NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24644341|ref|NP_649565|]
View 

uncharacterized protein Dmel_CG12170 [Drosophila melanogaster]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase family protein( domain architecture ID 10095930)

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:  11969206
SCOP:  3000122

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
24-434 0e+00

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


:

Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 564.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAE-FKGLPCQVAAQIPreNLQLDQHLTKSDIKLMSPATQLAVLA 102
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFdASGFPSRIAGEVP--DFDPEDYLDRKELRRMDRFAQFALAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 103 AEEALSTGKLcpkQLSEEELERFGVCVGMGMFDLAEVYGAWNQL-QRGYNRVSPFFVPRLLPSMACGHISMRHGLRGPNH 181
Cdd:cd00834  79 AEEALADAGL---DPEELDPERIGVVIGSGIGGLATIEEAYRALlEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 182 SVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVMGEGAA 261
Cdd:cd00834 156 TVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTR-NDDPEKASRPFDKDRDGFVLGEGAG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 262 VLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIESH 341
Cdd:cd00834 235 VLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESK 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 342 AIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD--VDVNVVT-KATDWsadqKRRVA 418
Cdd:cd00834 315 AIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDpeCDLDYVPnEAREA----PIRYA 390
                       410
                ....*....|....*.
gi 24644341 419 LKNSFGFGGTNASLCI 434
Cdd:cd00834 391 LSNSFGFGGHNASLVF 406
 
Name Accession Description Interval E-value
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
24-434 0e+00

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 564.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAE-FKGLPCQVAAQIPreNLQLDQHLTKSDIKLMSPATQLAVLA 102
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFdASGFPSRIAGEVP--DFDPEDYLDRKELRRMDRFAQFALAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 103 AEEALSTGKLcpkQLSEEELERFGVCVGMGMFDLAEVYGAWNQL-QRGYNRVSPFFVPRLLPSMACGHISMRHGLRGPNH 181
Cdd:cd00834  79 AEEALADAGL---DPEELDPERIGVVIGSGIGGLATIEEAYRALlEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 182 SVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVMGEGAA 261
Cdd:cd00834 156 TVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTR-NDDPEKASRPFDKDRDGFVLGEGAG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 262 VLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIESH 341
Cdd:cd00834 235 VLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESK 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 342 AIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD--VDVNVVT-KATDWsadqKRRVA 418
Cdd:cd00834 315 AIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDpeCDLDYVPnEAREA----PIRYA 390
                       410
                ....*....|....*.
gi 24644341 419 LKNSFGFGGTNASLCI 434
Cdd:cd00834 391 LSNSFGFGGHNASLVF 406
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
24-437 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: 562.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAEFK-GLPCQVAAQIPreNLQLDQHLTKSDIKLMSPATQLAVLA 102
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDAsGLPVRIAGEVK--DFDPEEYLDRKELRRMDRFTQYALAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 103 AEEALSTGKLcpkQLSEEELERFGVCVGMGMFDLAEVYGAWNQL-QRGYNRVSPFFVPRLLPSMACGHISMRHGLRGPNH 181
Cdd:COG0304  79 AREALADAGL---DLDEVDPDRTGVIIGSGIGGLDTLEEAYRALlEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 182 SVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVMGEGAA 261
Cdd:COG0304 156 TVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 262 VLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIESH 341
Cdd:COG0304 235 VLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETK 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 342 AIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD--VDVNVVTKATdwsADQKRRVAL 419
Cdd:COG0304 315 AIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDpeCDLDYVPNEA---REAKIDYAL 391
                       410
                ....*....|....*...
gi 24644341 420 KNSFGFGGTNASLCIASY 437
Cdd:COG0304 392 SNSFGFGGHNASLVFKRY 409
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
23-437 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 545.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   23 RRRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAEFK-GLPCQVAAQIPRENLqlDQHLTKSDIKLMSPATQLAVL 101
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTsDLAVKIAGEVKDFNP--DDYMSRKEARRMDRFIQYGIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  102 AAEEALSTGKLCPkqlSEEELERFGVCVGMG---MFDLAEVYGAWNQlqRGYNRVSPFFVPRLLPSMACGHISMRHGLRG 178
Cdd:PRK07314  79 AAKQAVEDAGLEI---TEENADRIGVIIGSGiggLETIEEQHITLLE--KGPRRVSPFFVPMAIINMAAGHVSIRYGAKG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  179 PNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVMGE 258
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTR-NDDPERASRPFDKDRDGFVMGE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  259 GAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRI 338
Cdd:PRK07314 233 GAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  339 ESHAIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDV--DVNVVTKAtdwSADQKRR 416
Cdd:PRK07314 313 ETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEecDLDYVPNE---ARERKID 389
                        410       420
                 ....*....|....*....|.
gi 24644341  417 VALKNSFGFGGTNASLCIASY 437
Cdd:PRK07314 390 YALSNSFGFGGTNASLVFKRY 410
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
24-433 0e+00

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 542.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSaEF--KGLPCQVAAQIPreNLQLDQHLTKSDIKLMSPATQLAVL 101
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPIT-RFdaSDLPVKIAGEVK--DFDPEDYIDKKEARRMDRFIQYALA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   102 AAEEALSTGKLcpkQLSEEELERFGVCVGMGMFDLAEVY-GAWNQLQRGYNRVSPFFVPRLLPSMACGHISMRHGLRGPN 180
Cdd:TIGR03150  78 AAKEAVEDSGL---DIEEEDAERVGVIIGSGIGGLETIEeQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   181 HSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTaFNDNPAVASRPFDKSRDGFVMGEGA 260
Cdd:TIGR03150 155 HAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALST-RNDDPEKASRPFDKDRDGFVMGEGA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   261 AVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIES 340
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   341 HAIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD--VDVNVVTKAtdwSADQKRRVA 418
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDpeCDLDYVPNE---AREAKIDYA 390
                         410
                  ....*....|....*
gi 24644341   419 LKNSFGFGGTNASLC 433
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
24-271 9.29e-60

