ID C2NMN7_BACCE Unreviewed; 162 AA.
AC C2NMN7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN ORFNames=bcere0004_39730 {ECO:0000313|EMBL:EEK54711.1};
OS Bacillus cereus BGSC 6E1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK54711.1};
RN [1] {ECO:0000313|EMBL:EEK54711.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK54711.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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}.
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:EEK54711.1}.
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DR EMBL; ACLU01000091; EEK54711.1; -; Genomic_DNA.
DR RefSeq; WP_000472870.1; NZ_CM000716.1.
DR AlphaFoldDB; C2NMN7; -.
DR GeneID; 75087327; -.
DR HOGENOM; CLU_016733_3_0_9; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000284; 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; 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; PS50968; BIOTINYL_LIPOYL; 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 85..161
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 162 AA; 17850 MW; 9B194D348C4B7040 CRC64;
MFKIQEVREL IKLIDSSNID EFEYKKDGTT IKMKKRGNEV VAVQAPVAKQ AVQPVAPVEV
ETTVAAAQVE VPKQEEKKAV QNENLHKITS PMVGTFYSSS SPDTPPYVSV GDRVSKDSIV
CIVEAMKLFN EIDADVDGEI VEILVNNGQL VEYGQPLFLV KA
//