ID B5LAS9_CAPAN Unreviewed; 551 AA.
AC B5LAS9;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
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:AFP90785.1};
OS Capsicum annuum (Capsicum pepper).
OG Plastid {ECO:0000313|EMBL:ACF17636.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072 {ECO:0000313|EMBL:ACF17636.1};
RN [1] {ECO:0000313|EMBL:ACF17636.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19553373; DOI=10.1104/pp.109.136549;
RA Mazourek M., Pujar A., Borovsky Y., Paran I., Mueller L., Jahn M.M.;
RT "A dynamic interface for capsaicinoid systems biology.";
RL Plant Physiol. 150:1806-1821(2009).
RN [2] {ECO:0000313|EMBL:AFP90785.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS4401 {ECO:0000313|EMBL:AFP90785.1};
RX PubMed=20978766; DOI=10.1007/s00299-010-0929-2;
RA Jo Y.D., Park J., Kim J., Song W., Hur C.G., Lee Y.H., Kang B.C.;
RT "Complete sequencing and comparative analyses of the pepper (Capsicum
RT annuum L.) plastome revealed high frequency of tandem repeats and large
RT insertion/deletions on pepper plastome.";
RL Plant Cell Rep. 30:217-229(2011).
RN [3] {ECO:0000313|EMBL:AFP90785.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FS4401 {ECO:0000313|EMBL:AFP90785.1};
RA Jo Y.D., Park J., Kim J., Song W., Hur C.-G., Lee Y.-H., Kang B.-C.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AYN59811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ann1 {ECO:0000313|EMBL:AYN60155.1}, Ann2
RC {ECO:0000313|EMBL:AYN59811.1}, and Ann3 {ECO:0000313|EMBL:AYN60327.1};
RX PubMed=30336638;
RA D'Agostino N., Tamburino R., Cantarella C., De Carluccio V., Sannino L.,
RA Cozzolino S., Cardi T., Scotti N.;
RT "The Complete Plastome Sequences of Eleven Capsicum Genotypes: Insights
RT into DNA Variation and Molecular Evolution.";
RL Genes (Basel) 9:E503-E503(2018).
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}.
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DR EMBL; EU616544; ACF17636.1; -; mRNA.
DR EMBL; JX270811; AFP90785.1; -; Genomic_DNA.
DR EMBL; MH559323; AYN59811.1; -; Genomic_DNA.
DR EMBL; MH559327; AYN60155.1; -; Genomic_DNA.
DR EMBL; MH559329; AYN60327.1; -; Genomic_DNA.
DR RefSeq; YP_006666039.1; NC_018552.1.
DR AlphaFoldDB; B5LAS9; -.
DR SMR; B5LAS9; -.
DR GeneID; 13540227; -.
DR KEGG; cann:13540227; -.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:AFP90785.1};
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:ACF17636.1};
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 282..551
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT ZN_FING 286..308
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT REGION 196..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ SEQUENCE 551 AA; 61958 MW; 6CD397CD5EB73810 CRC64;
MTIHLLYFHA NRGQENSMER WWFNSMLFKK EFERRCGLNK SMGSLGPIEN TSEDPNRKVK
NIPSCSNVDY LFGVKDIRNF ISDDTFVVSD RNGDSYSIYF DIENQIFEID NDHSFLSELE
SSFYSYRNSS YLNNGFRGED PYYNSYMYDT QYSWNNHINS CIDNYLQSQI CIDTSIISGS
ENYSDSYIYR AVCGGESKNS SENEGSSIQT RTKGSDLTIR ESSNGSDLTI GSDLTIGSDL
TNGSDLTIGS DLTIGSDLTN GSDLTIRESS NDLEVTQKYR HLWVQCENCY GLNYKKFFKS
KMNICEQCGY HLKMSSSDRI ELLVDPGTWD PMDEDMVSLD PIEFHSEEEP YKDRIDSYQR
KTGLTEAVQT GIGQINGIPV AIGVMDFQFM GGSMGSVVGE KITRLIEHAA NQILPLIIVC
ASGGARMQEG SLSLMQMAKI SSALYDYQLN KKLFYVSILT SPTTGGVTAS FGMLGDIIIA
EPNAYIAFAG KRVIEQTLNK TVPEGSQVAE YLFQKGLFDL IVPRNLLKSV LSELFKLHAF
FPLNQKSSKI K
//