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: 195.55  E-value: 9.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSA------EFKGLPCQVAAQIPRENLQLDQ---------HLTKSD 88
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrwdpdKLYDPPSRIAGKIYTKWGGLDDifdfdplffGISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    89 IKLMSPATQLAVLAAEEALSTGKLCPKQLSEEeleRFGVCVGMGMFDLAEVYGAWNQLqrGYNRVSPFFVPrLLPSMACG 168
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGS---RTGVFIGSGIGDYAALLLLDEDG--GPRRGSPFAVG-TMPSVIAG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   169 HISMRHGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTafnDNPAVASRPFD 248
Cdd:pfam00109 155 RISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP---DGPCKAFDPFA 231
                         250       260
                  ....*....|....*....|...
gi 24644341   249 ksrDGFVMGEGAAVLLLEELEHA 271
Cdd:pfam00109 232 ---DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
182-432 5.69e-32

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: 123.21  E-value: 5.69e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    182 SVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALStafndnPAVASRPFDKSRDGFVMGEGAA 261
Cdd:smart00825  92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGEGVG 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    262 VLLLEELEHARARGAPILAEILGYGLSgdayHitspsdDGAGATLAmkraiqdagiAPedvtyvNAHAtstptgdriesh 341
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVN----Q------DGRSNGIT----------AP------SGPA------------ 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    342 aigrvfgahtpQVRVSSTKGAHGHLLGSSGnLEALF-VVLACANNKLPPSINIE----HLDVD---VNVVTKATDWSADQ 413
Cdd:smart00825 208 -----------QLLIGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFEtpnpHIDLEespLRVPTELTPWPPPG 275
                          250
                   ....*....|....*....
gi 24644341    414 KRRVALKNSFGFGGTNASL 432
Cdd:smart00825 276 RPRRAGVSSFGFGGTNAHV 294
 
Name Accession Description Interval E-value
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
24-434 0e+00

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 564.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAE-FKGLPCQVAAQIPreNLQLDQHLTKSDIKLMSPATQLAVLA 102
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFdASGFPSRIAGEVP--DFDPEDYLDRKELRRMDRFAQFALAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 103 AEEALSTGKLcpkQLSEEELERFGVCVGMGMFDLAEVYGAWNQL-QRGYNRVSPFFVPRLLPSMACGHISMRHGLRGPNH 181
Cdd:cd00834  79 AEEALADAGL---DPEELDPERIGVVIGSGIGGLATIEEAYRALlEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 182 SVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVMGEGAA 261
Cdd:cd00834 156 TVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTR-NDDPEKASRPFDKDRDGFVLGEGAG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 262 VLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIESH 341
Cdd:cd00834 235 VLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESK 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 342 AIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD--VDVNVVT-KATDWsadqKRRVA 418
Cdd:cd00834 315 AIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDpeCDLDYVPnEAREA----PIRYA 390
                       410
                ....*....|....*.
gi 24644341 419 LKNSFGFGGTNASLCI 434
Cdd:cd00834 391 LSNSFGFGGHNASLVF 406
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
24-437 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: 562.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAEFK-GLPCQVAAQIPreNLQLDQHLTKSDIKLMSPATQLAVLA 102
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDAsGLPVRIAGEVK--DFDPEEYLDRKELRRMDRFTQYALAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 103 AEEALSTGKLcpkQLSEEELERFGVCVGMGMFDLAEVYGAWNQL-QRGYNRVSPFFVPRLLPSMACGHISMRHGLRGPNH 181
Cdd:COG0304  79 AREALADAGL---DLDEVDPDRTGVIIGSGIGGLDTLEEAYRALlEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 182 SVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVMGEGAA 261
Cdd:COG0304 156 TVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 262 VLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIESH 341
Cdd:COG0304 235 VLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETK 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 342 AIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD--VDVNVVTKATdwsADQKRRVAL 419
Cdd:COG0304 315 AIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDpeCDLDYVPNEA---REAKIDYAL 391
                       410
                ....*....|....*...
gi 24644341 420 KNSFGFGGTNASLCIASY 437
Cdd:COG0304 392 SNSFGFGGHNASLVFKRY 409
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
23-437 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 545.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   23 RRRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAEFK-GLPCQVAAQIPRENLqlDQHLTKSDIKLMSPATQLAVL 101
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTsDLAVKIAGEVKDFNP--DDYMSRKEARRMDRFIQYGIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  102 AAEEALSTGKLCPkqlSEEELERFGVCVGMG---MFDLAEVYGAWNQlqRGYNRVSPFFVPRLLPSMACGHISMRHGLRG 178
Cdd:PRK07314  79 AAKQAVEDAGLEI---TEENADRIGVIIGSGiggLETIEEQHITLLE--KGPRRVSPFFVPMAIINMAAGHVSIRYGAKG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  179 PNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVMGE 258
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTR-NDDPERASRPFDKDRDGFVMGE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  259 GAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRI 338
Cdd:PRK07314 233 GAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  339 ESHAIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDV--DVNVVTKAtdwSADQKRR 416
Cdd:PRK07314 313 ETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEecDLDYVPNE---ARERKID 389
                        410       420
                 ....*....|....*....|.
gi 24644341  417 VALKNSFGFGGTNASLCIASY 437
Cdd:PRK07314 390 YALSNSFGFGGTNASLVFKRY 410
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
24-433 0e+00

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 542.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSaEF--KGLPCQVAAQIPreNLQLDQHLTKSDIKLMSPATQLAVL 101
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPIT-RFdaSDLPVKIAGEVK--DFDPEDYIDKKEARRMDRFIQYALA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   102 AAEEALSTGKLcpkQLSEEELERFGVCVGMGMFDLAEVY-GAWNQLQRGYNRVSPFFVPRLLPSMACGHISMRHGLRGPN 180
Cdd:TIGR03150  78 AAKEAVEDSGL---DIEEEDAERVGVIIGSGIGGLETIEeQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   181 HSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTaFNDNPAVASRPFDKSRDGFVMGEGA 260
Cdd:TIGR03150 155 HAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALST-RNDDPEKASRPFDKDRDGFVMGEGA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   261 AVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIES 340
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   341 HAIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD--VDVNVVTKAtdwSADQKRRVA 418
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDpeCDLDYVPNE---AREAKIDYA 390
                         410
                  ....*....|....*
gi 24644341   419 LKNSFGFGGTNASLC 433
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
20-436 1.62e-170

