ID   ACCC_BACHD     STANDARD;      PRT;   452 AA.
AC   Q9KDS9;
DT   29-MAR-2004 (Rel. 43, Created)
DT   29-MAR-2004 (Rel. 43, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Biotin carboxylase (EC 6.3.4.14) (A subunit of acetyl-CoA carboxylase)
DE   (EC 6.4.1.2) (ACC).
GN   Name=accC; OrderedLocusNames=BH1132;
OS   Bacillus halodurans.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=86665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-125 / JCM 9153;
RX   MEDLINE=20512582; PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA   Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA   Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT   halodurans and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + biotin-carboxyl-carrier protein + CO(2)
CC       = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
CC   -!- PATHWAY: Long-chain fatty acid biosynthesis; first step.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is an heterohexamer of biotin
CC       carboxyl carrier protein, biotin carboxylase and the two subunits
CC       of carboxyl transferase in a 2:2 complex (By similarity).
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC   -!- SIMILARITY: Contains 1 biotin carboxylation domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AP001511; BAB04851.1; -.
DR   PIR; D83791; D83791.
DR   HSSP; P24182; 1BNC.
DR   InterPro; IPR005482; Biotin_carb_C.
DR   InterPro; IPR005481; CPase_L_N.
DR   InterPro; IPR005479; Cphp_synth_L_D2.
DR   InterPro; IPR011054; Rudmnt_hyb_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; CPSase_L_chain; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
KW   ATP-binding; Biotin; Complete proteome; Fatty acid biosynthesis;
KW   Ligase.
FT   DOMAIN        1    445       Biotin carboxylation.
FT   NP_BIND     116    116       ATP (By similarity).
FT   DOMAIN      120    317       ATP-grasp.
FT   NP_BIND     200    200       ATP (By similarity).
FT   NP_BIND     235    235       ATP (By similarity).
FT   ACT_SITE    292    292       By similarity.
SQ   SEQUENCE   452 AA;  49938 MW;  4BCF230D1A44E880 CRC64;
     MFKKVLIANR GEIAVRIIRT CQKLNIRTVA IYSEADVDSL HVKHADEAFL IGKPPVAESY
     LKVDTILEVA KQAGVDAIHP GYGLLSENAR FARACVEAGI SFIGPSPEVI ERMGSKIAAR
     TAMQTAGVPV IPGSDVALAD EEEAVHLARK FGYPVMLKAS AGGGGIGMQL VRNDEEMRKA
     FAGNQKRATS FFGDGTMFLE KAVENPRHIE VQIAADHHGH VVHLWERDCS IQRRHQKVVE
     EAPSPFVDEA LREKIGQLAV KAAKAIDYRN LGTVECLVDG EKNIYFLEMN TRLQVEHPVT
     EEITGIDLVE WQLLIAAGEQ LPYAQHEIPL QGHAIEVRIY AEDPVTFFPS PGMIKRFTLP
     EGEGIRHEYA ISEGYKVTPF YDPMVAKLIV SADTRGEAIQ RLGRALKQYE IEGIKTNIPM
     LKQVINHPVF QAGEATTAFV TNHLKVKTGR NP
//