ID B2D2S4_9LAMI Unreviewed; 122 AA.
AC B2D2S4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Acetyl-CoA carboxylase-D {ECO:0000313|EMBL:ACB58692.1};
DE Flags: Fragment;
GN Name=accD {ECO:0000313|EMBL:ACB58692.1};
OS Clerodendranthus spicatus.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ACB58692.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Teucrioideae; Clerodendranthus.
OX NCBI_TaxID=516067 {ECO:0000313|EMBL:ACB58692.1};
RN [1] {ECO:0000313|EMBL:ACB58692.1}
RP NUCLEOTIDE SEQUENCE.
RA Chen S.-L., Han J.-P., Yao H., Song J.-Y., Li Y., Shi L.-C., Ma X.-Y.,
RA Wu Q., Jia X.-C.;
RT "Use of DNA barcodes to identify labiate traditional medicines.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; EU590904; ACB58692.1; -; Genomic_DNA.
DR AlphaFoldDB; B2D2S4; -.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chloroplast {ECO:0000313|EMBL:ACB58692.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plastid {ECO:0000313|EMBL:ACB58692.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..122
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACB58692.1"
FT NON_TER 122
FT /evidence="ECO:0000313|EMBL:ACB58692.1"
SQ SEQUENCE 122 AA; 13274 MW; D6489F567EDA9404 CRC64;
EKITRLIEYA TNQFLPLIIV CASGGARMQE GSLSLMQMAK ISSALYDYQS NKKLLYVSIL
TSPTTGGVTA SFGMLGDIII AEPNSYIAFA GKRVIEQTLN KTVPEGSQAA EYLFQKGLFD
LI
//