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Database: UniProt
Entry: A0A1E3LUG1_9SPHN
LinkDB: A0A1E3LUG1_9SPHN
Original site: A0A1E3LUG1_9SPHN 
ID   A0A1E3LUG1_9SPHN        Unreviewed;       160 AA.
AC   A0A1E3LUG1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN   ORFNames=BFL28_18175 {ECO:0000313|EMBL:ODP37401.1};
OS   Sphingomonas turrisvirgatae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1888892 {ECO:0000313|EMBL:ODP37401.1, ECO:0000313|Proteomes:UP000094487};
RN   [1] {ECO:0000313|EMBL:ODP37401.1, ECO:0000313|Proteomes:UP000094487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCT13 {ECO:0000313|EMBL:ODP37401.1,
RC   ECO:0000313|Proteomes:UP000094487};
RA   D'Andrea M.M., Rossolini G.M., Thaller M.C.;
RT   "Draft genome of the agarase producing Sphingomonas sp. MCT13.";
RL   Submitted (AUG-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}.
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:ODP37401.1}.
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DR   EMBL; MDDS01000031; ODP37401.1; -; Genomic_DNA.
DR   RefSeq; WP_069320850.1; NZ_MDDS01000031.1.
DR   AlphaFoldDB; A0A1E3LUG1; -.
DR   STRING; 1888892.BFL28_18175; -.
DR   OrthoDB; 9811735at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000094487; 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   Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU364072};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094487}.
FT   DOMAIN          84..160
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          57..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   160 AA;  16533 MW;  0049EA7B5488D96D CRC64;
     MSEDSKGMHV DIELVRQLAS VLDDTNLTEI EVEDGDRKVR VARKAAAPAA VAYAPPPMAQ
     PAPAAAAPAA AMPSDPTQIT PAHENAVKSP MVGTAYLAAE PGAKPFIAVG AQVKAGETLL
     IVEAMKVMNP IAAPHGGTVK AILIENGQPV EFDQPLVVVE
//
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