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Database: UniProt
Entry: A0A0W1QKY9_9SPHN
LinkDB: A0A0W1QKY9_9SPHN
Original site: A0A0W1QKY9_9SPHN 
ID   A0A0W1QKY9_9SPHN        Unreviewed;       231 AA.
AC   A0A0W1QKY9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=ATB93_10075 {ECO:0000313|EMBL:KTF69201.1};
OS   Sphingomonas sp. WG.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF69201.1, ECO:0000313|Proteomes:UP000052965};
RN   [1] {ECO:0000313|EMBL:KTF69201.1, ECO:0000313|Proteomes:UP000052965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WG {ECO:0000313|EMBL:KTF69201.1,
RC   ECO:0000313|Proteomes:UP000052965};
RA   Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.;
RT   "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing
RT   strain.";
RL   Submitted (NOV-2015) 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:KTF69201.1}.
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DR   EMBL; LNOS01000034; KTF69201.1; -; Genomic_DNA.
DR   RefSeq; WP_019367948.1; NZ_LNOS01000034.1.
DR   AlphaFoldDB; A0A0W1QKY9; -.
DR   Proteomes; UP000052965; 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:KTF69201.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052965}.
FT   DOMAIN          1..166
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   231 AA;  24066 MW;  78B5A12BC77CB1D8 CRC64;
     MIRTVAETGS TNADILSLAL TGAGEGLWLR AERQTAGKGR QGRAWVSPAG NLYISTLVRV
     RSTDPSSATL ALLSAVALEE AVRAFGVSPM LKWPNDLLVG GAKLSGILLE RAGDAIAVGI
     GVNLAAAPDG LDRAATSLAA QGVTVAPDIF AEVLAESFGR WLERWRGEGV WPVRERWLAR
     AHPEGTALTA RLADGSSFDG LFGGLDSSGA LILRLADGTT RAIHAGDVFL L
//
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