ID A0A0Q8F780_9GAMM Unreviewed; 159 AA.
AC A0A0Q8F780;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN ORFNames=ASD77_07975 {ECO:0000313|EMBL:KRA54519.1};
OS Pseudoxanthomonas sp. Root65.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1736576 {ECO:0000313|EMBL:KRA54519.1, ECO:0000313|Proteomes:UP000051430};
RN [1] {ECO:0000313|EMBL:KRA54519.1, ECO:0000313|Proteomes:UP000051430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root65 {ECO:0000313|EMBL:KRA54519.1,
RC ECO:0000313|Proteomes:UP000051430};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA54519.1, ECO:0000313|Proteomes:UP000051430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root65 {ECO:0000313|EMBL:KRA54519.1,
RC ECO:0000313|Proteomes:UP000051430};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KRA54519.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMHA01000001; KRA54519.1; -; Genomic_DNA.
DR RefSeq; WP_055939731.1; NZ_LMHA01000001.1.
DR AlphaFoldDB; A0A0Q8F780; -.
DR STRING; 1736576.ASD77_07975; -.
DR OrthoDB; 9811735at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000051430; Unassembled WGS sequence.
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 Ligase {ECO:0000313|EMBL:KRA54519.1};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW Lipid metabolism {ECO:0000256|RuleBase:RU364072};
KW Reference proteome {ECO:0000313|Proteomes:UP000051430}.
FT DOMAIN 83..159
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 159 AA; 16588 MW; 2C3FB53BCF5DDD78 CRC64;
MDLRKIKKLI DLLEESNLAE IEIKEGEESV RLARTPKGGY AAPAAPAPVA YAEPRPAAPM
PMSSPTEAST GGTAKAGNAL PDGHVVRAPM VGTFYASPSP DKPSFVSIGQ AVKAGETLAI
IEAMKMFNPI EADVSGTVLS ILAESGQPIE FDQPLFVIG
//