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Database: UniProt
Entry: G4WXD2_BRAOL
LinkDB: G4WXD2_BRAOL
Original site: G4WXD2_BRAOL 
ID   G4WXD2_BRAOL            Unreviewed;       281 AA.
AC   G4WXD2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   13-SEP-2023, entry version 27.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|RuleBase:RU364072};
GN   Name=C.BCCP1.a {ECO:0000313|EMBL:AEI16458.1};
OS   Brassica oleracea (Wild cabbage).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3712 {ECO:0000313|EMBL:AEI16458.1};
RN   [1] {ECO:0000313|EMBL:AEI16458.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Guo L.Z., Min H.Z.;
RT   "The activity of acetyl-CoA carboxylase is correlated with the rate of
RT   lipid synthesis during development of oilseed rape (Brassica napus L.)
RT   embryos.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
CC       {ECO:0000256|RuleBase:RU364072}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|RuleBase:RU364072}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU364072}.
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DR   EMBL; JF504680; AEI16458.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4WXD2; -.
DR   UniPathway; UPA00094; -.
DR   ExpressionAtlas; G4WXD2; baseline.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   InterPro; IPR001249; AcCoA_biotinCC.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR00531; BCCP; 1.
DR   PANTHER; PTHR43416:SF38; BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR01071; ACOABIOTINCC.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   4: Predicted;
KW   Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|RuleBase:RU364072};
KW   Chloroplast {ECO:0000256|RuleBase:RU364072};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU364072};
KW   Ligase {ECO:0000313|EMBL:AEI16458.1};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU364072};
KW   Plastid {ECO:0000256|RuleBase:RU364072}.
FT   DOMAIN          204..280
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..203
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  29579 MW;  5FD82B201A45ABCB CRC64;
     MASSSFSVTS PAASVYGATQ TSSQLPLPTT RSRLPRRVSF RLSAKPKLRF LSKPSRSSYP
     VVKAQSNQVG GSASSKASAP AKIDEPSAKE KNASSSSSAD LATEESISEF LTQVTTLVKL
     VDSRDIVELQ LKQLDCELVI RKKEALPQPP QSPAPYVMMQ QPNQPSYVQS APPPPAPAAA
     SPAPSSTPAS SPPPSPPSPA KSSLPTVKSP MAGTFYRSPG PGEPPFIKVG DKVQKGQVLC
     IVEAMKLMNE IESDQTGTVV DIVAEDGKPV SLDTPLFVVQ P
//
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