ACCD_ANTAG
ID ACCD_ANTAG Reviewed; 313 AA.
AC Q31796;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, 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 Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91.
RC TISSUE=Thallus;
RX PubMed=8604330; DOI=10.1093/nar/24.6.1008;
RA Yoshinaga K., Iinuma H., Masuzawa T., Ueda K.;
RT "Extensive RNA editing of U to C in addition to C to U substitution in the
RT rbcL transcripts of hornwort chloroplasts and the origin of RNA editing in
RT green plants.";
RL Nucleic Acids Res. 24:1008-1014(1996).
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 -!- RNA EDITING: Modified_positions=50 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 59 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 78 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 87 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 104 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 132 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 139 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 146 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 149 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 160 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 170 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 177 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 185 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 198 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 208 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 223 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 226 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 228 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 243 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 246 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 252 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 260 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 264 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 277 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 285 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 295 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions 50,
CC 78, 104, 260 and 264 are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; AB086179; BAC55358.1; -; Genomic_DNA.
DR EMBL; AB087450; BAC55454.1; -; mRNA.
DR EMBL; D43695; BAA07797.1; ALT_SEQ; Genomic_DNA.
DR PIR; S71147; S71147.
DR RefSeq; NP_777422.1; NC_004543.1.
DR AlphaFoldDB; Q31796; -.
DR SMR; Q31796; -.
DR GeneID; 2553479; -.
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 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; RNA editing; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..313
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000199779"
FT DOMAIN 47..313
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 51..73
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 313 AA; 35272 MW; 6881B7B5FF780126 CRC64;
MSLMNWFEDR RKFSGLIGAF IEKATKGYIL SERRKDRHIK IDTTKGLWTR CDNCENMLYI
RFLRQNKRIC EECGYHLQMS STERIESLID RGTWHPMDED MVARDALKFS DEDSYKNRVL
FYQKRTGLTD AIQTGIGKLN GIPIALGVMD FQFMGGSMGS VVGEKITRLI EYGTRESMPV
IIVCSSGGAR MQEGTLSLMQ MAKISAVLQI HQAQKKLLYI AILTYPTTGG VTASFGMLGD
VIIAEPKAYI AFAGKRVIEQ TLRQKIPDGS QVAESLFDHG LLDLIVPRNL LRGVLSEIFE
LYSSAPCRRS NNS
