ACCD_ARATH
ID ACCD_ARATH Reviewed; 488 AA.
AC P56765;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 148.
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}; OrderedLocusNames=AtCg00500;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=10759501; DOI=10.1104/pp.122.4.1057;
RA Ke J., Wen T.N., Nikolau B.J., Wurtele E.S.;
RT "Coordinate regulation of the nuclear and plastidic genes coding for the
RT subunits of the heteromeric acetyl-coenzyme A carboxylase.";
RL Plant Physiol. 122:1057-1071(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
RN [3]
RP RNA EDITING.
RC STRAIN=cv. Columbia;
RX PubMed=11078738; DOI=10.1074/jbc.m008166200;
RA Sasaki Y., Kozaki A., Ohmori A., Iguchi H., Nagano Y.;
RT "Chloroplast RNA editing required for functional acetyl-CoA carboxylase in
RT plants.";
RL J. Biol. Chem. 276:3937-3940(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(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:0000269|PubMed:10759501}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:18431481}; Peripheral membrane protein. Plastid,
CC chloroplast stroma {ECO:0000269|PubMed:18431481}.
CC -!- TISSUE SPECIFICITY: Accumulates in fatty acids synthesizing tissues
CC such as embryos, expanding leaves, flower buds, flowers, and developing
CC siliques. {ECO:0000269|PubMed:10759501}.
CC -!- RNA EDITING: Modified_positions=265 {ECO:0000269|PubMed:11078738};
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; AF056971; AAF35256.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP000423; BAA84394.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_051068.1; NC_000932.1.
DR AlphaFoldDB; P56765; -.
DR SMR; P56765; -.
DR BioGRID; 29959; 3.
DR IntAct; P56765; 1.
DR STRING; 3702.ATCG00500.1; -.
DR PaxDb; P56765; -.
DR PeptideAtlas; P56765; -.
DR PRIDE; P56765; -.
DR ProteomicsDB; 244500; -.
DR GeneID; 844755; -.
DR KEGG; ath:ArthCp031; -.
DR Araport; ATCG00500; -.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_537942_0_0_1; -.
DR InParanoid; P56765; -.
DR OrthoDB; 623889at2759; -.
DR BioCyc; ARA:ATCG00500-MON; -.
DR BioCyc; MetaCyc:ATCG00500-MON; -.
DR BRENDA; 2.1.3.15; 399.
DR UniPathway; UPA00655; UER00711.
DR PRO; PR:P56765; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P56765; baseline and differential.
DR Genevisible; P56765; AT.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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; Membrane; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; RNA editing; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..488
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000199780"
FT DOMAIN 227..488
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 231..250
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 234
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 BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 488 AA; 55636 MW; 6923CD2003885AEB CRC64;
MEKSWFNFMF SKGELEYRGE LSKAMDSFAP GEKTTISQDR FIYDMDKNFY GWDERSSYSS
SYSNNVDLLV SSKDIRNFIS DDTFFVRDSN KNSYSIFFDK KKKIFEIDND FSDLEKFFYS
YCSSSYLNNR SKGDNDLHYD PYIKDTKYNC TNHINSCIDS YFRSYICIDN NFLIDSNNFN
ESYIYNFICS ESGKIRESKN YKIRTNRNRS NLISSKDFDI TQNYNQLWIQ CDNCYGLMYK
KVKMNVCEQC GHYLKMSSSE RIELLIDPGT WNPMDEDMVS ADPIKFHSKE EPYKNRIDSA
QKTTGLTDAV QTGTGQLNGI PVALGVMDFR FMGGSMGSVV GEKITRLIEY ATNQCLPLIL
VCSSGGARMQ EGSLSLMQMA KISSVLCDYQ SSKKLFYISI LTSPTTGGVT ASFGMLGDII
IAEPYAYIAF AGKRVIEQTL KKAVPEGSQA AESLLRKGLL DAIVPRNLLK GVLSELFQLH
AFFPLNTN