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 485.45  E-value: 1.62e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   20 PSGRRRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAE---------------FKGLPCQVAAQIPRENLQLD-QH 83
Cdd:PLN02836   2 PLPTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDdlkmksedeetqlytLDQLPSRVAALVPRGTGPGDfDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   84 LTKSDIKLMSPATQLAVLAAEEALSTGKLCPKQlsEEELERFGVCVGMGMFDLAEVYGAwNQLQRGY--NRVSPFFVPRL 161
Cdd:PLN02836  82 ELWLNSRSSSRFIGYALCAADEALSDARWLPSE--DEAKERTGVSIGGGIGSITDILEA-AQLICEKrlRRLSPFFVPRI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  162 LPSMACGHISMRHGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAFNDNPA 241
Cdd:PLN02836 159 LINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKFNSCPT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  242 VASRPFDKSRDGFVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPED 321
Cdd:PLN02836 239 EASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQ 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  322 VTYVNAHATSTPTGDRIESHAIGRVFG--AHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD-- 397
Cdd:PLN02836 319 VDYVNAHATSTPLGDAVEARAIKTVFSehATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDpi 398
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 24644341  398 VDVNVVTKATdwSADQKRRVALKNSFGFGGTNASLCIAS 436
Cdd:PLN02836 399 FDDGFVPLTA--SKAMLIRAALSNSFGFGGTNASLLFTS 435
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
22-438 5.62e-169

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 481.03  E-value: 5.62e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   22 GRRRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAEF-KGLPCQVAAQIP------RENLQLDQHLTKSDIKLMSP 94
Cdd:PRK06333   2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPvGDLATKIGGQVPdlaedaEAGFDPDRYLDPKDQRKMDR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   95 ATQLAVLAAEEALSTGKLCPKqlSEEELERFGVCVGMGMFDL-AEVYGAWNQLQRGYNRVSPFFVPRLLPSMACGHISMR 173
Cdd:PRK06333  82 FILFAMAAAKEALAQAGWDPD--TLEDRERTATIIGSGVGGFpAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  174 HGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAFNDNPAVASRPFDKSRDG 253
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFNDAPEQASRPFDRDRDG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  254 FVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTP 333
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  334 TGDRIESHAIGRVFGaHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDVDVN----VVTKATDW 409
Cdd:PRK06333 320 VGDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgldvVANKARPM 398
                        410       420
                 ....*....|....*....|....*....
gi 24644341  410 SADqkrrVALKNSFGFGGTNASLCIASYI 438
Cdd:PRK06333 399 DMD----YALSNGFGFGGVNASILFRRWE 423
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
33-437 8.84e-162

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 462.62  E-value: 8.84e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   33 AVTPLGNNGPDSWRRILAGESAISRLS--------------AEFK---GLPCQVAAQIPRENLqlDQHLTKSDIKlMSPA 95
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTefpkflpdcipeqkALENlvaAMPCQIAAEVDQSEF--DPSDFAPTKR-ESRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   96 TQLAVLAAEEALSTGKLCPkqLSEEELERFGVCVGMGMFDLAEVYGAWNQLQ-RGYNRVSPFFVPRLLPSMACGHISMRH 174
Cdd:PTZ00050  78 THFAMAAAREALADAKLDI--LSEKDQERIGVNIGSGIGSLADLTDEMKTLYeKGHSRVSPYFIPKILGNMAAGLVAIKH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  175 GLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAFNDNPAVASRPFDKSRDGF 254
Cdd:PTZ00050 156 KLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDDPQRASRPFDKDRAGF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  255 VMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAG-IAPEDVTYVNAHATSTP 333
Cdd:PTZ00050 236 VMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTP 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  334 TGDRIESHAIGRVFGAHT-PQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEH--LDVDVNVVTKATDwS 410
Cdd:PTZ00050 316 IGDKIELKAIKKVFGDSGaPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENpdAECDLNLVQGKTA-H 394
                        410       420
                 ....*....|....*....|....*..
gi 24644341  411 ADQKRRVALKNSFGFGGTNASLCIASY 437
Cdd:PTZ00050 395 PLQSIDAVLSTSFGFGGVNTALLFTKY 421
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
23-432 1.11e-120

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 357.78  E-value: 1.11e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   23 RRRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRL--------SAEFKGLPcqvaaqiprENLQLDQHLTKSDIKLMSP 94
Cdd:PRK08722   3 KRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIehfdttnfSTRFAGLV---------KDFNCEEYMSKKDARKMDL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   95 ATQLAVLAAEEALSTGKLcpkQLSEEELERFGVCVGMGM--FDLAEVyGAWNQLQRGYNRVSPFFVPRLLPSMACGHISM 172
Cdd:PRK08722  74 FIQYGIAAGIQALDDSGL---EVTEENAHRIGVAIGSGIggLGLIEA-GHQALVEKGPRKVSPFFVPSTIVNMIAGNLSI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  173 RHGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRD 252
Cdd:PRK08722 150 MRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTR-NDEPQKASRPWDKDRD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  253 GFVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATST 332
Cdd:PRK08722 229 GFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTST 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  333 PTGDRIESHAIGRVFG-AHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDVDVNVvtkatDWSA 411
Cdd:PRK08722 309 PAGDVAEIKGIKRALGeAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDI-----DLVP 383
                        410       420
                 ....*....|....*....|....*.
gi 24644341  412 DQKRRV-----ALKNSFGFGGTNASL 432
Cdd:PRK08722 384 HTARKVesmeyAICNSFGFGGTNGSL 409
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
24-432 1.16e-120

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 357.12  E-value: 1.16e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLS----AEFkglPCQVAAQIprENLQLDQHLTKSDIKLMSPATQLA 99
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITlfdaSDF---PVQIAGEI--TDFDPTEVMDPKEVKKADRFIQLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  100 VLAAEEALSTGKLCPkqlSEEELERFGVCVGMGMFDLAEVYGawNQL---QRGYNRVSPFFVPRLLPSMACGHISMRHGL 176
Cdd:PRK08439  77 LKAAREAMKDAGFLP---EELDAERFGVSSASGIGGLPNIEK--NSIicfEKGPRKISPFFIPSALVNMLGGFISIEHGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  177 RGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVM 256
Cdd:PRK08439 152 KGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTR-NDDPKKASRPFDKDRDGFVM 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  257 GEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDgaGATLAMKRAIQDAGIAPEDvtYVNAHATSTPTGD 336
Cdd:PRK08439 231 GEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNPKID--YINAHGTSTPYND 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  337 RIESHAIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEH------LDVDVNVVTKAtdws 410
Cdd:PRK08439 307 KNETAALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETpdpecdLDYIPNVARKA---- 382
                        410       420
                 ....*....|....*....|..
gi 24644341  411 adqKRRVALKNSFGFGGTNASL 432
Cdd:PRK08439 383 ---ELNVVMSNSFGFGGTNGVV 401
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
19-438 7.27e-106

