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Database: UniProt
Entry: A0A0Q8F780_9GAMM
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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}.
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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
//
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