ID D8P4H0_RALSL Unreviewed; 162 AA.
AC D8P4H0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 08-NOV-2023, entry version 49.
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:CBJ53806.1};
GN ORFNames=RCFBP_mp20380 {ECO:0000313|EMBL:CBJ53806.1};
OS Ralstonia solanacearum CFBP2957.
OG Plasmid RCFBPv3_mp {ECO:0000313|EMBL:CBJ53806.1}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=859656 {ECO:0000313|EMBL:CBJ53806.1};
RN [1] {ECO:0000313|EMBL:CBJ53806.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFBP2957 {ECO:0000313|EMBL:CBJ53806.1};
RC PLASMID=RCFBPv3_mp {ECO:0000313|EMBL:CBJ53806.1};
RX PubMed=20550686; DOI=10.1186/1471-2164-11-379;
RA Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E.,
RA Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G.,
RA Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.;
RT "Genomes of three tomato pathogens within the Ralstonia solanacearum
RT species complex reveal significant evolutionary divergence.";
RL BMC Genomics 11:379-379(2010).
RN [2] {ECO:0000313|EMBL:CBJ53806.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFBP2957 {ECO:0000313|EMBL:CBJ53806.1};
RC PLASMID=RCFBPv3_mp {ECO:0000313|EMBL:CBJ53806.1};
RA Genoscope - CEA;
RL Submitted (FEB-2010) 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; FP885907; CBJ53806.1; -; Genomic_DNA.
DR RefSeq; WP_013208310.1; NZ_CP115953.1.
DR AlphaFoldDB; D8P4H0; -.
DR PATRIC; fig|859656.5.peg.4195; -.
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; 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 Ligase {ECO:0000313|EMBL:CBJ53806.1};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW Lipid metabolism {ECO:0000256|RuleBase:RU364072};
KW Plasmid {ECO:0000313|EMBL:CBJ53806.1}.
FT DOMAIN 86..162
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 61..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 162 AA; 16989 MW; 8D668F3520C80709 CRC64;
MDLSQIKQLI DVMASSDLAE MSFSYQGWVL RLVRHPSAGQ CGGAETASPA LPAGARPTPA
ALAAAAVQQS SQSQTQPQPV AAAPQQRELL APMFGVVHLR PAPGEPVFVQ RGQTVQAGQT
VCVIEAMKVF NAVVAEHDGT VETVLVESGT EVEAGQPLFR FA
//
