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Database: UniProt
Entry: D4VN56_9BACE
LinkDB: D4VN56_9BACE
Original site: D4VN56_9BACE 
ID   D4VN56_9BACE            Unreviewed;       143 AA.
AC   D4VN56;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN   ORFNames=BN890_9850 {ECO:0000313|EMBL:CDM03432.1};
OS   Bacteroides xylanisolvens SD CC 1b.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=702447 {ECO:0000313|EMBL:CDM03432.1, ECO:0000313|Proteomes:UP000019380};
RN   [1] {ECO:0000313|EMBL:CDM03432.1, ECO:0000313|Proteomes:UP000019380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ramaraj T., Sundararajan A., Mudge J., Schilkey F.D., Delvecchio V.,
RA   Donlon M., Ziemer C.;
RT   "Improved hybrid genome assemblies of Bacteroides xylanisolvens SD CC 1b
RT   and Bacteroides xylanisolvens SD CC 2a using Illumina and 454 Sequencing.";
RL   Submitted (DEC-2013) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDM03432.1}.
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DR   EMBL; CBXG010000014; CDM03432.1; -; Genomic_DNA.
DR   RefSeq; WP_004314215.1; NZ_ADKP01000151.1.
DR   AlphaFoldDB; D4VN56; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000019380; Unassembled WGS sequence.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
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   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 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   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU364072};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU364072}.
FT   DOMAIN          66..143
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          48..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   143 AA;  15447 MW;  58B4F82BC27E9E91 CRC64;
     MKEYKYKING NSYKVTIGDI EDNIAHVEVN GTHYKVEMEK QPKPVAKPVT VRPMPNAPTA
     PTQVVKPTAP STGKSGVKSP LPGVILDIKV NVGDTVKKGQ TIIILEAMKM ENNINADKDG
     KITAINVNKG DSVLEGNDLV IIE
//
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