(data stored in SCRATCH zone)

SWISSPROT: ACCC1_BACSU

ID   ACCC1_BACSU             Reviewed;         450 AA.
AC   P49787;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   11-DEC-2019, entry version 149.
DE   RecName: Full=Biotin carboxylase 1;
DE            EC=6.3.4.14;
DE   AltName: Full=Acetyl-CoA carboxylase subunit A 1;
DE            Short=ACC 1;
DE            EC=6.4.1.2;
GN   Name=accC1; Synonyms=accC, yqhX; OrderedLocusNames=BSU24340;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7592499; DOI=10.1128/jb.177.23.7003-7006.1995;
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 carboxylase,
RT   the first enzyme of fatty acid synthesis.";
RL   J. Bacteriol. 177:7003-7006(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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).
RN   [4]
RP   SEQUENCE REVISION TO 107 AND 193.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC         CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC       carrier protein, biotin carboxylase and the two subunits of carboxyl
CC       transferase in a 2:2 complex. {ECO:0000250}.
CC   -!- CAUTION: Leu-235 is present instead of the conserved His which is
CC       expected to bind ATP. {ECO:0000305}.
DR   EMBL; U36245; AAB00183.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12569.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14365.2; -; Genomic_DNA.
DR   PIR; A69581; A69581.
DR   RefSeq; NP_390314.2; NC_000964.3.
DR   RefSeq; WP_003230253.1; NZ_JNCM01000036.1.
DR   SMR; P49787; -.
DR   IntAct; P49787; 1.
DR   MINT; P49787; -.
DR   STRING; 224308.BSU24340; -.
DR   jPOST; P49787; -.
DR   PaxDb; P49787; -.
DR   PRIDE; P49787; -.
DR   EnsemblBacteria; CAB14365; CAB14365; BSU24340.
DR   GeneID; 938588; -.
DR   KEGG; bsu:BSU24340; -.
DR   PATRIC; fig|224308.179.peg.2652; -.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   HOGENOM; HOG000008988; -.
DR   InParanoid; P49787; -.
DR   KO; K01961; -.
DR   OMA; FVEICSH; -.
DR   PhylomeDB; P49787; -.
DR   BioCyc; BSUB:BSU24340-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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.
PE   3: Inferred from homology;
DR   PRODOM; P49787.
DR   SWISS-2DPAGE; P49787.
KW   ATP-binding; Biotin; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Ligase; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..450
FT                   /note="Biotin carboxylase 1"
FT                   /id="PRO_0000146789"
FT   DOMAIN          1..447
FT                   /note="Biotin carboxylation"
FT   DOMAIN          120..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        107
FT                   /note="A -> P (in Ref. 2; BAA12569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="G -> R (in Ref. 2; BAA12569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="E -> G (in Ref. 1; AAB00183)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="D -> G (in Ref. 1; AAB00183)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344..348
FT                   /note="NPSKN -> TQVK (in Ref. 1; AAB00183)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        357..362
FT                   /note="KMYLPP -> NVPAS (in Ref. 1; AAB00183)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409..410
FT                   /note="SE -> QQ (in Ref. 1; AAB00183)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  49452 MW;  2F93B3E793478334 CRC64;
     MIKKLLIANR GEIAVRIIRA CRELGIETVA VYSEADKDAL HVQMADEAFC IGPKASKDSY
     LNVTNIVSVA KLTGTDAIHP GYGFLAENAD FAELCEEVNV TFVGPSADAI SKMGTKDVAR
     ETMKQAGVPI VPGSQGIIEN VEEAVSLANE IGYPVIIKAT AGGGGKGIRV ARTEEELING
     IKITQQEAAT AFGNPGVYIE 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
//

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