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
//