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Biotin carboxylase (EC 6.3.4.14) (Acetyl-CoA carboxylase subunit A) (ACC) (EC 6.4.1.2)

 ACCC_ECOLI              Reviewed;         449 AA.
P24182; Q2M8V9;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
22-NOV-2017, entry version 175.
RecName: Full=Biotin carboxylase;
EC=6.3.4.14;
AltName: Full=Acetyl-CoA carboxylase subunit A;
Short=ACC;
EC=6.4.1.2;
Name=accC; Synonyms=fabG; OrderedLocusNames=b3256, JW3224;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=K12;
PubMed=1682920; DOI=10.1073/pnas.88.21.9730;
Kondo H., Shiratsuchi K., Yoshimoto T., Masuda T., Kitazono A.,
Tsuru D., Anai M., Sekiguchi M., Tanabe T.;
"Acetyl-CoA carboxylase from Escherichia coli: gene organization and
nucleotide sequence of the biotin carboxylase subunit.";
Proc. Natl. Acad. Sci. U.S.A. 88:9730-9733(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1370469;
Li S.-J., Cronan J.E. Jr.;
"The gene encoding the biotin carboxylase subunit of Escherichia coli
acetyl-CoA carboxylase.";
J. Biol. Chem. 267:855-863(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Best E.A., Knauf V.C.;
"Cloning and characterization of the E. coli fabEG operon encoding
subunits of acetyl-CoA carboxylase.";
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160.
PubMed=2575489; DOI=10.1089/dna.1989.8.779;
Alix J.-H.;
"A rapid procedure for cloning genes from lambda libraries by
complementation of E. coli defective mutants: application to the fabE
region of the E. coli chromosome.";
DNA 8:779-789(1989).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=7915138; DOI=10.1021/bi00200a004;
Waldrop G.L., Rayment I., Holden H.M.;
"Three-dimensional structure of the biotin carboxylase subunit of
acetyl-CoA carboxylase.";
Biochemistry 33:10249-10256(1994).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP.
PubMed=10821865; DOI=10.1074/jbc.275.21.16183;
Thoden J.B., Blanchard C.Z., Holden H.M., Waldrop G.L.;
"Movement of the biotin carboxylase B-domain as a result of ATP
binding.";
J. Biol. Chem. 275:16183-16190(2000).
[10]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
ARG-19; GLU-23; PHE-363 AND ARG-366.
PubMed=16793549; DOI=10.1016/j.molcel.2006.04.026;
Shen Y., Chou C.-Y., Chang G.-G., Tong L.;
"Is dimerization required for the catalytic activity of bacterial
biotin carboxylase?";
Mol. Cell 22:807-818(2006).
-!- FUNCTION: This protein is a component of the acetyl coenzyme A
carboxylase complex; first, biotin carboxylase catalyzes the
carboxylation of the carrier protein and then the transcarboxylase
transfers the carboxyl group to form malonyl-CoA.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein].
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA.
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin
carboxyl carrier protein, biotin carboxylase and the two subunits
of carboxyl transferase in a 2:2 complex.
{ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:16793549}.
-!- INTERACTION:
P0ABD8:accB; NbExp=10; IntAct=EBI-542308, EBI-542320;
P0A9Q5:accD; NbExp=4; IntAct=EBI-542308, EBI-542064;
P16703:cysM; NbExp=3; IntAct=EBI-542308, EBI-542376;
P25539:ribD; NbExp=3; IntAct=EBI-542308, EBI-552457;
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M79446; AAA23748.1; -; Genomic_DNA.
EMBL; M80458; AAA23409.1; -; Genomic_DNA.
EMBL; M83198; AAA23746.1; -; Genomic_DNA.
EMBL; U18997; AAA58059.1; -; Genomic_DNA.
EMBL; U00096; AAC76288.1; -; Genomic_DNA.
EMBL; AP009048; BAE77297.1; -; Genomic_DNA.
EMBL; M32214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; JS0632; JS0632.
RefSeq; NP_417722.1; NC_000913.3.
RefSeq; WP_000884639.1; NZ_LN832404.1.
PDB; 1BNC; X-ray; 2.40 A; A/B=1-449.
PDB; 1DV1; X-ray; 1.90 A; A/B=1-449.
PDB; 1DV2; X-ray; 2.50 A; A/B=1-449.
PDB; 1K69; Model; -; A=1-447.
PDB; 2GPS; X-ray; 2.80 A; A/B=1-449.
PDB; 2GPW; X-ray; 2.20 A; A/B/C/D=1-449.
