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Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (ACCase subunit alpha) (Acetyl-CoA carboxylase carboxyltransferase subunit alpha) (EC 6.4.1.2)

 ACCA_ECOLI              Reviewed;         319 AA.
P0ABD5; P30867;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-JUN-2018, entry version 119.
RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
Short=ACCase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_00823, ECO:0000269|PubMed:15066985};
Name=accA {ECO:0000255|HAMAP-Rule:MF_00823};
OrderedLocusNames=b0185, JW0180;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=1355089;
Li S.-J., Cronan J.E. Jr.;
"The genes encoding the two carboxyltransferase subunits of
Escherichia coli acetyl-CoA carboxylase.";
J. Biol. Chem. 267:16841-16847(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9339543; DOI=10.1266/ggs.72.167;
Yamamoto Y., Miwa Y., Miyoshi K., Furuyama J., Ohmori H.;
"The Escherichia coli ldcC gene encodes another lysine decarboxylase,
probably a constitutive enzyme.";
Genes Genet. Syst. 72:167-172(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
4.0 - 6.0 min (189,987 - 281,416bp) region.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
TO 24.
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-319.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9226257; DOI=10.1128/jb.179.14.4486-4492.1997;
Kikuchi Y., Kojima H., Tanaka T., Takatsuka Y., Kamio Y.;
"Characterization of a second lysine decarboxylase isolated from
Escherichia coli.";
J. Bacteriol. 179:4486-4492(1997).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
PubMed=3316192; DOI=10.1128/jb.169.12.5735-5744.1987;
Tomasiewicz H.G., McHenry C.S.;
"Sequence analysis of the Escherichia coli dnaE gene.";
J. Bacteriol. 169:5735-5744(1987).
[9]
PROTEIN SEQUENCE OF 2-13.
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).
[10]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
ENZYME REGULATION.
PubMed=15066985; DOI=10.1074/jbc.M402989200;
Freiberg C., Brunner N.A., Schiffer G., Lampe T., Pohlmann J.,
Brands M., Raabe M., Haebich D., Ziegelbauer K.;
"Identification and characterization of the first class of potent
bacterial acetyl-CoA carboxylase inhibitors with antibacterial
activity.";
J. Biol. Chem. 279:26066-26073(2004).
[11]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
PubMed=16460018; DOI=10.1021/bi0520479;
Bilder P., Lightle S., Bainbridge G., Ohren J., Finzel B., Sun F.,
Holley S., Al-Kassim L., Spessard C., Melnick M., Newcomer M.,
Waldrop G.L.;
"The structure of the carboxyltransferase component of acetyl-coA
carboxylase reveals a zinc-binding motif unique to the bacterial
enzyme.";
Biochemistry 45:1712-1722(2006).
-!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC)
complex. First, biotin carboxylase catalyzes the carboxylation of
biotin on its carrier protein (BCCP) and then the CO(2) group is
transferred by the carboxyltransferase to acetyl-CoA to form
malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00823,
ECO:0000269|PubMed:15066985}.
-!- CATALYTIC ACTIVITY: [Biotin carboxyl-carrier protein]-N(6)-
carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier
protein]-N(6)-biotinyl-L-lysine + malonyl-CoA. {ECO:0000255|HAMAP-
Rule:MF_00823, ECO:0000269|PubMed:15066985}.
-!- ENZYME REGULATION: Competitively inhibited by pyrrolidine dione
antibiotic moiramide B (CPD1). {ECO:0000269|PubMed:15066985}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=100 uM for malonyl-CoA {ECO:0000269|PubMed:15066985};
KM=10 mM for biocytin {ECO:0000269|PubMed:15066985};
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00823}.
-!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of
biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC)
and two subunits each of ACCase subunit alpha (AccA) and ACCase
subunit beta (AccD).
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-542031, EBI-542031;
P0A9Q5:accD; NbExp=17; IntAct=EBI-542031, EBI-542064;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP-
Rule:MF_00823}.
-----------------------------------------------------------------------
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EMBL; M96394; AAA70370.1; -; Genomic_DNA.
EMBL; D49445; BAA08425.1; -; Genomic_DNA.
EMBL; U70214; AAB08614.1; -; Genomic_DNA.
EMBL; U00096; AAC73296.1; -; Genomic_DNA.
EMBL; AP009048; BAA77860.2; -; Genomic_DNA.
EMBL; D87518; BAA21655.1; -; Genomic_DNA.
EMBL; M19334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A43452; A43452.
RefSeq; NP_414727.1; NC_000913.3.
RefSeq; WP_000055741.1; NZ_LN832404.1.
PDB; 2F9Y; X-ray; 3.20 A; A=1-319.
PDBsum; 2F9Y; -.
ProteinModelPortal; P0ABD5; -.
SMR; P0ABD5; -.
BioGrid; 4259753; 211.
ComplexPortal; CPX-3206; Acetyl-CoA carboxylase complex.
DIP; DIP-35897N; -.
IntAct; P0ABD5; 32.
