....*....|....*....|...
gi 1443441168 383 LNTVLSNSFGFGGTNATLVFQRY 405
Cdd:PRK14691  318 MTYALSNGFGFAGVNASILLKRW 340
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
4-407 4.78e-66

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 216.42  E-value: 4.78e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   4 VVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGAPD-IDIESLVDRramrfhGRGTAWNHIAMDQA 82
Cdd:PRK06501   13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDfLPESPFGAS------ALSEALARLAAEEA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  83 IADAGL---------------TEEEVSNERTgiIMGSGGPSTrtIVDSADITREKGPKRVGPFAvPKAMSSTASATLATF 147
Cdd:PRK06501   87 LAQAGIgkgdfpgplflaappVELEWPARFA--LAAAVGDND--APSYDRLLRAARGGRFDALH-ERFQFGSIADRLADR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 148 FKIKGINYSISSACATSNHCIGNAYEMIQYGKQDRMFaggCEDLDWTLS----VLFDAMGAMSSKyNDTPSTASRAYDKN 223
Cdd:PRK06501  162 FGTRGLPISLSTACASGATAIQLGVEAIRRGETDRAL---CIATDGSVSaealIRFSLLSALSTQ-NDPPEKASKPFSKD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 224 RDGFVIAGGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYDMV--APSGEGAIRCMKMALS---TVTSKIDYINPHAT 298
Cdd:PRK06501  238 RDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTrsSPDGSPAIGAIRAALAdagLTPEQIDYINAHGT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 299 STPAGDAPEIEAIRQIFGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFAdMPIVRKRI 378
Cdd:PRK06501  318 STPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIP-LDVVPNVA 396

                         410       420
                  ....*....|....*....|....*....
gi 1443441168 379 DNVQLNTVLSNSFGFGGTNATLVFQRYQG 407
Cdd:PRK06501  397 RDARVTAVLSNSFGFGGQNASLVLTAEPA 425
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
1-404 8.53e-58

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 193.34  E-value: 8.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGsNTEEVTASLREAKSGISRAEEYAEL-GFRCQVHGAPDIDIESLVDrramrfhgrgtawnhIAM 79
Cdd:PRK05952    1 MMKVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQPFPELpPLPLGLIGNQPSSLEDLTK---------------TVV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  80 DQAIADAGLTEEEVSnerTGIIMGSggpsTRTIVDSADITREKGPKRVGPFAVPKAMSS-------TASATLATFFKIKG 152
Cdd:PRK05952   65 TAALKDAGLTPPLTD---CGVVIGS----SRGCQGQWEKLARQMYQGDDSPDEELDLENwldtlphQAAIAAARQIGTQG 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 153 INYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVL-FDAMGAMSskyndtpstASRAY--DKNRDGFVI 229
Cdd:PRK05952  138 PVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAgFQQMGALA---------KTGAYpfDRQREGLVL 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 230 AGGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYDMVAPSGEG--AIRCMKMAL--STVT-SKIDYINPHATSTPAGD 304
Cdd:PRK05952  209 GEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGksAIAAIQQCLarSGLTpEDIDYIHAHGTATRLND 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 305 APEIEAIRQIFGAGdvcPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEEldPAFaDMPIVRKRiDNVQLN 384
Cdd:PRK05952  289 QREANLIQALFPHR---VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEF-DLNFVRQA-QQSPLQ 361

                         410       420
                  ....*....|....*....|
gi 1443441168 385 TVLSNSFGFGGTNATLVFQR 404
Cdd:PRK05952  362 NVLCLSFGFGGQNAAIALGK 381
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
1-404 4.06e-55

