ACCD_SOLTU
ID ACCD_SOLTU Reviewed; 490 AA.
AC Q2VEG8; O78323;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 3.
DT 03-AUG-2022, entry version 66.
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 Solanum tuberosum (Potato).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TRANSCRIPT ANALYSIS, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Desiree;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Desiree;
RX PubMed=16835751; DOI=10.1007/s00299-006-0196-4;
RA Chung H.-J., Jung J.D., Park H.-W., Kim J.-H., Cha H.W., Min S.R.,
RA Jeong W.-J., Liu J.R.;
RT "The complete chloroplast genome sequences of Solanum tuberosum and
RT comparative analysis with Solanaceae species identified the presence of a
RT 241-bp deletion in cultivated potato chloroplast DNA sequence.";
RL Plant Cell Rep. 25:1369-1379(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Desiree;
RA Gargano D., Scotti N., Vezzi A., Bilardi A., Valle G., Grillo S., Cardi T.;
RT "Complete chloroplast genome sequences of Solanum tuberosum cultivar
RT Desiree and comparative analyses with other Solanaceae genomes.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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, stem, and tuber; the
CC least expression occurs in stems. RNA persists even in senescent
CC leaves. {ECO:0000269|PubMed:15232216}.
CC -!- INDUCTION: Not induced by light.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23997.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABB90050.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABD47066.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF069288; AAC23997.1; ALT_INIT; Genomic_DNA.
DR EMBL; DQ231562; ABB90050.1; ALT_INIT; Genomic_DNA.
DR EMBL; DQ386163; ABD47066.1; ALT_INIT; Genomic_DNA.
DR PIR; T07012; T07012.
DR RefSeq; YP_635648.1; NC_008096.2.
DR AlphaFoldDB; Q2VEG8; -.
DR SMR; Q2VEG8; -.
DR GeneID; 4099986; -.
DR KEGG; sot:4099986; -.
DR InParanoid; Q2VEG8; -.
DR OrthoDB; 623889at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000011115; Unassembled WGS sequence.
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 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW Plastid; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..490
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000277580"
FT DOMAIN 221..490
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 225..247
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT REGION 184..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT CONFLICT 399
FT /note="T -> K (in Ref. 2; ABB90050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 55596 MW; DFD4751300F86C5B CRC64;
MERWWFNSML FKKEFERRCG LNKSMGSLGP IENTSEDPNL KMKNIHSCSN VDYLFGVKDI
WNFISDDTFL VSDRNGDSYS IYFDIENQIF EVDNDHSFLS ELESSFSSYR NSSYLNNGFR
GEDPYYNSYM SYMYDTQYSW NNHINSCIDN YLQSQICIDT SIISGSESYG DSYIYRAICS
GESLNSSENE GSSRRTRTKG SDLTIRESSN DLEVTQKYKH LWVQCENCYG LNYKKFLKSK
MNICEQCGYH LKMSSSDRIE LLIDPGTWDP MDEDMVSLDP IEFHSEEEPY KDRIDSYQRK
TGLTEAVQTG IGQLNGIPVA IGVMDFQFMG GSMGSVVGEK ITRLIEHAAN QNLPLIIVCA
SGGARMQEGS LSLMQMAKIS SALYDYQLNK KLFYVSILTS PTTGGVTASF GMLGDIIIAE
PNAYIAFAGK RVIEQTLNKT VPEGSQAAEY LFQKGLFDLI VPRNLLKSVL SELFKLHAFF
PLNQKSSKIK