PDB; 2J9G; X-ray; 2.05 A; A/B=1-449.
PDB; 2V58; X-ray; 2.10 A; A/B=1-449.
PDB; 2V59; X-ray; 2.40 A; A/B=1-449.
PDB; 2V5A; X-ray; 2.31 A; A/B=1-449.
PDB; 2VR1; X-ray; 2.60 A; A/B=1-449.
PDB; 2W6M; X-ray; 2.00 A; A/B=1-449.
PDB; 2W6N; X-ray; 1.87 A; A/B=1-449.
PDB; 2W6O; X-ray; 2.50 A; A/C=1-449.
PDB; 2W6P; X-ray; 1.85 A; A/B=1-449.
PDB; 2W6Q; X-ray; 2.05 A; A/B=1-449.
PDB; 2W6Z; X-ray; 1.90 A; A/B=1-449.
PDB; 2W70; X-ray; 1.77 A; A/B=1-449.
PDB; 2W71; X-ray; 1.99 A; A/C=1-449.
PDB; 3G8C; X-ray; 2.00 A; A/B=1-444.
PDB; 3G8D; X-ray; 1.90 A; A/B=1-444.
PDB; 3JZF; X-ray; 2.13 A; A/B=1-449.
PDB; 3JZI; X-ray; 2.31 A; A/B=1-449.
PDB; 3RUP; X-ray; 1.99 A; A/B=1-449.
PDB; 3RV3; X-ray; 1.91 A; A/B=1-449.
PDB; 3RV4; X-ray; 1.98 A; A=1-449.
PDB; 4HR7; X-ray; 2.50 A; A/C/E/F=1-449.
PDBsum; 1BNC; -.
PDBsum; 1DV1; -.
PDBsum; 1DV2; -.
PDBsum; 1K69; -.
PDBsum; 2GPS; -.
PDBsum; 2GPW; -.
PDBsum; 2J9G; -.
PDBsum; 2V58; -.
PDBsum; 2V59; -.
PDBsum; 2V5A; -.
PDBsum; 2VR1; -.
PDBsum; 2W6M; -.
PDBsum; 2W6N; -.
PDBsum; 2W6O; -.
PDBsum; 2W6P; -.
PDBsum; 2W6Q; -.
PDBsum; 2W6Z; -.
PDBsum; 2W70; -.
PDBsum; 2W71; -.
PDBsum; 3G8C; -.
PDBsum; 3G8D; -.
PDBsum; 3JZF; -.
PDBsum; 3JZI; -.
PDBsum; 3RUP; -.
PDBsum; 3RV3; -.
PDBsum; 3RV4; -.
PDBsum; 4HR7; -.
ProteinModelPortal; P24182; -.
SMR; P24182; -.
BioGrid; 4262456; 258.
DIP; DIP-9035N; -.
IntAct; P24182; 20.
MINT; MINT-1266968; -.
STRING; 316385.ECDH10B_3431; -.
BindingDB; P24182; -.
DrugBank; DB08074; 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine.
PaxDb; P24182; -.
PRIDE; P24182; -.
EnsemblBacteria; AAC76288; AAC76288; b3256.
EnsemblBacteria; BAE77297; BAE77297; BAE77297.
GeneID; 947761; -.
KEGG; ecj:JW3224; -.
KEGG; eco:b3256; -.
PATRIC; fig|511145.12.peg.3355; -.
EchoBASE; EB0272; -.
EcoGene; EG10276; accC.
eggNOG; ENOG4105CER; Bacteria.
eggNOG; COG0439; LUCA.
HOGENOM; HOG000008988; -.
InParanoid; P24182; -.
KO; K01961; -.
PhylomeDB; P24182; -.
BioCyc; EcoCyc:BIOTIN-CARBOXYL-MONOMER; -.
BioCyc; MetaCyc:BIOTIN-CARBOXYL-MONOMER; -.
BRENDA; 6.3.4.14; 2026.
SABIO-RK; P24182; -.
UniPathway; UPA00655; UER00711.
EvolutionaryTrace; P24182; -.
PRO; PR:P24182; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IC:EcoliWiki.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004075; F:biotin carboxylase activity; IDA:EcoliWiki.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:EcoliWiki.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52440; SSF52440; 1.
TIGRFAMs; TIGR00514; accC; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00866; CPSASE_1; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Biotin; Complete proteome;
Direct protein sequencing; Fatty acid biosynthesis;
Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
Nucleotide-binding; Reference proteome.
CHAIN 1 449 Biotin carboxylase.