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 323.85  E-value: 7.27e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   19 TPSGRRRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSA-EFKGLPCQVAAQIprENLQLDQHLTKSDIKLMSPATQ 97
Cdd:PLN02787 124 PLTKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERfDCSQFPTRIAGEI--KSFSTDGWVAPKLSKRMDKFML 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   98 LAVLAAEEALSTGKLCPKQLSEEELERFGVCVGMGMFDLAEVYGAWNQLQRGYNRVSPFFVPRLLPSMACGHISMRHGLR 177
Cdd:PLN02787 202 YLLTAGKKALADGGITEDVMKELDKTKCGVLIGSAMGGMKVFNDAIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWM 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  178 GPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVMG 257
Cdd:PLN02787 282 GPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQR-NDDPTKASRPWDMNRDGFVMG 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  258 EGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDR 337
Cdd:PLN02787 361 EGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDL 440
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  338 IESHAIGRVFGAHtPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD--VDVNVVTKATDWSADQKr 415
Cdd:PLN02787 441 KEYQALMRCFGQN-PELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPEsgVDTKVLVGPKKERLDIK- 518
                        410       420
                 ....*....|....*....|...
gi 24644341  416 rVALKNSFGFGGTNASLCIASYI 438
Cdd:PLN02787 519 -VALSNSFGFGGHNSSILFAPYK 540
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
120-438 3.29e-99

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 300.11  E-value: 3.29e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  120 EELERFGVCVGMGMFDLAEV-YGAWNQLQRGYNRVSPFFVPRLLPSMACGHISMRHGLRGPNHSVSTACATGAHALGDAM 198
Cdd:PRK14691  23 EKQERTATIIGAGIGGFPAIaHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  199 RFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAFNDNPAVASRPFDKSRDGFVMGEGAAVLLLEELEHARARGAPI 278
Cdd:PRK14691 103 RMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHFNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  279 LAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIESHAIGRVFGaHTPQVRVSS 358
Cdd:PRK14691 183 LAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFG-ESNALAITS 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  359 TKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDVDVNVVTKATDWSADQKRRVALKNSFGFGGTNASLCIASYI 438
Cdd:PRK14691 262 TKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKRWV 341
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
14-437 5.54e-98

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 299.72  E-value: 5.54e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   14 TRSLSTPSGRRRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAEFK---GLPCQVAAQIPREnlqLDQHLTKSDIK 90
Cdd:PRK07910   2 MTELTTGKGFPNVVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVeefDLPVRIGGHLLEE---FDHQLTRVELR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   91 LMSPATQLAVLAAEEALSTGKlCPkqlsEEELERFGVCVGMGMFDLAEVYGAWNQL-QRGYNRVSPFFVPRLLPSMACGH 169
Cdd:PRK07910  79 RMSYLQRMSTVLGRRVWENAG-SP----EVDTNRLMVSIGTGLGSAEELVFAYDDMrARGLRAVSPLAVQMYMPNGPAAA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  170 ISMRHGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAFNDNPAVASRPFDK 249
Cdd:PRK07910 154 VGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMSTNNDDPAGACRPFDK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  250 SRDGFVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHA 329
Cdd:PRK07910 234 DRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  330 TSTPTGDRIESHAIGRVFGAHTPQVRVSstKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD--VDVNVVtkat 407
Cdd:PRK07910 314 TGTSVGDVAEGKAINNALGGHRPAVYAP--KSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDpeIDLDVV---- 387
                        410       420       430
                 ....*....|....*....|....*....|....
gi 24644341  408 dwsADQKR----RVALKNSFGFGGTNASLCIASY 437
Cdd:PRK07910 388 ---AGEPRpgnyRYAINNSFGFGGHNVALAFGRY 418
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
24-437 1.49e-96

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 295.43  E-value: 1.49e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRlSAEFK--GLPCQVAAQIpreNLQLDQHLTKSDIKLMSPATQLAVL 101
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITF-SPEFAemGMRSQVWGNV---KLDPTGLIDRKVMRFMGDASAYAYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  102 AAEEALSTGKLCPKQLSEEeleRFGVCVGMGmfdlaeVYGAWNQLQ--------RGYNRVSPFFVPRLLPSMACGHISMR 173
Cdd:PRK07967  78 AMEQAIADAGLSEEQVSNP---RTGLIAGSG------GGSTRNQVEaadamrgpRGPKRVGPYAVTKAMASTVSACLATP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  174 HGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAgFCRLRALSTAFNDNPAVASRPFDKSRDG 253
Cdd:PRK07967 149 FKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKYNDTPEKASRAYDANRDG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  254 FVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSddGAGATLAMKRAIQDAGiapEDVTYVNAHATSTP 333
Cdd:PRK07967 228 FVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPS--GEGAVRCMQMALATVD---TPIDYINTHGTSTP 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  334 TGDRIESHAIGRVFGAHTPQvrVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD---VDVNVVTKATDws 410
Cdd:PRK07967 303 VGDVKELGAIREVFGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDpqaAGMPIVTETTD-- 378
                        410       420
                 ....*....|....*....|....*..
gi 24644341  411 aDQKRRVALKNSFGFGGTNASLCIASY 437
Cdd:PRK07967 379 -NAELTTVMSNSFGFGGTNATLVFRRY 404
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
24-434 6.75e-92

