ID A0A1J5BZW0_9BURK Unreviewed; 304 AA.
AC A0A1J5BZW0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=biotin--[biotin carboxyl-carrier protein] ligase {ECO:0000256|ARBA:ARBA00024227};
DE EC=6.3.4.15 {ECO:0000256|ARBA:ARBA00024227};
GN ORFNames=AUK50_14425 {ECO:0000313|EMBL:OIP12919.1};
OS Comamonadaceae bacterium CG2_30_57_122.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1805089 {ECO:0000313|EMBL:OIP12919.1, ECO:0000313|Proteomes:UP000182154};
RN [1] {ECO:0000313|EMBL:OIP12919.1, ECO:0000313|Proteomes:UP000182154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_57_122 {ECO:0000313|EMBL:OIP12919.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) +
CC N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215;
CC EC=6.3.4.15; Evidence={ECO:0000256|ARBA:ARBA00000933};
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:OIP12919.1}.
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DR EMBL; MNXW01000327; OIP12919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5BZW0; -.
DR Proteomes; UP000182154; Unassembled WGS sequence.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR008988; Transcriptional_repressor_C.
DR NCBIfam; TIGR00121; birA_ligase; 1.
DR PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF50037; C-terminal domain of transcriptional repressors; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 2.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OIP12919.1}.
FT DOMAIN 150..190
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|Pfam:PF03099"
FT DOMAIN 254..294
FT /note="Biotin protein ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02237"
FT REGION 84..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 31640 MW; B169A895C691B07F CRC64;
MNPMLSPVRW PCEAIWQALE PLLPGFTVEV LPEVDSTNSE LMRRARAGQT DPVLLVTERQ
TAGRGRLGRQ WVSGSAAHAV ASVGDQGFTA GPPQGETAPP GGSAAHAVAS VGAIPSLTFS
LGLNLAPTDW SGLSLAVGLS VAQSLHPDLV LKWPNDLWWH DRKLAGILIE TANCAATSAS
RYVVIGIGIN LLAPQSTGLS TAPAGLEELM PGVDASQALL QIAAPLVHTV QTFEARGFAP
FVSAFNQRDA LAQVAVTLSD GVQGVAQGVD ATGALLVATP KGVQRVTSAE VSVRLQEGPR
YDQL
//