/FTId=PRO_0000146791.
DOMAIN 1 445 Biotin carboxylation.
DOMAIN 120 317 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
ACT_SITE 292 292 {ECO:0000255}.
BINDING 116 116 ATP. {ECO:0000269|PubMed:10821865}.
BINDING 201 201 ATP. {ECO:0000269|PubMed:10821865}.
BINDING 236 236 ATP. {ECO:0000269|PubMed:10821865}.
MUTAGEN 19 19 R->E: Loss of homodimerization. No effect
on ATP binding.
{ECO:0000269|PubMed:16793549}.
MUTAGEN 23 23 E->R: Loss of homodimerization. No effect
on ATP binding.
{ECO:0000269|PubMed:16793549}.
MUTAGEN 363 363 F->A: Loss of homodimerization. No effect
on ATP binding.
{ECO:0000269|PubMed:16793549}.
MUTAGEN 366 366 R->E: Loss of homodimerization. No effect
on ATP binding.
{ECO:0000269|PubMed:16793549}.
CONFLICT 136 136 G -> A (in Ref. 7). {ECO:0000305}.
CONFLICT 160 160 A -> P (in Ref. 7). {ECO:0000305}.
CONFLICT 260 261 CA -> SR (in Ref. 2). {ECO:0000305}.
CONFLICT 313 313 L -> M (in Ref. 1; AAA23748).
{ECO:0000305}.
STRAND 3 7 {ECO:0000244|PDB:2W70}.
HELIX 11 24 {ECO:0000244|PDB:2W70}.
STRAND 27 33 {ECO:0000244|PDB:2W70}.
HELIX 34 36 {ECO:0000244|PDB:2W70}.
HELIX 40 44 {ECO:0000244|PDB:2W70}.
STRAND 45 52 {ECO:0000244|PDB:2W70}.
HELIX 56 58 {ECO:0000244|PDB:2W70}.
TURN 59 61 {ECO:0000244|PDB:2W70}.
HELIX 63 73 {ECO:0000244|PDB:2W70}.
STRAND 77 79 {ECO:0000244|PDB:2W70}.
TURN 84 87 {ECO:0000244|PDB:2W70}.
HELIX 89 97 {ECO:0000244|PDB:2W70}.
STRAND 101 105 {ECO:0000244|PDB:2W70}.
HELIX 107 114 {ECO:0000244|PDB:2W70}.
HELIX 116 126 {ECO:0000244|PDB:2W70}.
HELIX 142 152 {ECO:0000244|PDB:2W70}.
STRAND 154 160 {ECO:0000244|PDB:2W70}.
TURN 165 168 {ECO:0000244|PDB:2W70}.
STRAND 170 172 {ECO:0000244|PDB:2W70}.
HELIX 175 193 {ECO:0000244|PDB:2W70}.
STRAND 198 202 {ECO:0000244|PDB:2W70}.
STRAND 208 216 {ECO:0000244|PDB:2W70}.
STRAND 218 220 {ECO:0000244|PDB:2W6O}.
STRAND 222 234 {ECO:0000244|PDB:2W70}.
STRAND 237 244 {ECO:0000244|PDB:2W70}.
HELIX 250 267 {ECO:0000244|PDB:2W70}.
STRAND 271 280 {ECO:0000244|PDB:2W70}.
STRAND 283 290 {ECO:0000244|PDB:2W70}.
HELIX 297 304 {ECO:0000244|PDB:2W70}.
HELIX 308 317 {ECO:0000244|PDB:2W70}.
HELIX 325 327 {ECO:0000244|PDB:2W70}.
STRAND 332 340 {ECO:0000244|PDB:2W70}.
TURN 344 346 {ECO:0000244|PDB:2W70}.
STRAND 356 358 {ECO:0000244|PDB:2W70}.
STRAND 365 368 {ECO:0000244|PDB:2W70}.
STRAND 379 381 {ECO:0000244|PDB:2W70}.
STRAND 383 394 {ECO:0000244|PDB:2W70}.
HELIX 395 408 {ECO:0000244|PDB:2W70}.
STRAND 410 414 {ECO:0000244|PDB:2W70}.
HELIX 418 425 {ECO:0000244|PDB:2W70}.
HELIX 428 432 {ECO:0000244|PDB:2W70}.
HELIX 439 444 {ECO:0000244|PDB:2W70}.
SEQUENCE 449 AA; 49321 MW; 68C55F10ACB4F170 CRC64;
MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY
LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI
AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ
SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NAIYLAERDC 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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