ACCD_ECOLI
ID ACCD_ECOLI Reviewed; 304 AA.
AC P0A9Q5; P08193; P76937; P78251;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01395};
GN Name=accD {ECO:0000255|HAMAP-Rule:MF_01395}; Synonyms=dedB, usg;
GN OrderedLocusNames=b2316, JW2313;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3040739; DOI=10.1016/s0021-9258(18)45358-6;
RA Bognar A.L., Osborne C., Shane B.;
RT "Primary structure of the Escherichia coli folC gene and its
RT folylpolyglutamate synthetase-dihydrofolate synthetase product and
RT regulation of expression by an upstream gene.";
RL J. Biol. Chem. 262:12337-12343(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3040734; DOI=10.1016/s0021-9258(18)45338-0;
RA Nonet M.L., Marvel C.C., Tolan D.R.;
RT "The hisT-purF region of the Escherichia coli K-12 chromosome.
RT Identification of additional genes of the hisT and purF operons.";
RL J. Biol. Chem. 262:12209-12217(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
RX PubMed=7678242; DOI=10.1128/jb.175.2.332-340.1993;
RA Li S.-J., Cronan J.E. Jr.;
RT "Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase,
RT which catalyzes the first committed step of lipid biosynthesis.";
RL J. Bacteriol. 175:332-340(1993).
RN [7]
RP SIMILARITY TO ZFPA.
RX PubMed=1886618; DOI=10.1007/bf00282448;
RA Nagano Y., Matsuno R., Sasaki Y.;
RT "An essential gene of Escherichia coli that has sequence similarity to a
RT chloroplast gene of unknown function.";
RL Mol. Gen. Genet. 228:62-64(1991).
RN [8]
RP FUNCTION.
RX PubMed=1355086; DOI=10.1128/jb.174.17.5755-5757.1992;
RA Li S.-J., Rock C.O., Cronan J.E. Jr.;
RT "The dedB (usg) open reading frame of Escherichia coli encodes a subunit of
RT acetyl-coenzyme A carboxylase.";
RL J. Bacteriol. 174:5755-5757(1992).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=15066985; DOI=10.1074/jbc.m402989200;
RA Freiberg C., Brunner N.A., Schiffer G., Lampe T., Pohlmann J., Brands M.,
RA Raabe M., Haebich D., Ziegelbauer K.;
RT "Identification and characterization of the first class of potent bacterial
RT acetyl-CoA carboxylase inhibitors with antibacterial activity.";
RL J. Biol. Chem. 279:26066-26073(2004).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RNA-BINDING, SUGGESTED
RP MECHANISM OF TRANSLATIONAL REGULATION, AND MUTAGENESIS OF CYS-27; CYS-30;
RP CYS-46 AND CYS-49.
RX PubMed=19965770; DOI=10.1093/nar/gkp1079;
RA Meades G. Jr., Benson B.K., Grove A., Waldrop G.L.;
RT "A tale of two functions: enzymatic activity and translational repression
RT by carboxyltransferase.";
RL Nucleic Acids Res. 38:1217-1227(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), AND ZINC-FINGER.
RX PubMed=16460018; DOI=10.1021/bi0520479;
RA Bilder P., Lightle S., Bainbridge G., Ohren J., Finzel B., Sun F.,
RA Holley S., Al-Kassim L., Spessard C., Melnick M., Newcomer M.,
RA Waldrop G.L.;
RT "The structure of the carboxyltransferase component of acetyl-coA
RT carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.";
RL Biochemistry 45:1712-1722(2006).
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC transcarboxylase to acetyl-CoA to form malonyl-CoA.
CC -!- FUNCTION: Controls translation of mRNA for both itself and the alpha-
CC subunit (accA) by binding to a probable hairpin in the 5' of the mRNA.
CC Binding to mRNA inhibits translation; this is partially relieved by
CC acetyl-CoA. Increasing amounts of mRNA also inhibit enzyme activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01395,
CC ECO:0000269|PubMed:19965770};
CC Note=Binds 1 zinc ion per subunit. The zinc is involved in both
CC translation regulation via mRNA-binding and catalysis.
CC {ECO:0000255|HAMAP-Rule:MF_01395, ECO:0000269|PubMed:19965770};
CC -!- ACTIVITY REGULATION: Competitively inhibited by pyrrolidine dione
CC antibiotic moiramide B (CPD1). {ECO:0000269|PubMed:15066985}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40.0 uM for malonyl-CoA {ECO:0000269|PubMed:15066985,
CC ECO:0000269|PubMed:19965770};
CC KM=11.4 mM for biocytin {ECO:0000269|PubMed:15066985,
CC ECO:0000269|PubMed:19965770};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01395}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC (AccD).
CC -!- INTERACTION:
CC P0A9Q5; P0ABD5: accA; NbExp=17; IntAct=EBI-542064, EBI-542031;
CC P0A9Q5; P24182: accC; NbExp=4; IntAct=EBI-542064, EBI-542308;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M32445; AAA23807.1; -; Genomic_DNA.
