ID   ACCA_CHLMU              Reviewed;         324 AA.
AC   Q9PKC9;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 45.
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=TC_0536;
OS   Chlamydia muridarum.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=83560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
RA   White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
RA   Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
RA   Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
RA   McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
RT   pneumoniae AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39376.1; -; Genomic_DNA.
DR   PIR; D81691; D81691.
DR   RefSeq; NP_296913.1; -.
DR   GeneID; 1245896; -.
DR   GenomeReviews; AE002160_GR; TC_0536.
DR   KEGG; cmu:TC0536; -.
DR   TIGR; TC_0536; -.
DR   HOGENOM; Q9PKC9; -.
DR   OMA; Q9PKC9; HSVYTVA.
DR   BioCyc; CMUR243161:TC_0536-MON; -.
DR   BRENDA; 6.4.1.2; 256349.
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_0000223751.
SQ   SEQUENCE   324 AA;  36346 MW;  F0679CDAF82FC2B8 CRC64;
     MELLPHEKQV VEYEKTIADF KEKNKENSLL SSSEIQKLEN RLDRLKEKIY SNLTPWERVQ
     ICRHPSRPRT INYIEGMCEE FVELCGDRTF RDDPAVVGGF AKIQGQRFML IGQEKGCDTT
     SRMHRNFGML CPEGFRKALR LAKMAEKFGL PIIFLVDTPG AFPGLTAEER GQGWAIATNL
     FELARLATPI IVVVIGEGCS GGALGMAIGD VVAMLEHSYY SVISPEGCAS ILWKDPKKNS
     DAAAMLKMHG EDLKGFAIVD AVIKEPIGGA HHNPVATYRS VQEYVLQEWL KLKDLPVEEL
     LEKRYQKFRT IGLYETSSES SSEA
//