ID   ACAC_CATRO              Reviewed;          31 AA.
AC   P85438;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Acetyl-CoA carboxylase;
DE            Short=ACC;
DE            EC=6.4.1.2;
DE   Flags: Fragments;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RA   Varman P.A.M., Ranjitha Kumari B.D.;
RL   Submitted (JAN-2008) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC         CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q00955};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:Q00955}.
CC   -!- MASS SPECTROMETRY: Mass=16986; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is:
CC       4.86, its MW is: 16.9 kDa.
CC   -!- CAUTION: The order of the peptides shown is unknown. {ECO:0000305}.
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   AlphaFoldDB; P85438; -.
DR   UniPathway; UPA00655; UER00711.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Nucleotide-binding.
FT   CHAIN           <1..>31
FT                   /note="Acetyl-CoA carboxylase"
FT                   /id="PRO_0000322590"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_CONS        17..18
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         31
SQ   SEQUENCE   31 AA;  3398 MW;  8B6F4DD2307766FD CRC64;
     RISSSVIAHK TQLDSGKREV YSSHMQLGGP K