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Database: UniProt
Entry: B2D2S4_9LAMI
LinkDB: B2D2S4_9LAMI
Original site: B2D2S4_9LAMI 
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
//
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