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Database: UniProt
Entry: Q47PS0_THEFY
LinkDB: Q47PS0_THEFY
Original site: Q47PS0_THEFY 
ID   Q47PS0_THEFY            Unreviewed;       120 AA.
AC   Q47PS0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN   OrderedLocusNames=Tfu_1513 {ECO:0000313|EMBL:AAZ55549.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ55549.1};
RN   [1] {ECO:0000313|EMBL:AAZ55549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ55549.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) 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|RuleBase:RU364072}.
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DR   EMBL; CP000088; AAZ55549.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47PS0; -.
DR   STRING; 269800.Tfu_1513; -.
DR   KEGG; tfu:Tfu_1513; -.
DR   eggNOG; COG0511; Bacteria.
DR   HOGENOM; CLU_2048617_0_0_11; -.
DR   UniPathway; UPA00094; -.
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; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR01071; ACOABIOTINCC.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
PE   4: Predicted;
KW   Biotin {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          44..117
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00364"
SQ   SEQUENCE   120 AA;  12792 MW;  56973B736961BD74 CRC64;
     MGLFGERVVE RKFYGSGGQG TGRPGSATGI RRSMQGAGMP ATRVITSPVS GHFYRRPKPD
     APPFVEEGQR VEAGQTIGMV EAAKQFTEVK SVSSGTLAEF AVHDRQKLAE GDTIARIAEP
//
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