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 186.97  E-value: 4.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   1 MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHGAPDIDIESLVDRRAmRFHGRG-----TAWN 75
Cdd:PRK09185    1 MTPVYISAFGATSALGRGLDAILAALRAGRASGMRPCDFWLVDLPTWVGEVVGVELPALPAALA-AFDCRNnrlalLALQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  76 HI--AMDQAIADAGlteeevsNERTGIIMGSggpSTRTIVDSADITREKGPKRVG---PFAVPKAMSSTASATLATFFKI 150
Cdd:PRK09185   80 QIepAVEAAIARYG-------ADRIGVVLGT---STSGILEGELAYRRRDPAHGAlpaDYHYAQQELGSLADFLRAYLGL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 151 KGINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLdwTLSVL--FDAMGAMSSkyndtpsTASRAYDKNRDGFV 228
Cdd:PRK09185  150 SGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSL--CRLTLngFNSLESLSP-------QPCRPFSANRDGIN 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 229 IAGGAGVLVLEDLETALARgakiygeIVGYGATSDGYDMVAP--SGEGAIRCMKMALSTV---TSKIDYINPHATSTPAG 303
Cdd:PRK09185  221 IGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPhpEGLGAILAMQQALADAglaPADIGYINLHGTATPLN 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 304 DAPEIEAIRQIFGAGdvcPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFADMPIVRKRiDNVQL 383
Cdd:PRK09185  294 DAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENA-QALAI 369

                         410       420
                  ....*....|....*....|.
gi 1443441168 384 NTVLSNSFGFGGTNATLVFQR 404
Cdd:PRK09185  370 RYVLSNSFAFGGNNCSLIFGR 390
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 72-401 2.56e-53

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: 182.76  E-value: 2.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  72 TAWnhiamdQAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDsaditreKGPKRVGPFAVPKAMSSTASATLATFFKIK 151
Cdd:cd00833    94 VAW------EALEDAGYSPESLAGSRTGVFVGASSSDYLELLA-------RDPDEIDAYAATGTSRAFLANRISYFFDLR 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 152 GINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCE-DLDWTLSVLFDAMGAMSskyndtPSTASRAYDKNRDGFVIA 230
Cdd:cd00833   161 GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNlILSPDMFVGFSKAGMLS------PDGRCRPFDADADGYVRG 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 231 GGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYD--MVAPSGEGAIRCMKMALSTVT---SKIDYINPHATSTPAGDA 305
Cdd:cd00833   235 EGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTkgITAPSGEAQAALIRRAYARAGvdpSDIDYVEAHGTGTPLGDP 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 306 PEIEAIRQIFGAGDVCPP---IAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPA--FADMP--IVRKRI 378
Cdd:cd00833   315 IEVEALAKVFGGSRSADQpllIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKidFEESPlrVPTEAR 394

                         330       340
                  ....*....|....*....|....*.
gi 1443441168 379 DNVQLNTVLS---NSFGFGGTNATLV 401
Cdd:cd00833   395 PWPAPAGPRRagvSSFGFGGTNAHVI 420
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 78-401 2.60e-42

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: 149.13  E-value: 2.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  78 AMDQAIADAGLTeeevSNERTGIIMGSGGPSTRtivdsaditrekgpkrvgpfavpkamSSTASATLATFFKIKGI-NYS 156
Cdd:cd00327    14 AAEQAIADAGLS----KGPIVGVIVGTTGGSGE--------------------------FSGAAGQLAYHLGISGGpAYS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 157 ISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDldwtlsvlfdamgamsskyndtpstasraydknrdgFVIAGGAGVL 236
Cdd:cd00327    64 VNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGDGAAAA 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 237 VLEDLETALARGAKIYGEIVGYGATSDGYDMV-APSGEGAIRCMKMALSTV---TSKIDYINPHATSTPAGDAPEIEAIR 312
Cdd:cd00327   108 VVESEEHALRRGAHPQAEIVSTAATFDGASMVpAVSGEGLARAARKALEGAgltPSDIDYVEAHGTGTPIGDAVELALGL 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 313 QIFGAGDvcPPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFIceSAHIEELDpafadmpivrkridnvqlnTVLSNSFG 392
Cdd:cd00327   188 DPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFI--PPTPREPR-------------------TVLLLGFG 244


