ID B3IUF0_TAKLE Unreviewed; 316 AA.
AC B3IUF0;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01395};
DE Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01395};
GN Name=accD {ECO:0000256|HAMAP-Rule:MF_01395,
GN ECO:0000313|EMBL:BAG50119.1};
OS Takakia lepidozioides (Moss).
OG Plastid; Chloroplast {ECO:0000313|EMBL:BAG50119.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Takakiophytina; Takakiopsida; Takakiales; Takakiaceae; Takakia.
OX NCBI_TaxID=37425 {ECO:0000313|EMBL:BAG50119.1};
RN [1] {ECO:0000313|EMBL:BAG50119.1}
RP NUCLEOTIDE SEQUENCE.
RA Sugita M., Sugiura C., Arikawa T., Higuchi M.;
RT "Molecular evidence of an rpoA gene in the basal moss chloroplast genomes:
RT rpoA is a useful molecular marker for phylogenetic analysis of mosses.";
RL Hikobia 14:171-175(2004).
RN [2] {ECO:0000313|EMBL:BAG50119.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16960353; DOI=10.1271/bbb.60204;
RA Sugita M., Miyata Y., Maruyama K., Sugiura C., Arikawa T., Higuchi M.;
RT "Extensive RNA editing in transcripts from the psbB operon and rpoA gene of
RT plastids from the enigmatic moss Takakia lepidozioides.";
RL Biosci. Biotechnol. Biochem. 70:2268-2274(2006).
RN [3] {ECO:0000313|EMBL:BAG50119.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18650260; DOI=10.1093/dnares/dsn016;
RA Yura K., Miyata Y., Arikawa T., Higuchi M., Sugita M.;
RT "Characteristics and prediction of RNA editing sites in transcripts of the
RT Moss Takakia lepidozioides chloroplast.";
RL DNA Res. 15:309-321(2008).
RN [4] {ECO:0000313|EMBL:BAG50119.1}
RP NUCLEOTIDE SEQUENCE.
RA Miyata Y., Sugita C., Maruyama K., Sugita M.;
RT "RNA editing in the anticodon of tRNALeu (CAA) occurs before group I intron
RT splicing in plastids of a moss Takakia lepidozioides S. Hatt. & Inoue.";
RL Plant Biol. 10:250-255(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:0000256|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:0000256|HAMAP-Rule:MF_01395};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01395};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01395};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|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:0000256|ARBA:ARBA00011842}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein, biotin carboxylase and two subunits each of
CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC {ECO:0000256|HAMAP-Rule:MF_01395}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000256|HAMAP-
CC Rule:MF_01395}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; AB299142; BAG50119.1; -; Genomic_DNA.
DR EMBL; AB299149; BAG50134.1; -; mRNA.
DR AlphaFoldDB; B3IUF0; -.
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_beta.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011762; COA_CT_N.
DR NCBIfam; TIGR00515; accD; 1.
DR PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01395}; Chloroplast {ECO:0000313|EMBL:BAG50119.1};
KW Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395};
KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01395}; Plastid {ECO:0000313|EMBL:BAG50119.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01395}; Zinc {ECO:0000256|HAMAP-Rule:MF_01395};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}.
FT DOMAIN 47..316
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT ZN_FING 51..73
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ SEQUENCE 316 AA; 35930 MW; 54C8F7FD9D36E56E CRC64;
MSLMNWFEDK RRFGGLIGAF IEKATKGYVL SEREKDRYIK IDTTKGLWTR CDNCENMLYV
RFLRQNRRIC EECGYHLQMS STERIELLID RGTWHPMDED MVARDVLRFS DEDSYKNRVT
FYQKRTGLTD AIQTGIGKLD GTPVALGVMD FQFMGGSMGS VVGEKITRLI EYATRKSMPL
IIVCSSGGAR MQEGTLSLMQ MAKISSVLQI HQAQKRLLYI PILTYPTTGG VTASFGMLGD
IIIAEPKAYI AFAGKRVIEQ TLRQKIPDGF QVAESLFDHG LLDLIVPRNL SKGVLSEIFE
LYGSAPCKER NNYYFR
//
