ID   ACCA_CHLFF              Reviewed;         324 AA.
AC   Q253Y8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=CF0628;
OS   Chlamydophila felis (strain Fe/C-56).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H.,
RA   Fukushi H., Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(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; AP006861; BAE81400.1; -; Genomic_DNA.
DR   RefSeq; YP_515545.1; -.
DR   GeneID; 3958640; -.
DR   GenomeReviews; AP006861_GR; CF0628.
DR   KEGG; cfe:CF0628; -.
DR   HOGENOM; Q253Y8; -.
DR   OMA; Q253Y8; PKKNSEA.
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    324       Acetyl-coenzyme A carboxylase carboxyl
FT                                transferase subunit alpha.
FT                                /FTId=PRO_1000062603.
SQ   SEQUENCE   324 AA;  36403 MW;  3CE8886AAAD41D08 CRC64;
     MELLPHEKQV VEYEKTIAEF KEKNKKNSLL SSSEIQKLER RLDKLKEKIY SDLTPWERVQ
     ICRHPSRPRS VNYIEGMCEE FVELCGDRTF RDDPAVVGGL AKINGQRFML IGQEKGCDTS
     SRMHRNFGML CPEGFRKALR LAKMAEKFGL PIVFLVDTPG AFPGLTAEAR GQGWAIANNL
     FQLARLKTPI IVLVIGEGCS GGALGMAIGD VIAMLEHSYY SVISPEGCAS ILWKDPKKNS
     EAAAMLKMHG EDLKQFAIVD VVIKEPVGGA HHNPSAVYRD VQNFILQEWL RLKDLSIEDL
     LEKRYQKFRT IGLYETSSES GPEA
//