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Database: UniProt
Entry: B0CLN1_BRUSI
LinkDB: B0CLN1_BRUSI
Original site: B0CLN1_BRUSI 
ID   B0CLN1_BRUSI            Unreviewed;       156 AA.
AC   B0CLN1;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 65.
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:ABY38011.1};
GN   OrderedLocusNames=BSUIS_A0946 {ECO:0000313|EMBL:ABY38011.1};
OS   Brucella suis (strain ATCC 23445 / NCTC 10510).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=470137 {ECO:0000313|EMBL:ABY38011.1, ECO:0000313|Proteomes:UP000008545};
RN   [1] {ECO:0000313|EMBL:ABY38011.1, ECO:0000313|Proteomes:UP000008545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23445 / NCTC 10510 {ECO:0000313|Proteomes:UP000008545};
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL   Submitted (DEC-2007) 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|ARBA:ARBA00003761, 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; CP000911; ABY38011.1; -; Genomic_DNA.
DR   RefSeq; WP_002964036.1; NC_010169.1.
DR   AlphaFoldDB; B0CLN1; -.
DR   GeneID; 58775980; -.
DR   KEGG; bmt:BSUIS_A0946; -.
DR   PATRIC; fig|359391.4.peg.963; -.
DR   HOGENOM; CLU_016733_3_1_5; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000008545; Chromosome I.
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          80..156
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   156 AA;  16267 MW;  B0CDB881D80AF5AD CRC64;
     MSSKNSVIDK ETIRDLADIL NETDLTDIEV EHGDLRIRVS RKVTVQAAAT VMPAVAPAAV
     AAPAAATASA SEPSKADLAK NAVPSPMVGT AYLAPAPGAR NFIEVGTQVK EGQTLLIIEA
     MKTMNQIPAP RAGTVKAILV EDAQPVEFGE PLVVIE
//
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