ID A0A099FDA3_9RHOB Unreviewed; 255 AA.
AC A0A099FDA3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=IC63_05765 {ECO:0000313|EMBL:KGJ08186.1};
OS Paracoccus sphaerophysae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=690417 {ECO:0000313|EMBL:KGJ08186.1, ECO:0000313|Proteomes:UP000029917};
RN [1] {ECO:0000313|EMBL:KGJ08186.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ08186.1,
RC ECO:0000313|Proteomes:UP000029917};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ08186.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ08186.1,
RC ECO:0000313|Proteomes:UP000029917};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KGJ08186.1}.
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DR EMBL; JRKS01000012; KGJ08186.1; -; Genomic_DNA.
DR RefSeq; WP_036717785.1; NZ_JRKS01000012.1.
DR AlphaFoldDB; A0A099FDA3; -.
DR STRING; 690417.IC63_05765; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000029917; 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; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KGJ08186.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029917}.
FT DOMAIN 1..190
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 255 AA; 26629 MW; 960FF07DFE39560C CRC64;
MTESPDWPAG VARHVLPRID STNAEALRLA ATLSGPTWIM AREQTAGRGR RGRAWRDPQG
NLAATLLIRP TGSPADASLY SFVAALALHE ALVATCGPAA RVQIKWPNDG LLNGGKVAGI
LLESAGQGAR VTALAIGIGV NLAAAPDPTT LEPGATPPVS VLGETGHAVT ADQFLDLLAP
AFARWQAQLE TWGFAPIRSA WLARAARLGQ PVTARTGRDT RHGTFEGIDD SGALILTTPA
GRETIPAADI HFHEA
//
