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Database: UniProt
Entry: Q8X9B6
LinkDB: Q8X9B6
Original site: Q8X9B6 
ID   ACCC_ECO57              Reviewed;         449 AA.
AC   Q8X9B6;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   05-DEC-2018, entry version 114.
DE   RecName: Full=Biotin carboxylase;
DE            EC=6.3.4.14;
DE   AltName: Full=Acetyl-CoA carboxylase subunit A;
DE            Short=ACC;
DE            EC=6.4.1.2;
GN   Name=accC; OrderedLocusNames=Z4616, ECs4128;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin
CC       carboxyl carrier protein, biotin carboxylase and the two subunits
CC       of carboxyl transferase in a 2:2 complex. {ECO:0000250}.
DR   EMBL; AE005174; AAG58384.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37551.1; -; Genomic_DNA.
DR   PIR; D85990; D85990.
DR   PIR; H91144; H91144.
DR   RefSeq; NP_312155.1; NC_002695.1.
DR   RefSeq; WP_000884642.1; NZ_NOKN01000002.1.
DR   ProteinModelPortal; Q8X9B6; -.
DR   SMR; Q8X9B6; -.
DR   STRING; 155864.Z4616; -.
DR   PRIDE; Q8X9B6; -.
DR   EnsemblBacteria; AAG58384; AAG58384; Z4616.
DR   EnsemblBacteria; BAB37551; BAB37551; BAB37551.
DR   GeneID; 916024; -.
DR   KEGG; ece:Z4616; -.
DR   KEGG; ecs:ECs4128; -.
DR   PATRIC; fig|386585.9.peg.4311; -.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   HOGENOM; HOG000008988; -.
DR   KO; K01961; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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;
KW   ATP-binding; Biotin; Complete proteome; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    449       Biotin carboxylase.
FT                                /FTId=PRO_0000146792.
FT   DOMAIN        1    445       Biotin carboxylation.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   ACT_SITE    292    292       {ECO:0000255}.
FT   BINDING     116    116       ATP. {ECO:0000250}.
FT   BINDING     201    201       ATP. {ECO:0000250}.
FT   BINDING     236    236       ATP. {ECO:0000250}.
SQ   SEQUENCE   449 AA;  49337 MW;  BC5716323F6233ED CRC64;
     MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY
     LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI
     AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ
     SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NSIYLAERDC SMQRRHQKVV
     EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT
     EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP
     GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL
     QIRIMNDENF QHGGTNIHYL EKKLGLQEK
//
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