MINT; P0ABD5; -.
STRING; 316385.ECDH10B_0165; -.
EPD; P0ABD5; -.
PaxDb; P0ABD5; -.
PRIDE; P0ABD5; -.
EnsemblBacteria; AAC73296; AAC73296; b0185.
EnsemblBacteria; BAA77860; BAA77860; BAA77860.
GeneID; 944895; -.
KEGG; ecj:JW0180; -.
KEGG; eco:b0185; -.
PATRIC; fig|1411691.4.peg.2094; -.
EchoBASE; EB1600; -.
EcoGene; EG11647; accA.
eggNOG; ENOG4107QM9; Bacteria.
eggNOG; COG0825; LUCA.
HOGENOM; HOG000273832; -.
InParanoid; P0ABD5; -.
KO; K01962; -.
OMA; CSSILWR; -.
PhylomeDB; P0ABD5; -.
BioCyc; EcoCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER; -.
BioCyc; MetaCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER; -.
SABIO-RK; P0ABD5; -.
UniPathway; UPA00655; UER00711.
EvolutionaryTrace; P0ABD5; -.
PRO; PR:P0ABD5; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009329; C:acetate CoA-transferase complex; IDA:EcoCyc.
GO; GO:0005737; C:cytoplasm; IC:EcoliWiki.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; NAS:EcoliWiki.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
InterPro; IPR001095; Acetyl_CoA_COase_a_su.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR011763; COA_CT_C.
PANTHER; PTHR42853; PTHR42853; 1.
Pfam; PF03255; ACCA; 1.
PRINTS; PR01069; ACCCTRFRASEA.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR00513; accA; 1.
PROSITE; PS50989; COA_CT_CTER; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
Nucleotide-binding; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298646}.
CHAIN 2 319 Acetyl-coenzyme A carboxylase carboxyl
transferase subunit alpha.
/FTId=PRO_0000146774.
DOMAIN 35 296 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
HELIX 10 14 {ECO:0000244|PDB:2F9Y}.
TURN 15 20 {ECO:0000244|PDB:2F9Y}.
HELIX 39 43 {ECO:0000244|PDB:2F9Y}.
HELIX 44 48 {ECO:0000244|PDB:2F9Y}.
TURN 49 52 {ECO:0000244|PDB:2F9Y}.
HELIX 53 56 {ECO:0000244|PDB:2F9Y}.
HELIX 60 67 {ECO:0000244|PDB:2F9Y}.
HELIX 75 82 {ECO:0000244|PDB:2F9Y}.
STRAND 84 88 {ECO:0000244|PDB:2F9Y}.
STRAND 93 95 {ECO:0000244|PDB:2F9Y}.
STRAND 101 108 {ECO:0000244|PDB:2F9Y}.
STRAND 111 118 {ECO:0000244|PDB:2F9Y}.
HELIX 126 129 {ECO:0000244|PDB:2F9Y}.
HELIX 131 133 {ECO:0000244|PDB:2F9Y}.
HELIX 137 152 {ECO:0000244|PDB:2F9Y}.
STRAND 157 164 {ECO:0000244|PDB:2F9Y}.
HELIX 170 174 {ECO:0000244|PDB:2F9Y}.
HELIX 177 189 {ECO:0000244|PDB:2F9Y}.
STRAND 195 204 {ECO:0000244|PDB:2F9Y}.
HELIX 205 209 {ECO:0000244|PDB:2F9Y}.
STRAND 215 219 {ECO:0000244|PDB:2F9Y}.
STRAND 224 228 {ECO:0000244|PDB:2F9Y}.
HELIX 230 237 {ECO:0000244|PDB:2F9Y}.
HELIX 244 251 {ECO:0000244|PDB:2F9Y}.
HELIX 255 259 {ECO:0000244|PDB:2F9Y}.
TURN 260 262 {ECO:0000244|PDB:2F9Y}.
HELIX 275 277 {ECO:0000244|PDB:2F9Y}.
HELIX 279 293 {ECO:0000244|PDB:2F9Y}.
TURN 294 299 {ECO:0000244|PDB:2F9Y}.
HELIX 302 315 {ECO:0000244|PDB:2F9Y}.
SEQUENCE 319 AA; 35242 MW; A810DE891CEA2B4F CRC64;
MSLNFLDFEQ PIAELEAKID SLTAVSRQDE KLDINIDEEV HRLREKSVEL TRKIFADLGA
WQIAQLARHP QRPYTLDYVR LAFDEFDELA GDRAYADDKA IVGGIARLDG RPVMIIGHQK
GRETKEKIRR NFGMPAPEGY RKALRLMQMA ERFKMPIITF IDTPGAYPGV GAEERGQSEA
IARNLREMSR LGVPVVCTVI GEGGSGGALA IGVGDKVNML QYSTYSVISP EGCASILWKS
ADKAPLAAEA MGIIAPRLKE LKLIDSIIPE PLGGAHRNPE AMAASLKAQL LADLADLDVL
STEDLKNRRY QRLMSYGYA


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