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Database: UniProt
Entry: Q1LIU0_CUPMC
LinkDB: Q1LIU0_CUPMC
Original site: Q1LIU0_CUPMC 
ID   Q1LIU0_CUPMC            Unreviewed;       153 AA.
AC   Q1LIU0;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 75.
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:ABF09936.1};
GN   OrderedLocusNames=Rmet_3064 {ECO:0000313|EMBL:ABF09936.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF09936.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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|RuleBase:RU364072}.
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DR   EMBL; CP000352; ABF09936.1; -; Genomic_DNA.
DR   RefSeq; WP_011517564.1; NC_007973.1.
DR   AlphaFoldDB; Q1LIU0; -.
DR   STRING; 266264.Rmet_3064; -.
DR   KEGG; rme:Rmet_3064; -.
DR   eggNOG; COG0511; Bacteria.
DR   HOGENOM; CLU_016733_3_1_4; -.
DR   OMA; IKSPIIG; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002429; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT   DOMAIN          77..153
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   153 AA;  15976 MW;  456DC6374B1FA297 CRC64;
     MDLRKLKTLI DLVAESGISE LEVTEGEGKV RIVKQPPQVM AAPMAMPQYQ QLPAAPAVNV
     AGAPAAAAAE APQVPAGHVV TSPMVGTFYR APSPGAAPFV NVGDTVKEGQ TVCIIEAMKL
     LNEIECDKAG VIKEILVENG QAVEYGQPLF VIG
//
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