ID   ACCA_ANAVT              Reviewed;         326 AA.
AC   Q3MA36;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Ava_2535;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000117; ABA22150.1; -; Genomic_DNA.
DR   RefSeq; YP_323045.1; -.
DR   GeneID; 3682420; -.
DR   GenomeReviews; CP000117_GR; Ava_2535.
DR   KEGG; ava:Ava_2535; -.
DR   NMPDR; fig|240292.3.peg.2016; -.
DR   HOGENOM; Q3MA36; -.
DR   OMA; Q3MA36; HSVYTVA.
DR   BioCyc; AVAR240292:AVA_2535-MON; -.
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    326       Acetyl-coenzyme A carboxylase carboxyl
FT                                transferase subunit alpha.
FT                                /FTId=PRO_1000062574.
SQ   SEQUENCE   326 AA;  35699 MW;  2B60D30FF39CF693 CRC64;
     MATTERKPLL LDFEKPLAEL ANRIDQIRQL AEENGVDVSG EIRKLETRAM QLREEIFSTL
     SPSQRLQVAR HPRRPSTLDY IQAISDEWME LHGDRCGGDD PALIGGVARL GGKPVVMLGH
     QKGRDTKDNI ARNFGMATPG GYRKAMRLME HANKFSMPIL TFIDTPGALP TVVAERQGAG
     EAIAYNLREM FSLDVPIICT VIGEGGSGGA LGIGVGDRLL MFEHSVYTVA TPEACAAILW
     KDASKSPQAA VALKIVSHDL KNLGIIDQIL PEPTGGAHSD PLTAATTLKQ ALLDNLDELD
     RLTSQERRQL RYDKFRKIGV FTEVAH
//