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Database: UniProt
Entry: Q9MTL3
LinkDB: Q9MTL3
Original site: Q9MTL3 
ID   ACCD_OENEH              Reviewed;         517 AA.
AC   Q9MTL3;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   24-JAN-2024, entry version 97.
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   Oenothera elata subsp. hookeri (Hooker's evening primrose) (Oenothera
OS   hookeri).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX   NCBI_TaxID=85636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Johansen;
RX   PubMed=10852478; DOI=10.1007/pl00008686;
RA   Hupfer H., Swiatek M., Hornung S., Herrmann R.G., Maier R.M., Chiu W.-L.,
RA   Sears B.;
RT   "Complete nucleotide sequence of the Oenothera elata plastid chromosome,
RT   representing plastome I of the five distinguishable Euoenothera
RT   plastomes.";
RL   Mol. Gen. Genet. 263:581-585(2000).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS AND 80-94.
RX   PubMed=18299283; DOI=10.1093/nar/gkn081;
RA   Greiner S., Wang X., Rauwolf U., Silber M.V., Mayer K., Meurer J.,
RA   Haberer G., Herrmann R.G.;
RT   "The complete nucleotide sequences of the five genetically distinct plastid
RT   genomes of Oenothera, subsection Oenothera: I. Sequence evaluation and
RT   plastome evolution.";
RL   Nucleic Acids Res. 36:2366-2378(2008).
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; AJ271079; CAB67165.2; -; Genomic_DNA.
DR   RefSeq; NP_084700.2; NC_002693.2.
DR   AlphaFoldDB; Q9MTL3; -.
DR   SMR; Q9MTL3; -.
DR   GeneID; 802793; -.
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_beta.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011762; COA_CT_N.
DR   NCBIfam; TIGR00515; accD; 1.
DR   PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; ClpP/crotonase; 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..517
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta, chloroplastic"
FT                   /id="PRO_0000199787"
FT   DOMAIN          243..514
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   ZN_FING         247..269
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   REGION          1..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..130
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ   SEQUENCE   517 AA;  59318 MW;  10B67C3400C24C60 CRC64;
     MKPTKPEGPK KPNKSNEEAE ELEGDNKEDL EGPKKPNKSN EEAEELEGDN KEDLEGPKKP
     NKSNEEAEEL EGDKQKDKKD GIFVLNYDDE YEEDLEYDDE YEEDLEYDDE YEEDLEYDDE
     EYDDEYEEDL EGDNKPHKED LEGDNKPHKE DLEGDNKPHK EDLEGDKQKE EEEKQKEEEE
     KLKDCPWHWF HQIYPKHWGC PHRKHRDRKS VPAKERELVP AQSTKRDTDP DSEASLKSNY
     AHLWVHCKLC SGFNYKKILK SKNNVCEQCG SHLKMHSSDR IDLMLDPKTW APMHEGLLSL
     DPIEFHSEKD PYKDRVASYK RKTGLSEAIQ TGRGYLKRIH LGIGLMDFQF MGGSMGSVVG
     ERITRLVEYA TNRVLPLILV CASGGARMQE GSLSLMQMAK ISSALSDYQF NRTVFYVALL
     TSPTTGGVTA SFGMLGDIIL AEPNAYIAFA GKRVIEQTLN IEVPEGSQTA EYLFDKGLFD
     QIVPRNPLKG SLSELFNFHG FVTLNSQVIN IYNYLYS
//
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