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ACCD_DAUCA
ID   ACCD_DAUCA              Reviewed;         491 AA.
AC   Q0G9V3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {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};
OS   Daucus carota (Wild carrot).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Danvers Half-long;
RX   PubMed=16945140; DOI=10.1186/1471-2164-7-222;
RA   Ruhlman T., Lee S.-B., Jansen R.K., Hostetler J.B., Tallon L.J., Town C.D.,
RA   Daniell H.;
RT   "Complete plastid genome sequence of Daucus carota: implications for
RT   biotechnology and phylogeny of angiosperms.";
RL   BMC Genomics 7:222-222(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. {ECO:0000255|HAMAP-
CC       Rule:MF_01395}.
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       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01395};
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, biotin carboxylase and 2 subunits each of
CC       ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000255|HAMAP-
CC       Rule:MF_01395}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01395}.
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DR   EMBL; DQ898156; ABI32433.1; -; Genomic_DNA.
DR   RefSeq; YP_740126.1; NC_008325.1.
DR   AlphaFoldDB; Q0G9V3; -.
DR   SMR; Q0G9V3; -.
DR   PRIDE; Q0G9V3; -.
DR   EnsemblPlants; KZM81231; KZM81231; DCAR_032493.
DR   GeneID; 4266752; -.
DR   Gramene; KZM81231; KZM81231; DCAR_032493.
DR   OMA; HICINSH; -.
DR   OrthoDB; 623889at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
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   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00515; accD; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW   Plastid; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..491
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta, chloroplastic"
FT                   /id="PRO_0000359134"
FT   DOMAIN          223..491
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   ZN_FING         227..249
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   REGION          28..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ   SEQUENCE   491 AA;  55550 MW;  A0695B0342B49544 CRC64;
     MERWWFDSIL FKKGFEHRCG LSKSMGGLGP IENTSESEDP NRNDMKKNSH SWGSRDNSSY
     SNVDYLFGVK DIWNFISDET FLVVDRNGNS YSIYLDIEKH IFEIDSGHFF QSGLESSFYS
     YWNLSYLNNG SKTDDPHDDH YMDDTQYSWN NHINSYIDIY LESQIFIDTY IVSGSDNYSN
     SYISRSVCGE SESKGSNIST STNGSTIIES SNDLDITQKY RHLWVQCENC YGLNYKKILK
     SKMNLCEQCG YHLKMSSSDR IELSIDPDTW DAMDEDMVSL DPIEFHSEEE PYKDRIDSYQ
     RKTGLTEAVQ TGIGQLNGIP IALGVMDFQF MGGSMGSVVG EKITRLIEYA TNQLLPLIIV
     CASGGARMQE GSLSLMQMAK ISSALYDYQS NKKLFYVPIL TSPTTGGVTA SFGMLGDIII
     AEPNAYIAFA GKRVIEQTLN KTVPEGSQAA EYLFQKGLFD LIVPRNLLKS VLSELFQLHA
     FFPLNKNSIE H
 
 
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