DR EMBL; J02808; AAA23801.1; -; Genomic_DNA.
DR EMBL; M68934; AAA23965.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75376.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16173.1; -; Genomic_DNA.
DR EMBL; S53037; AAB24894.2; -; mRNA.
DR PIR; B65004; XMECBD.
DR RefSeq; NP_416819.1; NC_000913.3.
DR RefSeq; WP_000118404.1; NZ_STEB01000008.1.
DR PDB; 2F9Y; X-ray; 3.20 A; B=1-304.
DR PDBsum; 2F9Y; -.
DR AlphaFoldDB; P0A9Q5; -.
DR SMR; P0A9Q5; -.
DR BioGRID; 4261361; 233.
DR BioGRID; 851137; 11.
DR ComplexPortal; CPX-3206; Acetyl-CoA carboxylase complex.
DR DIP; DIP-35878N; -.
DR IntAct; P0A9Q5; 28.
DR MINT; P0A9Q5; -.
DR STRING; 511145.b2316; -.
DR jPOST; P0A9Q5; -.
DR PaxDb; P0A9Q5; -.
DR PRIDE; P0A9Q5; -.
DR EnsemblBacteria; AAC75376; AAC75376; b2316.
DR EnsemblBacteria; BAA16173; BAA16173; BAA16173.
DR GeneID; 66673801; -.
DR GeneID; 946796; -.
DR KEGG; ecj:JW2313; -.
DR KEGG; eco:b2316; -.
DR PATRIC; fig|511145.12.peg.2411; -.
DR EchoBASE; EB0213; -.
DR eggNOG; COG0777; Bacteria.
DR HOGENOM; CLU_015486_1_0_6; -.
DR InParanoid; P0A9Q5; -.
DR OMA; PEGLWIK; -.
DR PhylomeDB; P0A9Q5; -.
DR BioCyc; EcoCyc:CARBOXYL-TRANSFERASE-BETA-MON; -.
DR BioCyc; MetaCyc:CARBOXYL-TRANSFERASE-BETA-MON; -.
DR BRENDA; 6.4.1.2; 2026.
DR SABIO-RK; P0A9Q5; -.
DR UniPathway; UPA00655; UER00711.
DR EvolutionaryTrace; P0A9Q5; -.
DR PRO; PR:P0A9Q5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009329; C:acetate CoA-transferase complex; IDA:EcoCyc.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:EcoliWiki.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IMP:EcoCyc.
DR GO; GO:0003729; F:mRNA binding; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; NAS:EcoliWiki.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0017148; P:negative regulation of translation; IDA:EcoCyc.
DR HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR041010; Znf-ACC.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF17848; zf-ACC; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00515; accD; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Metal-binding;
KW Nucleotide-binding; Reference proteome; RNA-binding; Transferase;
KW Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..304
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /id="PRO_0000199770"
FT DOMAIN 23..292
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 27..49
FT /note="C4-type"
FT /evidence="ECO:0000305"
FT REGION 284..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 27
FT /note="C->A: Vmax decreases 9-fold."
FT /evidence="ECO:0000269|PubMed:19965770"
FT MUTAGEN 30
FT /note="C->A: Vmax decreases 140-fold. Loss of nucleic acid-
FT binding."
FT /evidence="ECO:0000269|PubMed:19965770"
FT MUTAGEN 46
FT /note="C->A: Vmax decreases 11-fold."
FT /evidence="ECO:0000269|PubMed:19965770"
FT MUTAGEN 49
FT /note="C->A: Vmax decreases 8-fold."
FT /evidence="ECO:0000269|PubMed:19965770"
FT CONFLICT 76..77
FT /note="EL -> SV (in Ref. 2; AAA23965)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..239
FT /note="IGFAGPRVIEQTVRE -> MALPVRVLSNRPFAK (in Ref. 1;
FT AAA23807/AAA23801)"
FT /evidence="ECO:0000305"
FT CONFLICT 226..235
FT /note="GFAGPRVIEQ -> ALPVRVLSNR (in Ref. 2; AAA23965)"
FT /evidence="ECO:0000305"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:2F9Y"
FT TURN 36..44
FT /evidence="ECO:0007829|PDB:2F9Y"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:2F9Y"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 171..189
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:2F9Y"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:2F9Y"
SQ SEQUENCE 304 AA; 33322 MW; 401FEC94D728F3CB CRC64;
MSWIERIKSN ITPTRKASIP EGVWTKCDSC GQVLYRAELE RNLEVCPKCD HHMRMTARNR
LHSLLDEGSL VELGSELEPK DVLKFRDSKK YKDRLASAQK ETGEKDALVV MKGTLYGMPV
VAAAFEFAFM GGSMGSVVGA RFVRAVEQAL EDNCPLICFS ASGGARMQEA LMSLMQMAKT
SAALAKMQER GLPYISVLTD PTMGGVSASF AMLGDLNIAE PKALIGFAGP RVIEQTVREK
LPPGFQRSEF LIEKGAIDMI VRRPEMRLKL ASILAKLMNL PAPNPEAPRE GVVVPPVPDQ
EPEA
