ACCD_TOBAC
ID ACCD_TOBAC Reviewed; 495 AA.
AC P12219;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 110.
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}; Synonyms=ycf11, zfpA;
OS Nicotiana tabacum (Common tobacco).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Bright Yellow 4;
RX PubMed=16453699; DOI=10.1002/j.1460-2075.1986.tb04464.x;
RA Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N.,
RA Matsubayashi T., Zaita N., Chunwongse J., Obokata J.,
RA Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M.,
RA Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A.,
RA Tohdoh N., Shimada H., Sugiura M.;
RT "The complete nucleotide sequence of the tobacco chloroplast genome: its
RT gene organization and expression.";
RL EMBO J. 5:2043-2049(1986).
RN [2]
RP DETECTION IN CHLOROPLASTS, AND OVEREXPRESSION.
RC STRAIN=cv. Xanthi; TISSUE=Fruit, and Leaf;
RX PubMed=12514249; DOI=10.1093/pcp/pcf172;
RA Madoka Y., Tomizawa K., Mizoi J., Nishida I., Nagano Y., Sasaki Y.;
RT "Chloroplast transformation with modified accD operon increases acetyl-CoA
RT carboxylase and causes extension of leaf longevity and increase in seed
RT yield in tobacco.";
RL Plant Cell Physiol. 43:1518-1525(2002).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=15232216;
RA Lee S.S., Jeong W.J., Bae J.M., Bang J.W., Liu J.R., Harn C.H.;
RT "Characterization of the plastid-encoded carboxyltransferase subunit (accD)
RT gene of potato.";
RL Mol. Cells 17:422-429(2004).
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 -!- TISSUE SPECIFICITY: RNA expressed in leaf, root and stem; the least
CC expression occurs in stems. {ECO:0000269|PubMed:15232216}.
CC -!- BIOTECHNOLOGY: Overexpression of the accD operon increases the specific
CC activity of acetyl-coenzyme A carboxylase, increases leaf longevity and
CC seed production. The accD operon consists of accD, psaI, ycf4, cemA,
CC and petA in this order.
CC -!- MISCELLANEOUS: The protein in tobacco runs as 53 kDa; thus this may not
CC be the correct start site.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA77362.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z00044; CAA77362.1; ALT_INIT; Genomic_DNA.
DR PIR; A05196; A05196.
DR RefSeq; NP_054508.1; NC_001879.2.
DR AlphaFoldDB; P12219; -.
DR SMR; P12219; -.
DR PRIDE; P12219; -.
DR GeneID; 800510; -.
DR KEGG; nta:800510; -.
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 1: Evidence at protein level;
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..495
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000199796"
FT DOMAIN 226..495
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 230..252
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT REGION 187..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 233
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"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 495 AA; 56459 MW; BC468ABFFDCAF24E CRC64;
MERWWFNSML FKKEFERRCG LNKSMGSLGP IENTNEDPNR KVKNIHSWRN RDNSSCSNVD
YLFGVKDIRN FISDDTFLVS DRNGDSYSIY FDIENHIFEI DNDHSFLSEL ESSFYSYRNS
NYRNNGFRGE DPYYNSYMYD TQYSWNNHIN SCIDSYLQSQ ICIDTSIISG SENYGDSYIY
RAVCGGESRN SSENEGSSRR TRTKGSDLTI RESSNDLEVT QKYRHLWVQC ENCYGLNYKK
FLKSKMNICE QCGYHLKMSS SDRIELLIDP GTWDPMDEDM VSLDPIEFHS EEEPYKDRID
SYQRKTGLTE AVQTGIGQLN GIPVAIGVMD FQFMGGSMGS VVGEKITRLI EYAANQILPL
IIVCASGGAR MQEGSLSLMQ MAKISSALYD YQLNKKLFYV SILTSPTTGG VTASFGMLGD
IIIAEPNAYI AFAGKRVIEQ TLNKTVPEGS QAAEYLFQKG LFDLIVPRNL LKSVLSELFK
LHAFFPLNQK SSKIK
