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Database: UniProt
Entry: A0A149W0T9_9PROT
LinkDB: A0A149W0T9_9PROT
Original site: A0A149W0T9_9PROT 
ID   A0A149W0T9_9PROT        Unreviewed;        72 AA.
AC   A0A149W0T9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
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:KXW58764.1};
GN   ORFNames=FEMY_07920 {ECO:0000313|EMBL:KXW58764.1};
OS   Ferrovum myxofaciens.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC   Ferrovum.
OX   NCBI_TaxID=416213 {ECO:0000313|EMBL:KXW58764.1, ECO:0000313|Proteomes:UP000075653};
RN   [1] {ECO:0000313|EMBL:KXW58764.1, ECO:0000313|Proteomes:UP000075653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z-31 {ECO:0000313|EMBL:KXW58764.1,
RC   ECO:0000313|Proteomes:UP000075653};
RA   Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.;
RT   "Genome sequence of the acidophilic iron oxidising Ferrovum strain Z-31.";
RL   Submitted (JAN-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:KXW58764.1}.
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DR   EMBL; LRRD01000011; KXW58764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A149W0T9; -.
DR   STRING; 1789004.FEMY_07920; -.
DR   PATRIC; fig|1789004.3.peg.801; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000075653; 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:UP000075653}.
FT   DOMAIN          1..70
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   72 AA;  7781 MW;  9F0AC7606E1127B1 CRC64;
     MVGTFYRSPS PGAPVFAEIG QSINEGQTLC IIEAMKLLNE IESDVTGFVK HILVENGQPI
     EYGQPLFVIA TA
//
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