ID   ACCA_BORA1              Reviewed;         321 AA.
AC   Q2KX40;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha;
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha;
DE            Short=ACCase subunit alpha;
DE            EC=6.4.1.2;
GN   Name=accA; OrderedLocusNames=BAV2560;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC)
CC       complex. First, biotin carboxylase catalyzes the carboxylation of
CC       biotin on its carrier protein (BCCP) and then the CO(2) group is
CC       transferred by the carboxyltransferase to acetyl-CoA to form
CC       malonyl-CoA (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
CC       + malonyl-CoA.
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is an heterohexamer composed of
CC       biotin carboxyl carrier protein (accB), biotin carboxylase (accC)
CC       and two subunits each of ACCase subunit alpha (accA) and ACCase
CC       subunit beta (accD) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the accA family.
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DR   EMBL; AM167904; CAJ50170.1; -; Genomic_DNA.
DR   RefSeq; YP_787068.1; -.
DR   GeneID; 6267333; -.
DR   GenomeReviews; AM167904_GR; BAV2560.
DR   KEGG; bav:BAV2560; -.
DR   NMPDR; fig|521.1.peg.242; -.
DR   HOGENOM; Q2KX40; -.
DR   OMA; Q2KX40; HSVYTVA.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00823; -; 1.
DR   InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR   InterPro; IPR011763; COA_CT_C.
DR   PANTHER; PTHR22855:SF3; Ac-CoA_carboxylA; 1.
DR   Pfam; PF03255; ACCA; 1.
DR   PRINTS; PR01069; ACCCTRFRASEA.
DR   TIGRFAMs; TIGR00513; accA; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Fatty acid biosynthesis;
KW   Ligase; Lipid synthesis; Nucleotide-binding.
FT   CHAIN         1    321       Acetyl-coenzyme A carboxylase carboxyl
FT                                transferase subunit alpha.
FT                                /FTId=PRO_1000062581.
SQ   SEQUENCE   321 AA;  35845 MW;  D6411309F209069A CRC64;
     MRNTFLEFEQ PLAELENKIE QLRYVQADSA VDISDEIGRL QQKSQTLAKE IYGKLTPWQT
     ALVARHPQRP YTLDYVREIF TDFHELHGDR MYADDQSIVG GLARFNGQSC MVIGHQKGRD
     TKERAARNFG MPRPEGYRKA QRLMRLAEKF KLPIFTFVDT PGAYPGIGAE ERGQSEAIGH
     NLYVMAELKV PVIVTIIGEG GSGGALAIAV GNAVLMLQYS TYSVISPEGC ASILWRSADK
     APEAAEALAI TAPRLKDLGL IDRVVNEPIG GAHRDPRVMA RLLRRALGDS LRQLQDLTPE
     QLVEQRLERV LAYGRFQEVR G
//