                  ....*....
gi 1443441168 393 FGGTNATLV 401
Cdd:cd00327   245 LGGTNAAVV 253
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 2-244 2.02e-37

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: 136.23  E-value: 2.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAelgFRCQVHGAPDIDIESLVDRRAMRFHGRGTAWNHI---- 77
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADR---WDPDKLYDPPSRIAGKIYTKWGGLDDIFDFDPLFfgis 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  78 -----AMD-----------QAIADAGLTEEEVSNERTGIIMGSGGPSTRTIVDSADitrEKGPKRVGPFAVPkAMSSTAS 141
Cdd:pfam00109  78 preaeRMDpqqrllleaawEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDE---DGGPRRGSPFAVG-TMPSVIA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 142 ATLATFFKIKGINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCE-DLDWTLSVLFDAMGAMSSkynDTPSTASRAY 220
Cdd:pfam00109 154 GRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSP---DGPCKAFDPF 230

                         250       260
                  ....*....|....*....|....
gi 1443441168 221 DknrDGFVIAGGAGVLVLEDLETA 244
Cdd:pfam00109 231 A---DGFVRGEGVGAVVLKRLSDA 251
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 72-398 1.23e-33

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 133.46  E-value: 1.23e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   72 TAWnhiamdQAIADAGLTEEEVSNERTGIIMGSGGpstrtiVDSADITREkGPKRVGPFAVPKAMSSTASATLATFFKIK 151
Cdd:COG3321     98 VAW------EALEDAGYDPESLAGSRTGVFVGASS------NDYALLLLA-DPEAIDAYALTGNAKSVLAGRISYKLDLR 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  152 GINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCeDLDWT--LSVLFDAMGAMSskyndtPSTASRAYDKNRDGFVI 229
Cdd:COG3321    165 GPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGV-NLMLTpeSFILFSKGGMLS------PDGRCRAFDADADGYVR 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  230 AGGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYD--MVAPSGEGAIRCMKMALST--VT-SKIDYINPHATSTPAGD 304
Cdd:COG3321    238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQAAVIRRALADagVDpATVDYVEAHGTGTPLGD 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  305 APEIEAIRQIFGAGDV----CpPIAATKSLTGHSLGATGVqeA--IYSLLMMQNNFICESAHIEELDPA--FADMPivrk 376
Cdd:COG3321    318 PIEAAALTAAFGQGRPadqpC-AIGSVKSNIGHLEAAAGV--AglIKAVLALRHGVLPPTLHFETPNPHidFENSP---- 390

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1443441168  377 ridnVQLNTVLS-------------NSFGFGGTNA 398
Cdd:COG3321    391 ----FYVNTELRpwpagggprragvSSFGFGGTNA 421
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 252-362 4.36e-32

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: 117.67  E-value: 4.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 252 YGEIVGYGATSDGYDMV--APSGEGAIRCMKMALSTVTSK---IDYINPHATSTPAGDAPEIEAIRQIFGAG--DVCPPI 324
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGltAPNGEGQARAIRRALADAGVDpedVDYVEAHGTGTPLGDPIEAEALKRVFGSGarKQPLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1443441168 325 AATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIE 362
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 2-401 7.91e-31

