ID A0A0X8X706_HALHR Unreviewed; 163 AA.
AC A0A0X8X706;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN ORFNames=HH1059_01250 {ECO:0000313|EMBL:BAU56797.1};
OS Halorhodospira halochloris (Ectothiorhodospira halochloris).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=1052 {ECO:0000313|EMBL:BAU56797.1, ECO:0000313|Proteomes:UP000218890};
RN [1] {ECO:0000313|Proteomes:UP000218890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-1059 {ECO:0000313|Proteomes:UP000218890};
RA Tsukatani Y.;
RT "Halorhodospira halochloris DSM-1059 complete genome sequence.";
RL Submitted (FEB-2016) 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; AP017372; BAU56797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X8X706; -.
DR KEGG; hhk:HH1059_01250; -.
DR OrthoDB; 9811735at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000218890; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000218890}.
FT DOMAIN 86..162
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 17..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..63
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 163 AA; 17701 MW; 7A9650C302620B89 CRC64;
MDIRKIKRLI ELLDESGIHE IEIAEGEESV RITRNSPQPS PPPAQMGYPP YPQPAPAPQP
AAEPQPSATS TGSETPTEPG EEEPEGEPIR SPMVGTFYRS PSPTSKPFVE VGQKVRAGDT
LCIIEAMKML NQIEADRDGV VTAVLVENGQ PVEFDQPLFL VSN
//
