ID BCCP_ECOLI Reviewed; 156 AA. AC P0ABD8; P02905; Q2M8W0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 16-DEC-2008, entry version 32. DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase; DE Short=BCCP; GN Name=accB; Synonyms=fabE; OrderedLocusNames=b3255, JW3223; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=89282408; PubMed=2660106; DOI=10.1093/nar/17.10.3982; RA Muramatsu S., Mizuno T.; RT "Nucleotide sequence of the fabE gene and flanking regions containing RT a bent DNA sequence of Escherichia coli."; RL Nucleic Acids Res. 17:3982-3982(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90126231; PubMed=2575489; RA Alix J.-H.; RT "A rapid procedure for cloning genes from lambda libraries by RT complementation of E. coli defective mutants: application to the fabE RT region of the E. coli chromosome."; RL DNA 8:779-789(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=92112819; PubMed=1370469; RA Li S.-J., Cronan J.E. Jr.; RT "The gene encoding the biotin carboxylase subunit of Escherichia coli RT acetyl-CoA carboxylase."; RL J. Biol. Chem. 267:855-863(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RA Best E.A., Knauf V.C.; RT "Cloning and characterization of the E. coli fabEG operon encoding RT subunits of acetyl-CoA carboxylase."; RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25. RX MEDLINE=93123150; PubMed=7678242; RA Li S.-J., Cronan J.E. Jr.; RT "Growth rate regulation of Escherichia coli acetyl coenzyme A RT carboxylase, which catalyzes the first committed step of lipid RT biosynthesis."; RL J. Bacteriol. 175:332-340(1993). RN [8] RP PROTEIN SEQUENCE OF 1-4. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=98263247; PubMed=9600841; DOI=10.1006/jmbi.1998.1726; RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., RA Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., RA Williams K.L., Hochstrasser D.F.; RT "Protein identification with N and C-terminal sequence tags in RT proteome projects."; RL J. Mol. Biol. 278:599-608(1998). RN [9] RP PROTEIN SEQUENCE OF 75-156. RX MEDLINE=77187896; PubMed=324999; RA Sutton M.R., Fall R.R., Nervi A.M., Alberts A.W., Vagelos P.R., RA Bradshaw R.A.; RT "Amino acid sequence of Escherichia coli biotin carboxyl carrier RT protein (9100)."; RL J. Biol. Chem. 252:3934-3940(1977). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-156. RC STRAIN=K12; RX MEDLINE=92052166; PubMed=1682920; RA Kondo H., Shiratsuchi K., Yoshimoto T., Masuda T., Kitazono A., RA Tsuru D., Anai M., Sekiguchi M., Tanabe T.; RT "Acetyl-CoA carboxylase from Escherichia coli: gene organization and RT nucleotide sequence of the biotin carboxylase subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9730-9733(1991). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-156. RX MEDLINE=96363677; PubMed=8747466; DOI=10.1016/S0969-2126(01)00277-5; RA Athappilly F.K., Hendrickson W.A.; RT "Structure of the biotinyl domain of acetyl-coenzyme A carboxylase RT determined by MAD phasing."; RL Structure 3:1407-1419(1995). RN [12] RP STRUCTURE BY NMR OF 70-156. RX MEDLINE=98060761; PubMed=9398236; DOI=10.1021/bi971485f; RA Yao X., Wei D., Soden C. Jr., Summers M.F., Beckett D.; RT "Structure of the carboxy-terminal fragment of the apo-biotin carboxyl RT carrier subunit of Escherichia coli acetyl-CoA carboxylase."; RL Biochemistry 36:15089-15100(1997). RN [13] RP STRUCTURE BY NMR OF 77-156. RX MEDLINE=99230195; PubMed=10213607; DOI=10.1021/bi982466o; RA Roberts E.L., Shu N., Howard M.J., Broadhurst R.W., Chapman-Smith A., RA Wallace J.C., Morris T., Cronan J.E. Jr., Perham R.N.; RT "Solution structures of apo and holo biotinyl domains from acetyl RT coenzyme A carboxylase of Escherichia coli determined by triple- RT resonance nuclear magnetic resonance spectroscopy."; RL Biochemistry 38:5045-5053(1999). 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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Contains 1 biotinyl-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14825; CAA32933.1; -; Genomic_DNA. DR EMBL; M80458; AAA23408.1; -; Genomic_DNA. DR EMBL; M32214; AAA23744.1; -; Genomic_DNA. DR EMBL; M83198; AAA23745.1; -; Genomic_DNA. DR EMBL; U18997; AAA58058.1; -; Genomic_DNA. DR EMBL; U00096; AAC76287.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77296.1; -; Genomic_DNA. DR EMBL; S52932; AAB24892.1; -; mRNA. DR EMBL; M79446; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A93687; BKEC9. DR RefSeq; AP_003795.1; -. DR RefSeq; NP_417721.1; -. DR PDB; 1A6X; NMR; -; A=70-156. DR PDB; 1BDO; X-ray; 1.80 A; A=77-156. DR PDB; 1K67; Model; -; B=77-155. DR PDB; 1K69; Model; -; B=77-156. DR PDB; 2BDO; NMR; -; A=77-156. DR PDB; 3BDO; NMR; -; A=75-156. DR PDBsum; 1A6X; -. DR PDBsum; 1BDO; -. DR PDBsum; 1K67; -. DR PDBsum; 1K69; -. DR PDBsum; 2BDO; -. DR PDBsum; 3BDO; -. DR DisProt; DP00415; -. DR SWISS-2DPAGE; P0ABD8; -. DR GeneID; 947758; -. DR GenomeReviews; AP009048_GR; JW3223. DR GenomeReviews; U00096_GR; b3255. DR KEGG; ecj:JW3223; -. DR KEGG; eco:b3255; -. DR EchoBASE; EB0271; -. DR EcoGene; EG10275; accB. DR HOGENOM; P0ABD8; -. DR BioCyc; EcoCyc:BCCP-MON; -. DR LinkHub; P0ABD8; -. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro. DR GO; GO:0009374; F:biotin binding; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR InterPro; IPR001249; AcCoA_biotinCC. DR InterPro; IPR001882; Biotin_BS. DR InterPro; IPR000089; Biotin_lipoyl. DR Pfam; PF00364; Biotin_lipoyl; 1. DR PRINTS; PR01071; ACOABIOTINCC. DR TIGRFAMs; TIGR00531; BCCP; 1. DR PROSITE; PS00188; BIOTIN; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. PE 1: Evidence at protein level; KW 3D-structure; Biotin; Complete proteome; Direct protein sequencing; KW Fatty acid biosynthesis; Lipid synthesis. FT CHAIN 1 156 Biotin carboxyl carrier protein of FT acetyl-CoA carboxylase. FT /FTId=PRO_0000146805. FT DOMAIN 81 155 Biotinyl-binding. FT BINDING 122 122 Biotin (covalent). FT CONFLICT 113 113 D -> N (in Ref. 2). FT STRAND 80 84 FT STRAND 86 96 FT STRAND 114 120 FT STRAND 123 128 FT STRAND 133 138 FT STRAND 151 155 SQ SEQUENCE 156 AA; 16687 MW; 05FFDCB912A683A3 CRC64; MDIRKIKKLI ELVEESGISE LEISEGEESV RISRAAPAAS FPVMQQAYAA PMMQQPAQSN AAAPATVPSM EAPAAAEISG HIVRSPMVGT FYRTPSPDAK AFIEVGQKVN VGDTLCIVEA MKMMNQIEAD KSGTVKAILV ESGQPVEFDE PLVVIE //