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 283.42  E-value: 6.75e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLS--AEFKGLPCQVAAqiPRENLQLDQHLTKSDIKLMSPATQLAVL 101
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPewDRYDGLNTRLAA--PIDDFELPAHYTRKKIRSMGRVSLMATR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  102 AAEEALSTGKLcpkqLSEEELE--RFGVCVGMGMFDLAEVYGAWNQLQRGY-NRVSPFFVPRLLPSMACGHISMRHGLRG 178
Cdd:PRK09116  80 ASELALEDAGL----LGDPILTdgRMGIAYGSSTGSTDPIGAFGTMLLEGSmSGITATTYVRMMPHTTAVNVGLFFGLKG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  179 PNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEAcIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGFVMGE 258
Cdd:PRK09116 156 RVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTR-NDAPELTPRPFDANRDGLVIGE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  259 GAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGatLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRI 338
Cdd:PRK09116 234 GAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIA 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  339 ESHAIGRVFGAHTPqvrVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDVDVNvvtkATDWSADQKRRV- 417
Cdd:PRK09116 312 ESQATAAVFGARMP---ISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACG----ALDYIMGEAREId 384
                        410       420
                 ....*....|....*....|
gi 24644341  418 ---ALKNSFGFGGTNASLCI 434
Cdd:PRK09116 385 teyVMSNNFAFGGINTSLIF 404
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
24-432 3.30e-86

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 268.92  E-value: 3.30e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  24 RRVVVTGSGAVTPLGNN---GPDSWRRILAGESAISRLSAEFKGLPCQVAAQIPrenlqlDQHLTKSDIK---LMSPATQ 97
Cdd:cd00828   1 SRVVITGIGVVSPHGEGcdeVEEFWEALREGRSGIAPVARLKSRFDRGVAGQIP------TGDIPGWDAKrtgIVDRTTL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  98 LAVLAAEEALSTGKLCPKQlsEEELERFGVCVGMGMFDLAEVYGAWNQLqrgYNRVSPFFVPR--LLPSMACGHISMRHG 175
Cdd:cd00828  75 LALVATEEALADAGITDPY--EVHPSEVGVVVGSGMGGLRFLRRGGKLD---ARAVNPYVSPKwmLSPNTVAGWVNILLL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 176 L-RGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEAcIDPLSIAGFCRLRALSTAfNDNPAVASRPFDKSRDGF 254
Cdd:cd00828 150 SsHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTA-EEEPEEMSRPFDETRDGF 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 255 VMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHiTSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPT 334
Cdd:cd00828 228 VEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAG-RSVPAGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPA 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 335 GDRIESHAIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDVDV---NVVTKATDWSA 411
Cdd:cd00828 307 NDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVehlSVVGLSRDLNL 386
                       410       420
                ....*....|....*....|.
gi 24644341 412 dqKRRVALKNSFGFGGTNASL 432
Cdd:cd00828 387 --KVRAALVNAFGFGGSNAAL 405
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
22-437 4.92e-86

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 269.19  E-value: 4.92e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   22 GRRRVVVTGSGAVTPLGNNGPDSWRRILAGES---AISRLSAEfkGLPCQVAAQIprenlqldQHLTKSDIKLMSPATQL 98
Cdd:PRK06501   9 GRPIVAVTGMGVVTSLGQGKADNWAALTAGESgihTITRFPTE--GLRTRIAGTV--------DFLPESPFGASALSEAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   99 AVLAAEEALSTGklcpkqlseeelerfgvCVGMGMFD------LAEVYGAWNQLQRGYNRVSPFFVP---RLLPSMACG- 168
Cdd:PRK06501  79 ARLAAEEALAQA-----------------GIGKGDFPgplflaAPPVELEWPARFALAAAVGDNDAPsydRLLRAARGGr 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  169 ---------------HISMRHGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALS 233
Cdd:PRK06501 142 fdalherfqfgsiadRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALS 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  234 TAfNDNPAVASRPFDKSRDGFVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQ 313
Cdd:PRK06501 222 TQ-NDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  314 DAGIAPEDVTYVNAHATSTPTGDRIESHAIGRVFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINI 393
Cdd:PRK06501 301 DAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINY 380
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 24644341  394 EH------LDVDVNVvtkatdwSADQKRRVALKNSFGFGGTNASLCIASY 437
Cdd:PRK06501 381 DNpdpaipLDVVPNV-------ARDARVTAVLSNSFGFGGQNASLVLTAE 423
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
25-436 1.02e-79

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 251.51  E-value: 1.02e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   25 RVVVTGSGAVTPLGNNgPDSWRRILAGESAISRLS--AEFKGLPCQVAAQIPRENLQLDQHLTKS---DIKLMSPATQLA 99
Cdd:PRK05952   3 KVVVTGIGLVSALGDL-EQSWQRLLQGKSGIKLHQpfPELPPLPLGLIGNQPSSLEDLTKTVVTAalkDAGLTPPLTDCG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  100 VlaaeeALSTGKLCpkQLSEEELERFGVcVGMGMFDLAEVYGAWnqLQRgynrvspffvprlLPSMACGHISMRHGLRGP 179
Cdd:PRK05952  82 V-----VIGSSRGC--QGQWEKLARQMY-QGDDSPDEELDLENW--LDT-------------LPHQAAIAAARQIGTQGP 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  180 NHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAfndnpavASRPFDKSRDGFVMGEG 259
Cdd:PRK05952 139 VLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKT-------GAYPFDRQREGLVLGEG 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  260 AAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIE 339
Cdd:PRK05952 212 GAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQRE 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  340 SHAIGRVFGahtPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDVDVNVVTKAtdwsADQKRRVAL 419
Cdd:PRK05952 292 ANLIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVRQA----QQSPLQNVL 364
                        410
                 ....*....|....*..
gi 24644341  420 KNSFGFGGTNASLCIAS 436
Cdd:PRK05952 365 CLSFGFGGQNAAIALGK 381
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
25-432 4.71e-77

