FABF_COXBU
ID FABF_COXBU Reviewed; 414 AA.
AC Q83E37;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2;
DE EC=2.3.1.179 {ECO:0000250|UniProtKB:P0AAI5};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II;
DE AltName: Full=Beta-ketoacyl-ACP synthase II;
DE Short=KAS II;
GN Name=fabF; OrderedLocusNames=CBU_0497;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Nine Mile Crazy / RSA 514;
RX PubMed=17088354; DOI=10.1128/iai.00883-06;
RA Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J.,
RA Samuel J.E., Heinzen R.A.;
RT "Proteome and antigen profiling of Coxiella burnetii developmental forms.";
RL Infect. Immun. 75:290-298(2007).
CC -!- FUNCTION: Involved in the type II fatty acid elongation cycle.
CC Catalyzes the elongation of a wide range of acyl-ACP by the addition of
CC two carbons from malonyl-ACP to an acyl acceptor. Can efficiently
CC catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP)
CC to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in
CC the thermal regulation of fatty acid composition.
CC {ECO:0000250|UniProtKB:P0AAI5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC Evidence={ECO:0000250|UniProtKB:P0AAI5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-
CC octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:55040,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989,
CC ChEBI:CHEBI:138538; EC=2.3.1.179;
CC Evidence={ECO:0000250|UniProtKB:P0AAI5};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P0AAI5}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AAI5}.
CC -!- DEVELOPMENTAL STAGE: More than twofold more abundant in the large cell
CC variant (LCV) stage than in the small cell variant (SCV) stage (at
CC protein level). LCVs are more metabolically active than SCVs.
CC {ECO:0000269|PubMed:17088354}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; AE016828; AAO90045.1; -; Genomic_DNA.
DR RefSeq; NP_819531.1; NC_002971.3.
DR RefSeq; WP_010957615.1; NZ_CCYB01000053.1.
DR AlphaFoldDB; Q83E37; -.
DR SMR; Q83E37; -.
DR STRING; 227377.CBU_0497; -.
DR EnsemblBacteria; AAO90045; AAO90045; CBU_0497.
DR GeneID; 1208381; -.
DR KEGG; cbu:CBU_0497; -.
DR PATRIC; fig|227377.7.peg.488; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_6; -.
DR OMA; QIGHCLG; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712; PTHR11712; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000447; KAS_II; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR03150; fabF; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..414
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT /id="PRO_0000324814"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ SEQUENCE 414 AA; 44075 MW; 217D267AA6C2547E CRC64;
MEKRRVVITG LGVVSPLGNK VSDMWQALLA GKSGVKPITR FDASSFPTQI AAEVRDFDPA
LVLDLKSIRK TDVFVQFAME SARQAWEDSG LEINETNAPR VGVAIGSGIG GMPWIEKNYD
ALLTSGPRKI SPFFIPGAII NMASGMVSIK YDLKGPNISI VTACTTGLHN IGHAARMIAH
NDADAMIAGG TEMASTPLGI GGFAAVRALS TRNDEPEKAS RPWDKGRDGF VLGEGAACVV
VEELEHAKKR NATIYAEIIG FGMSGDAYHM TRPDPEAEGF TTCMKNSLRD AGIAPERVDY
INAHGTSTPA ADPLEARAIK KTFGDHAYKL AVSSTKSMTG HMLGAAGALE TVISVLAIRD
NTAPPTINLE NPDEGCDLDF VPNEAREMKI DTVMSNSFGF GGTNGTLVLS RVFD
