ID   ACCA_ACAM1              Reviewed;         325 AA.
AC   B0CF67;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 12.
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=AM1_5633;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M.,
RA   Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J.,
RA   Mimuro M., Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW30583.1; -; Genomic_DNA.
DR   RefSeq; YP_001519902.1; -.
DR   GeneID; 5684423; -.
DR   GenomeReviews; CP000828_GR; AM1_5633.
DR   KEGG; amr:AM1_5633; -.
DR   OMA; B0CF67; 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    325       Acetyl-coenzyme A carboxylase carboxyl
FT                                transferase subunit alpha.
FT                                /FTId=PRO_1000083917.
SQ   SEQUENCE   325 AA;  36099 MW;  F4AE7CA05BE3FD42 CRC64;
     MAVSDRKLQL LDFEKPLAEL EDRIEQIRSL SEQNGVDVTD QIAQLEGRAE QLRQEIFSSL
     TPMQELQLAR HPRRPSTLDY IHAISDEWME LHGDRRGYDD PAIVGGVGRI GGQPVLMLGH
     QKGRDTKDNV ARNFGMPFPS GYRKAMRLMD HADRFGLPII SFIDTPAAWA GLEAEQFGQG
     EAIALNLREM FRLDVPIICT VIGEGGSGGA LGIGVGDRLL MFEHSIYSVA PPEACAAILW
     RDAQEGPQAA EALKITATDL QELGIIDQIL PEPPGGAHVN PIKAANIIKT AILSNLEELW
     RLSPQERRQQ RYHKFRNMGI FSQLP
//