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: 245.93  E-value: 4.71e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  25 RVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAEFKGlpcqVAAQIPRENLQ----------LDQH---------LT 85
Cdd:cd00833   2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWD----ADGYYPDPGKPgktytrrggfLDDVdafdaaffgIS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  86 KSDIKLMSPATQLAVLAAEEALSTGKLCPKQLSeeeLERFGVCVGMGMFDLAEvygawnQLQRGYNRVSPFFVPRLLPSM 165
Cdd:cd00833  78 PREAEAMDPQQRLLLEVAWEALEDAGYSPESLA---GSRTGVFVGASSSDYLE------LLARDPDEIDAYAATGTSRAF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 166 ACGHISMRHGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALStafndnPAVASR 245
Cdd:cd00833 149 LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS------PDGRCR 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 246 PFDKSRDGFVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAY--HITSPSddGAGATLAMKRAIQDAGIAPEDVT 323
Cdd:cd00833 223 PFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPS--GEAQAALIRRAYARAGVDPSDID 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 324 YVNAHATSTPTGDRIESHAIGRVFGAHTPQVR---VSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIE----HL 396
Cdd:cd00833 301 YVEAHGTGTPLGDPIEVEALAKVFGGSRSADQpllIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFEtpnpKI 380
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 24644341 397 DVD---VNVVTKATDWSADQKRRVALKNSFGFGGTNASL 432
Cdd:cd00833 381 DFEespLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHV 419
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
25-436 2.64e-68

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 222.60  E-value: 2.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   25 RVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAEFKGLPCQ---------VAAQIPreNLQLDQHLTKSDIKLMSPA 95
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDagaglasafIGAELD--SLALPERLDAKLLRRASLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   96 TQLAVLAAEEALSTGKLCPKQLSeeeleRFGVCVGMGMFDLAEVYGAWNQLQRGYNRVSPFFVPRLLPSMACGHISMRHG 175
Cdd:PRK07103  81 AQAALAAAREAWRDAALGPVDPD-----RIGLVVGGSNLQQREQALVHETYRDRPAFLRPSYGLSFMDTDLVGLCSEQFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  176 LRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTA-FNDNPAVASRPFDKSRDGF 254
Cdd:PRK07103 156 IRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDrFADEPEAACRPFDQDRDGF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  255 VMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGAtlAMKRAIQDAGIAPEDVTYVNAHATSTPT 334
Cdd:PRK07103 236 IYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMR--VIRAALRRAGLGPEDIDYVNPHGTGSPL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  335 GDRIESHAIgrvFGAHTPQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEH-LDVDVNVVTKAtdwSADQ 413
Cdd:PRK07103 314 GDETELAAL---FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEpIDERFRWVGST---AESA 387
                        410       420
                 ....*....|....*....|...
gi 24644341  414 KRRVALKNSFGFGGTNASLCIAS 436
Cdd:PRK07103 388 RIRYALSLSFGFGGINTALVLER 410
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
175-432 2.41e-66

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 217.02  E-value: 2.41e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  175 GLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSgeacIDPLS---IAGFCRLRALSTAfndnpavASRPFDKSR 251
Cdd:PRK09185 148 GLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGG----VDSLCrltLNGFNSLESLSPQ-------PCRPFSANR 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  252 DGFVMGEGAAVLLLEelehaRARGAPILaeILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATS 331
Cdd:PRK09185 217 DGINIGEAAAFFLLE-----REDDAAVA--LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTA 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  332 TPTGDRIESHAIGRVFGAHTPqvrVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLD---VDVNVVTKAtd 408
Cdd:PRK09185 290 TPLNDAMESRAVAAVFGDGVP---CSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDpalPPLYLVENA-- 364
                        250       260
                 ....*....|....*....|....
gi 24644341  409 wsADQKRRVALKNSFGFGGTNASL 432
Cdd:PRK09185 365 --QALAIRYVLSNSFAFGGNNCSL 386
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
24-271 9.29e-60

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: 195.55  E-value: 9.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSA------EFKGLPCQVAAQIPRENLQLDQ---------HLTKSD 88
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrwdpdKLYDPPSRIAGKIYTKWGGLDDifdfdplffGISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    89 IKLMSPATQLAVLAAEEALSTGKLCPKQLSEEeleRFGVCVGMGMFDLAEVYGAWNQLqrGYNRVSPFFVPrLLPSMACG 168
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGS---RTGVFIGSGIGDYAALLLLDEDG--GPRRGSPFAVG-TMPSVIAG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   169 HISMRHGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTafnDNPAVASRPFD 248
Cdd:pfam00109 155 RISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP---DGPCKAFDPFA 231
                         250       260
                  ....*....|....*....|...
gi 24644341   249 ksrDGFVMGEGAAVLLLEELEHA 271
Cdd:pfam00109 232 ---DGFVRGEGVGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
95-432 1.78e-57

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 192.08  E-value: 1.78e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  95 ATQLAVLAAEEALSTGKLCPKQLSEEeleRFGVCVGM-GMFDLAEVYGAWNQLQrgynrVSPFFVPRLLPSMACGHISMR 173
Cdd:cd00825  11 VSILGFEAAERAIADAGLSREYQKNP---IVGVVVGTgGGSPRFQVFGADAMRA-----VGPYVVTKAMFPGASGQIATP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 174 HGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALStafndnPAVASRPFDKSRDG 253
Cdd:cd00825  83 LGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST------PEKASRTFDAAADG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 254 FVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTP 333
Cdd:cd00825 157 FVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 334 TGDRIESHAIGRVFGAHTPQvrVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDVD-VNVVTKATdwsaD 412
Cdd:cd00825 237 IGDVKELKLLRSEFGDKSPA--VSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAgLNIVTETT----P 310
                       330       340
                ....*....|....*....|
gi 24644341 413 QKRRVALKNSFGFGGTNASL 432
Cdd:cd00825 311 RELRTALLNGFGLGGTNATL 330
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
126-430 2.63e-55

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 198.17  E-value: 2.63e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  126 GVCVGMGMFDLaevygaWNQLQRGYNRVSPFFVPRLLPSMACGHISMRHGLRGPNHSVSTACATGAHALGDAMRFIRSGD 205
Cdd:COG3321  119 GVFVGASSNDY------ALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGE 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  206 ADLMLAGSGEACIDPLSIAGFCRLRALStafndnPAVASRPFDKSRDGFVMGEGAAVLLLEELEHARARGAPILAEILGY 285
Cdd:COG3321  193 CDLALAGGVNLMLTPESFILFSKGGMLS------PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGS 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  286 GLS--GDAYHITSPSddGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIESHAIGRVFGAHTPQVR---VSSTK 360
Cdd:COG3321  267 AVNqdGRSNGLTAPN--GPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPADQpcaIGSVK 344
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644341  361 GAHGHLLGSSGnLEALF-VVLACANNKLPPSINIE----HLDVD---VNVVTKATDWSADQKRRVALKNSFGFGGTNA 430
Cdd:COG3321  345 SNIGHLEAAAG-VAGLIkAVLALRHGVLPPTLHFEtpnpHIDFEnspFYVNTELRPWPAGGGPRRAGVSSFGFGGTNA 421
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
24-432 4.41e-53

