ACCD_SOLLC
ID ACCD_SOLLC Reviewed; 490 AA.
AC Q2MI91;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 80.
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 lycopersicum (Tomato) (Lycopersicon esculentum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. LA3023;
RX PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., Guda C.,
RA Tomkins J., Jansen R.K.;
RT "Complete chloroplast genome sequences of Solanum bulbocastanum, Solanum
RT lycopersicum and comparative analyses with other Solanaceae genomes.";
RL Theor. Appl. Genet. 112:1503-1518(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. IPA-6;
RX PubMed=16830097; DOI=10.1007/s00239-005-0254-5;
RA Kahlau S., Aspinall S., Gray J.C., Bock R.;
RT "Sequence of the tomato chloroplast DNA and evolutionary comparison of
RT solanaceous plastid genomes.";
RL J. Mol. Evol. 63:194-207(2006).
RN [3]
RP LEVEL OF PROTEIN EXPRESSION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. IPA-6;
RX PubMed=18441214; DOI=10.1105/tpc.107.055202;
RA Kahlau S., Bock R.;
RT "Plastid transcriptomics and translatomics of tomato fruit development and
RT chloroplast-to-chromoplast differentiation: chromoplast gene expression
RT largely serves the production of a single protein.";
RL Plant Cell 20:856-874(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 (By similarity). Is
CC up-regulated upon chromoplast differentiation, presumably for fatty
CC acid biosynthesis. {ECO:0000255|HAMAP-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:0000305}.
CC Plastid, chromoplast stroma {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, ripening and mature fruit.
CC -!- DEVELOPMENTAL STAGE: Transcription is reduced upon fruit development;
CC as fruit ripens and chloroplasts differentitate into chromoplasts
CC transcripts increase again. Protein levels also increase in
CC chromoplasts (at protein level). {ECO:0000269|PubMed:18441214}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC56309.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAJ32402.1; Type=Erroneous initiation; Evidence={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 EMBL; DQ347959; ABC56309.1; ALT_INIT; Genomic_DNA.
DR EMBL; AM087200; CAJ32402.1; ALT_INIT; Genomic_DNA.
DR RefSeq; AP_004937.1; AC_000188.1.
DR RefSeq; XP_004228575.1; XM_004228527.3.
DR RefSeq; YP_008563097.1; NC_007898.3.
DR AlphaFoldDB; Q2MI91; -.
DR SMR; Q2MI91; -.
DR STRING; 4081.Solyc01g007340.2.1; -.
DR PaxDb; Q2MI91; -.
DR PRIDE; Q2MI91; -.
DR GeneID; 3950389; -.
DR KEGG; sly:3950389; -.
DR eggNOG; KOG0540; Eukaryota.
DR InParanoid; Q2MI91; -.
DR OrthoDB; 623889at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000004994; Chloroplast.
DR ExpressionAtlas; Q2MI91; baseline.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009575; C:chromoplast 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; Chromoplast; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..490
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000277421"
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 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"
SQ SEQUENCE 490 AA; 55674 MW; 7F80CA6C3C9AEBC4 CRC64;
MERWWFNSML FKKEFERRCG LNKSMGSLGP IENTSEDPNL KVKNIHSCSN VDYLFGVKDI
WNFISNDTFL VSDRNGDSYS IYFDIENHIF EVDNDHSFLS ELESSFYSYR NSSYLNNGFR
GEDPYYNSYM SYMYDTQYSW NNHINSCIDN YLQSQICIDT SIISGSESNG DSYIYRAICS
GQSLNSSENE GSSRRTRTKD SDLTIRESSN DLEVTQKYKH LWVQCENCYG LNYKKFLKSK
MNICEQCGYH LKMSSSDRIE LLIDPGTWDP MDEDMVSLDP IEFHSEEEPY KDRIDSYQRK
TGLTEAVQTG IGQLNGIPVA IGVMDFQFMG GSMGSVVGEK ITRLIEHAAN QNLPLMIVCA
SGGARMQEGS LSLMQMAKIS SALYDYQLNK KLFYVSILTS PTTGGVTASF GMLGDIIIAE
PNAYIAFAGK RVIEQTLNKT VPEGSQAAEY LFQKGLFDLI VPRNLLKSVL SELFKLHAFF
PLNQKSSKIK
