ID   ACCC_BACSU     STANDARD;      PRT;   450 AA.
AC   P49787;
DT   01-OCT-1996 (Rel. 34, Created)
DT   29-MAR-2004 (Rel. 43, Last sequence update)
DT   01-FEB-2005 (Rel. 46, 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=BSU24340;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=168;
RX   MEDLINE=96074336; PubMed=7592499;
RA   Marini P.E., Li S.J., Gardiol D., Cronan J.E. Jr., de Mendoza D.;
RT   "The genes encoding the biotin carboxyl carrier protein and biotin
RT   carboxylase subunits of Bacillus subtilis acetyl coenzyme A
RT   carboxylase, the first enzyme of fatty acid synthesis.";
RL   J. Bacteriol. 177:7003-7006(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=168 / JH642;
RX   MEDLINE=97124195; PubMed=8969508;
RA   Mizuno M., Masuda S., Takemaru K.-I., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of
RT   the Bacillus subtilis genome containing the skin element and many
RT   sporulation genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.K., Codani J.J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Dusterhoft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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.
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.
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; U36245; AAB00183.1; -.
DR   EMBL; D84432; BAA12569.1; -.
DR   EMBL; Z99116; CAB14365.1; -.
DR   PIR; A69581; A69581.
DR   HSSP; P24182; 1BNC.
DR   SubtiList; BG11384; accC.
DR   InterPro; IPR004549; AccC.
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   TIGRFAMs; TIGR00514; accC; 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    447       Biotin carboxylation.
FT   NP_BIND     116    116       ATP (By similarity).
FT   DOMAIN      120    318       ATP-grasp.
FT   NP_BIND     200    200       ATP (By similarity).
FT   NP_BIND     235    235       ATP (By similarity).
FT   ACT_SITE    293    293       By similarity.
FT   CONFLICT    107    107       P -> A (in Ref. 1).
FT   CONFLICT    193    193       R -> G (in Ref. 1).
FT   CONFLICT    240    240       E -> G (in Ref. 1).
FT   CONFLICT    248    248       D -> G (in Ref. 1).
FT   CONFLICT    344    348       NPSKN -> TQVK (in Ref. 1).
FT   CONFLICT    357    362       KMYLPP -> NVPAS (in Ref. 1).
FT   CONFLICT    409    410       SE -> QQ (in Ref. 1).
SQ   SEQUENCE   450 AA;  49577 MW;  95856349D2A0BC83 CRC64;
     MIKKLLIANR GEIAVRIIRA CRELGIETVA VYSEADKDAL HVQMADEAFC IGPKASKDSY
     LNVTNIVSVA KLTGTDAIHP GYGFLAENAD FAELCEEVNV TFVGPSPDAI SKMGTKDVAR
     ETMKQAGVPI VPGSQGIIEN VEEAVSLANE IGYPVIIKAT AGGGGKGIRV ARTEEELING
     IKITQQEAAT AFRNPGVYIE KYIEDFRHVE IQVLADNYGN TIHLGERDCS IQRRLQKLLE
     ESPSPALDSE IREQMGDAAV KAAKAVGYTG AGTVEFIYDY NEQRYYFMEM NTRIQVEHPV
     TEMVTGTDLI KEQIKVASGM ELSLKQEDVE FEGWAIECRI NAENPSKNFM PSPGEIKMYL
     PPGGLGVRVD SAAYPGYSIP PYYDSMIAKV ITYGKTRDEA IARMKRALSE FVIEGIETTI
     PFHLKLLEHE TFVSGEFNTK FLETYDVMGS
//