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: 182.56  E-value: 4.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  24 RRVVVTGSGAVTPLGNNGPDSWRRILAGESAISRLSAE-FKGLPCQVAAQIPreNLQLDQHLTKSDIKLMSPATQLAVLA 102
Cdd:cd00832   1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFdPSGYPARLAGEVP--DFDAAEHLPGRLLPQTDRMTRLALAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 103 AEEALSTGKLCPKQLSEEELerfGVCV----GMGMFDLAEVYGAWNQlqrGYNRVSPFFVPRLLPSMACGHISMRHGLRG 178
Cdd:cd00832  79 ADWALADAGVDPAALPPYDM---GVVTasaaGGFEFGQRELQKLWSK---GPRHVSAYQSFAWFYAVNTGQISIRHGMRG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 179 PNHSVSTACATGAHALGDAMRFIRSGdADLMLAGSGEACIDPLSIAGFCRLRALSTAfnDNPAVASRPFDKSRDGFVMGE 258
Cdd:cd00832 153 PSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTS--DDPARAYLPFDAAAAGYVPGE 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 259 GAAVLLLEELEHARARGAPILAEILGYGLSGDAyhitsPSDDGAGATL--AMKRAIQDAGIAPEDVTYVNAHATSTPTGD 336
Cdd:cd00832 230 GGAILVLEDAAAARERGARVYGEIAGYAATFDP-----PPGSGRPPGLarAIRLALADAGLTPEDVDVVFADAAGVPELD 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 337 RIESHAIGRVFGAHtpQVRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIEHLDVDVNVvtkatDWSADQKR- 415
Cdd:cd00832 305 RAEAAALAAVFGPR--GVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGL-----DLVTGRPRp 377
                       410       420
                ....*....|....*....|
gi 24644341 416 ---RVALKNSFGFGGTNASL 432
Cdd:cd00832 378 aalRTALVLARGRGGFNSAL 397
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
279-394 7.73e-42

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: 143.86  E-value: 7.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   279 LAEILGYGLSGDAYHITSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTPTGDRIESHAIGRVFGAHTPQ--VRV 356
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 24644341   357 SSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSINIE 394
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
164-434 1.19e-32

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 124.09  E-value: 1.19e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 164 SMACGHISMRHGLR-GPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACidplsiagfcrlralstafndnpav 242
Cdd:cd00327  44 SGAAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF------------------------- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 243 asrpfdksrdgfVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGD-AYHITSPSDDGAGAtlAMKRAIQDAGIAPED 321
Cdd:cd00327  99 ------------VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVSGEGLAR--AARKALEGAGLTPSD 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 322 VTYVNAHATSTPTGDRIESHAIGRVFGAHTPQvrVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSiniehldvdvn 401
Cdd:cd00327 165 IDYVEAHGTGTPIGDAVELALGLDPDGVRSPA--VSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------- 231
                       250       260       270
                ....*....|....*....|....*....|...
gi 24644341 402 vvtkatdwsaDQKRRVALKNSFGFGGTNASLCI 434
Cdd:cd00327 232 ----------PREPRTVLLLGFGLGGTNAAVVL 254
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
182-432 5.69e-32

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: 123.21  E-value: 5.69e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    182 SVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALStafndnPAVASRPFDKSRDGFVMGEGAA 261
Cdd:smart00825  92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGEGVG 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    262 VLLLEELEHARARGAPILAEILGYGLSgdayHitspsdDGAGATLAmkraiqdagiAPedvtyvNAHAtstptgdriesh 341
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVN----Q------DGRSNGIT----------AP------SGPA------------ 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    342 aigrvfgahtpQVRVSSTKGAHGHLLGSSGnLEALF-VVLACANNKLPPSINIE----HLDVD---VNVVTKATDWSADQ 413
Cdd:smart00825 208 -----------QLLIGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFEtpnpHIDLEespLRVPTELTPWPPPG 275
                          250
                   ....*....|....*....
gi 24644341    414 KRRVALKNSFGFGGTNASL 432
Cdd:smart00825 276 RPRRAGVSSFGFGGTNAHV 294
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
159-437 2.16e-28

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: 118.95  E-value: 2.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    159 PRLLPSMACGHISMRHGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLagSGEACID--PLSIAGFCRlralSTAF 236
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMI--TGGVCTDnsPFMYMSFSK----TPAF 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    237 NDNPAVasRPFDKSRDGFVMGEGAAVLLLEELEHARARGAPILAEILGYGLSGDAY--HITSPSDDGAGAtlAMKRAIQD 314
Cdd:TIGR02813  252 TTNEDI--QPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQAK--ALKRAYDD 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341    315 AGIAPEDVTYVNAHATSTPTGDRIESHAIGRVFGAHTPQ---VRVSSTKGAHGHLLGSSGNLEALFVVLACANNKLPPSI 391
Cdd:TIGR02813  328 AGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTI 407
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24644341    392 NIEH----LDVDVN---VVTKATDWSA--DQKRRVALKNSFGFGGTNASLCIASY 437
Cdd:TIGR02813  408 NVDQpnpkLDIENSpfyLNTETRPWMQreDGTPRRAGISSFGFGGTNFHMVLEEY 462
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
24-325 9.57e-08

