ID   ACCA_BLOPB              Reviewed;         319 AA.
AC   Q493B6;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=BPEN_295;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40926.1; -; Genomic_DNA.
DR   RefSeq; YP_277799.1; -.
DR   SMR; Q493B6; 19-318.
DR   GeneID; 3562840; -.
DR   GenomeReviews; CP000016_GR; BPEN_295.
DR   KEGG; bpn:BPEN_295; -.
DR   HOGENOM; Q493B6; -.
DR   OMA; Q493B6; HSVYTVA.
DR   BioCyc; CBLO291272:BPEN_295-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    319       Acetyl-coenzyme A carboxylase carboxyl
FT                                transferase subunit alpha.
FT                                /FTId=PRO_0000223738.
SQ   SEQUENCE   319 AA;  35643 MW;  DF6DC76AB1D01BA8 CRC64;
     MGLNVLDFEK PILDLEEKIN SLTSIVHSDK KSKKNVNAEI NRLRSKSIEL TQKIFSNLNA
     WQVAQLARHP RRPYTLDYIE RIFNDFDELS GDRVYADDKA IVGGIARLNS RPVMIIGHQK
     GRDTKEKIKR NFGMSAPEGY RKALRLMKMA ERFKIPLITF IDTPGAYPGV GAEKRGQSAA
     IAKNLRTMSI LKIPIICTVI GEGGSGGALA ISVGDKVNML EYSTYSVISP EGCASILWKN
     VKKAPIAAEA MGITAYRLKE LNLIDSVISE PLGGAHRDIL TTSISLKTQL LLDLTELDSF
     DEKELLNRRY QRLMHYGYC
//