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Database: UniProt
Entry: F8LVE2_STRTR
LinkDB: F8LVE2_STRTR
Original site: F8LVE2_STRTR 
ID   F8LVE2_STRTR            Unreviewed;       162 AA.
AC   F8LVE2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN   Name=accB {ECO:0000313|EMBL:CCC19229.1};
GN   ORFNames=STH8232_0497 {ECO:0000313|EMBL:CCC19229.1};
OS   Streptococcus thermophilus JIM 8232.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1051074 {ECO:0000313|EMBL:CCC19229.1, ECO:0000313|Proteomes:UP000000300};
RN   [1] {ECO:0000313|EMBL:CCC19229.1, ECO:0000313|Proteomes:UP000000300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JIM 8232 {ECO:0000313|EMBL:CCC19229.1,
RC   ECO:0000313|Proteomes:UP000000300};
RA   Renault P., Loux V.;
RT   "Complete genome sequence of Streptococcus thermophilus strain JIM8232.";
RL   Submitted (JUN-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}.
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DR   EMBL; FR875178; CCC19229.1; -; Genomic_DNA.
DR   RefSeq; WP_011680783.1; NC_017581.1.
DR   AlphaFoldDB; F8LVE2; -.
DR   KEGG; stu:STH8232_0497; -.
DR   PATRIC; fig|1051074.3.peg.402; -.
DR   HOGENOM; CLU_016733_3_2_9; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000300; Chromosome.
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   NCBIfam; TIGR00531; BCCP; 1.
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          86..162
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   162 AA;  16945 MW;  56B480B32B397136 CRC64;
     MNISEIKDLL AQFDASTLRE FSYKNNGEEL NLSKNQTSSV TTSPVAPTVE VVASSPQVPV
     APVAAPAAVE TPATPVEEAS AQAAEGEVVE SPLVGVAYLS PSPEKPAFVS VGDTVKKGQT
     LLIVEAMKVM NEVPAPKDGV ITEILVANEE VVDYGKGLVR IK
//
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