GenomeNet

Database: UniProt
Entry: B5KS49_9ASPA
LinkDB: B5KS49_9ASPA
Original site: B5KS49_9ASPA 
ID   B5KS49_9ASPA            Unreviewed;       122 AA.
AC   B5KS49;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=AccD {ECO:0000313|EMBL:ABW99854.1};
DE   Flags: Fragment;
GN   Name=accD {ECO:0000313|EMBL:ABW99854.1};
OS   Crocus speciosus subsp. speciosus.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ABW99854.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae;
OC   Crocoideae; Croceae; Crocus.
OX   NCBI_TaxID=481117 {ECO:0000313|EMBL:ABW99854.1};
RN   [1] {ECO:0000313|EMBL:ABW99854.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Petersen G., Seberg O., Thorsoe S., Jorgensen T., Mathew B.;
RT   "A phylogeny of the genus Crocus (Iridaceae) based on sequence data from
RT   five plastid regions.";
RL   Taxon 57:487-499(2008).
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   ---------------------------------------------------------------------------
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; EU110280; ABW99854.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5KS49; -.
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:ABW99854.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plastid {ECO:0000313|EMBL:ABW99854.1};
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:ABW99854.1"
FT   NON_TER         122
FT                   /evidence="ECO:0000313|EMBL:ABW99854.1"
SQ   SEQUENCE   122 AA;  13171 MW;  925A473B2F0A6DA6 CRC64;
     EKITRLIEYA TNRSIPVIIV CASGGARMQE GSLSLMQMAK ISSALYNYQS NKKLFYVSIL
     TSPTTGGVTA SFGMLGDVII AEPNAHVAFA GKRVIEQTLN KQVPDGSQAA EYSFHKGLFD
     PI
//
DBGET integrated database retrieval system