ID D1L8P7_BRANA Unreviewed; 489 AA.
AC D1L8P7;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {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:ACY66222.1};
GN ORFNames=DARMORV10_C09P40220.1 {ECO:0000313|EMBL:CAF1752433.1};
OS Brassica napus (Rape).
OG Plastid {ECO:0000313|EMBL:ACY66222.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:ACY66222.1};
RN [1] {ECO:0000313|EMBL:ACY66222.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZY036 {ECO:0000313|EMBL:ACY66222.1};
RA Hu Z.Y., Hua W., Huang S.M., Wang H.Z.;
RT "Complete chloroplast genome sequence of rapeseed (Brassica napus L.) and
RT its evolutionary implications.";
RL Genet. Resour. Crop Evol. 58:875-887(2011).
RN [2] {ECO:0000313|EMBL:AEQ19133.1}
RP NUCLEOTIDE SEQUENCE.
RA Qi F.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AEQ19133.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23185237; DOI=10.1371/journal.pone.0047284;
RA Zeng C.L., Wang G.Y., Wang J.B., Yan G.X., Chen B.Y., Xu K., Li J.,
RA Gao G.Z., Wu X.M., Zhao B., Liu L.;
RT "High-Throughput Discovery of Chloroplast and Mitochondrial DNA
RT Polymorphisms in Brassicaceae Species by ORG-EcoTILLING.";
RL PLoS ONE 7:E47284-E47284(2012).
RN [4] {ECO:0000313|EMBL:AKD00098.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=51218 {ECO:0000313|EMBL:AKD00098.1};
RA Hao W., Hua W., Wang H.;
RT "A mitochondrial gene ORF188 contributes to cytoplasmic effects on seed oil
RT content in Brassica napus L.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ASY95024.1}
RP NUCLEOTIDE SEQUENCE.
RA Lee H.O., Perumal S., Ko H.-C., Yang T.-J., Kim C.-K.;
RT "Diversity and evolution of six U's triangle Brassica species revealed by
RT whole genome sequences of 28 accessions.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:CAF1752433.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope - CEA;
RA William W.;
RL Submitted (JAN-2021) 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: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 (AccB), biotin carboxylase (AccC) and two
CC subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC (AccD). {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 -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC Rule:MF_01395}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01395}.
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; GQ861354; ACY66222.1; -; Genomic_DNA.
DR EMBL; JF807893; AEQ19133.1; -; Genomic_DNA.
DR EMBL; KP161617; AKD00098.1; -; Genomic_DNA.
DR EMBL; KX681666; ASY95024.1; -; Genomic_DNA.
DR EMBL; HG994373; CAF1752433.1; -; Genomic_DNA.
DR RefSeq; YP_005089961.1; NC_016734.1.
DR AlphaFoldDB; D1L8P7; -.
DR EnsemblPlants; CDX92357; CDX92357; GSBRNA2T00154098001.
DR EnsemblPlants; CDX98576; CDX98576; GSBRNA2T00106250001.
DR EnsemblPlants; CDX99936; CDX99936; GSBRNA2T00108784001.
DR EnsemblPlants; CDX99943; CDX99943; GSBRNA2T00108796001.
DR GeneID; 11542019; -.
DR Gramene; CDX92357; CDX92357; GSBRNA2T00154098001.
DR Gramene; CDX98576; CDX98576; GSBRNA2T00106250001.
DR Gramene; CDX99936; CDX99936; GSBRNA2T00108784001.
DR Gramene; CDX99943; CDX99943; GSBRNA2T00108796001.
DR KEGG; bna:11542019; -.
DR OMA; KMNICEH; -.
DR OrthoDB; 5398975at2759; -.
DR UniPathway; UPA00655; UER00711.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01395}; Chloroplast {ECO:0000313|EMBL:ACY66222.1};
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};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:ACY66222.1};
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 225..489
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ SEQUENCE 489 AA; 55581 MW; 9C475FAC23DF2130 CRC64;
MEKSWFNLMF SKGELEYRGE LSKAMDSFAP IEKTTISKDR FIYDMDKNFY GWGERSSYYN
NVDLLVNSKD IRNFISDDTF FVRDSNKNSY SIYFDIKKKK FEINNDLSDL EIFFYSYCSS
SYLNNRSKGD NDLHYDPYIK DTKYNCNNHI NSCIDSYFRS HICINSHFLS DSNNSNESYI
YNFICSESGS GKIRESKNDK IRTNSNRNNL MSSKDFDITK NYNQLWIQCD NCYGLMYKKV
EMNVCEECGH YLKMTSSERI ELSIDPGTWN PMDEDMVSAD PIKFHSREEP YKKRIASAQK
KTGLTDAIQT GTGQLNGIPV ALGVMDFQFM GGSMGSVVGE KITRLIEYAT NQCLPLILVC
SSGGARMQEG SLSLMQMAKI SSVLCDYQSS KKLFYISILT SPTTGGVTAS FGMLGDIIIA
EPYAYIAFAG KRVIEQTLKK AVPEGSQAAE SLLRKGLLDA IVPRNPLKGV VSELFQLHAF
FPLNKNEIK
//