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: 121.70  E-value: 7.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   2 RRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG-APDIDIESLVDRRAMRFHGRGTAWNHIAMD 80
Cdd:cd00832     1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGeVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  81 QAIADAGLTEEEVSNERTGIIM--GSGGpstrtivdsADIT-RE------KGPKRVGPFavpkaMSstasatLATFFKIK 151
Cdd:cd00832    81 WALADAGVDPAALPPYDMGVVTasAAGG---------FEFGqRElqklwsKGPRHVSAY-----QS------FAWFYAVN 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 152 GINYSI-------SSACATSN----HCIGNAYEMIQYGKqDRMFAGGCED----LDWTLSVlfdAMGAMSSkyNDTPSTA 216
Cdd:cd00832   141 TGQISIrhgmrgpSGVVVAEQagglDALAQARRLVRRGT-PLVVSGGVDSalcpWGWVAQL---SSGRLST--SDDPARA 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 217 SRAYDKNRDGFVIAGGAGVLVLEDLETALARGAKIYGEIVGYGATSDGyDMVAPSGEGAIRCMKMALS---TVTSKIDYI 293
Cdd:cd00832   215 YLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDP-PPGSGRPPGLARAIRLALAdagLTPEDVDVV 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168 294 NPHATSTPAGDAPEIEAIRQIFGAGDVcpPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDPAFaDMPI 373
Cdd:cd00832   294 FADAAGVPELDRAEAAALAAVFGPRGV--PVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAY-GLDL 370

                         410       420
                  ....*....|....*....|....*...
gi 1443441168 374 VRKRIDNVQLNTVLSNSFGFGGTNATLV 401
Cdd:cd00832   371 VTGRPRPAALRTALVLARGRGGFNSALV 398
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 77-405 4.45e-21

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: 96.23  E-value: 4.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   77 IAMDQAIADAGLTEEeVSNERTGIIMGSGG--------------PSTRTIVDSADITREKGPKRVGPF----------AV 132
Cdd:TIGR02813   99 VVAKEVLNDAGLPDG-YDRDKIGITLGVGGgqkqssslnarlqyPVLKKVFKASGVEDEDSEMLIKKFqdqyihweenSF 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  133 PKAMSSTASATLATFFKIKGINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGcedldwtlsVLFDAMGAMSSKYNDT 212
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---------VCTDNSPFMYMSFSKT 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  213 PSTAS----RAYDKNRDGFVIAGGAGVLVLEDLETALARGAKIYGEIVGYGATSDGY--DMVAPSGEGAIRCMKMALSTV 286
Cdd:TIGR02813  249 PAFTTnediQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQAKALKRAYDDA 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  287 ---TSKIDYINPHATSTPAGDAPEIEAIRQIFGAG-DVCPPIA--ATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAH 360
Cdd:TIGR02813  329 gfaPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDnDQKQHIAlgSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTIN 408

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1443441168  361 IEELDPAF--ADMPIV--------RKRIDNVQLNTVLSnSFGFGGTNATLVFQRY 405
Cdd:TIGR02813  409 VDQPNPKLdiENSPFYlntetrpwMQREDGTPRRAGIS-SFGFGGTNFHMVLEEY 462
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 72-401 1.55e-15

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: 76.60  E-value: 1.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168   72 TAWnhiamdQAIADAGLTEEEVSNERTGIIMGsggpstrtivdsaditrekgpkrvgpfavpkAMSSTASATLATffkik 151
Cdd:smart00825  58 VAW------EALEDAGIDPESLRGSRTGVFVG-------------------------------VSSSDYSVTVDT----- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  152 ginysissACATSNHCIGNAYEMIQYGKQDRMFAGGCE-DLDWTLSVLFDAMGAMSskyndtPSTASRAYDKNRDGFVIA 230
Cdd:smart00825  96 --------ACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  231 GGAGVLVLEDLETALARGAKIYGEIVGYGATSDGYD--MVAPSGEGaircmkmalstvtskidyinphatstpagdapei 308
Cdd:smart00825 162 EGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGPA---------------------------------- 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441168  309 eairQIfgagdvcpPIAATKSLTGHSLGATGVQEAIYSLLMMQNNFICESAHIEELDP--AFADMPIV------------ 374
Cdd:smart00825 208 ----QL--------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPhiDLEESPLRvpteltpwpppg 275

                          330       340
                   ....*....|....*....|....*..
gi 1443441168  375 RKRIDNVqlntvlsNSFGFGGTNATLV 401
Cdd:smart00825 276 RPRRAGV-------SSFGFGGTNAHVI 295
 
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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