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 53.49  E-value: 9.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   24 RRVVVTGSGAVTPLGnngPDSWRRILAGESAIS-----RLSAEFKGlPCQVAAQIPrenlqLDQHLTKSdiklmSPATQL 98
Cdd:PRK06147   3 RALAIVGSGMVTAVG---LDAPSSCAAIRARLDnfqetRFIDPPGG-EWLIGAPVP-----LPPPWRGP-----ERLAEM 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   99 AVLAAEEALStgKLCPKQLSE-------EELERFGVCVgmgmfDLAEvygawnqlqrgynrvspffvpRLLPSmacghIS 171
Cdd:PRK06147  69 AAPAIAEALE--GLPALDASEaplllcvAEEERPGRPP-----DLEE---------------------RLLRE-----LE 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  172 MRHGLR--GPNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEACIDPLSIAGFCRLRALSTAFNDNpavasrpfdk 249
Cdd:PRK06147 116 ARLGLRlePGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNSN---------- 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24644341  250 srdGFVMGEGAAVLLLEELEHARARGAPilaeILGYGLSGDAYHITSPSD---DGAGATLAMKRAIQDAGIAPEDVTYV 325
Cdd:PRK06147 186 ---GFIPGEAAAAVLLGRPAGGEAPGLP----LLGLGLGREPAPVGESEDlplRGDGLTQAIRAALAEAGCGLEDMDYR 257
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
259-325 1.09e-05

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


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 47.47  E-value: 1.09e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24644341 259 GAAVLLLEELEHARARGAPILAEILGYGLSGDAyhitsPSDDGAGATLAMKRAIQDAGIAPEDVTYV 325
Cdd:cd00751 247 GAAAVLLMSEEKAKELGLKPLARIVGYAVAGVD-----PAIMGIGPVPAIPKALKRAGLTLDDIDLI 308
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
21-282 1.14e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 47.26  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   21 SGRRRVVVTGSGAVTPLGNnGPDSWRRILAGESAISRLSAE-FKGLPCQ------VAAQIPRenlqldqhltKSDIKLMS 93
Cdd:PRK06519   3 MQPNDVVITGIGLVSSLGE-GLDAHWNALSAGRPQPNVDTEtFAPYPVHplpeidWSQQIPK----------RGDQRQME 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341   94 PATQLAVLAAEEALSTGKLcpkQLSEEELERFGVCV--GMGMFDLAEVYGAWNQLQRGYNRVSpFFVPRL---------- 161
Cdd:PRK06519  72 TWQRLGTYAAGLALDDAGI---KGNEELLSTMDMIVaaGGGERDIAVDTAILNEARKRNDRGV-LLNERLmtelrptlfl 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  162 --LPSMACGHISMRHGLRGPNHSVSTACATGAHALGDAMRFIRSGDADLMLAG---SGEAcIDPL---SIAGFCRLRALS 233
Cdd:PRK06519 148 aqLSNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGgayNAER-PDMLllyELGGLLLKGGWA 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 24644341  234 TAFNDNPAVAsrpfdksrDGFVMGEGAAVLLLEELEHARARGAPILAEI 282
Cdd:PRK06519 227 PVWSRGGEDG--------GGFILGSGGAFLVLESREHAEARGARPYARI 267
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
259-325 4.26e-05

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: 45.44  E-value: 4.26e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24644341 259 GAAVLLLEELEHARARGAPILAEILGYGLSGDAyhitsPSDDGAGATLAMKRAIQDAGIAPEDVTYV 325
Cdd:COG0183 251 GAAALLLMSEEAAKELGLKPLARIVAYAVAGVD-----PEIMGIGPVPATRKALARAGLTLDDIDLI 312
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
256-371 6.43e-05

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 44.88  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  256 MGEGAAVLLLEELEHARARGAPILAEILGYGLSGdayhiTSPSDDGAGATLAMKRAIQDAGIAPEDVTYVNAHATSTptg 335
Cdd:PRK05656 250 LNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAG-----VDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFA--- 321
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 24644341  336 drIESHAIGRVFGAHTPQVRVSSTKGAHGHLLGSSG 371
Cdd:PRK05656 322 --AQSLAVGKELGWDAAKVNVNGGAIALGHPIGASG 355
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
245-371 6.86e-05

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 44.70  E-value: 6.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  245 RPFDKSRDGFV-------MGEGAAVLLLEELEHARARGAPILAEILGYglsGDA-----YHITSPSddgagatLAMKRAI 312
Cdd:PLN02644 232 RPSFKEDGGSVtagnassISDGAAALVLVSGEKALELGLQVIAKIRGY---ADAaqapeLFTTAPA-------LAIPKAL 301
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24644341  313 QDAGIAPEDVTY--VNaHATStptgdrIESHAIGRVFGAHTPQVRVSSTKGAHGHLLGSSG 371
Cdd:PLN02644 302 KHAGLEASQVDYyeIN-EAFS------VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSG 355
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
170-334 1.37e-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: 43.79  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 170 ISMRHGLRG-PNHSVSTACATGAHALGDAMRFIRSGDADLMLAGSGEA--------------------CIDPLSIAGFCR 228
Cdd:cd00829  59 IAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKmsdvptgdeaggrasdleweGPEPPGGLTPPA 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341 229 LRALSTAF-----------------------NDNP-AVASRPFD-----KSR---------DGFVMGEGAAVLLLEELEH 270
Cdd:cd00829 139 LYALAARRymhrygttredlakvavknhrnaARNPyAQFRKPITvedvlNSRmiadplrllDCCPVSDGAAAVVLASEER 218
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24644341 271 ARARGAPiLAEILGYGLSGDAYHITSPSDDGA--GATLAMKRAIQDAGIAPEDVTYVNAHATSTPT 334
Cdd:cd00829 219 ARELTDR-PVWILGVGAASDTPSLSERDDFLSldAARLAARRAYKMAGITPDDIDVAELYDCFTIA 283
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
389-430 1.98e-04

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 40.61  E-value: 1.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 24644341   389 PSINIEHLDvD--VNVVTKATDWSADqkrRVALkNSFGFGGTNA 430
Cdd:pfam16197   1 PNPDIPALL-DgrLKVVTEPTPWPGG---IVGV-NSFGFGGANA 39
PRK05790 PRK05790
putative acyltransferase; Provisional
245-322 6.95e-03

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 38.59  E-value: 6.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644341  245 RP-FDKsrDGFV-------MGEGAAVLLLEELEHARARGAPILAEILGYGLSGdayhiTSPSDDGAGATLAMKRAIQDAG 316
Cdd:PRK05790 233 RPaFDK--DGTVtagnasgINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAG-----VDPAIMGIGPVPAIRKALEKAG 305

                 ....*.
gi 24644341  317 IAPEDV 322
Cdd:PRK05790 306 WSLADL 311
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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