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Database: UniProt
Entry: M4SAS6_9SPHN
LinkDB: M4SAS6_9SPHN
Original site: M4SAS6_9SPHN 
ID   M4SAS6_9SPHN            Unreviewed;       163 AA.
AC   M4SAS6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=G432_00235 {ECO:0000313|EMBL:AGH47777.1};
OS   Sphingomonas sp. MM-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH47777.1, ECO:0000313|Proteomes:UP000011816};
RN   [1] {ECO:0000313|EMBL:AGH47777.1, ECO:0000313|Proteomes:UP000011816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MM-1 {ECO:0000313|EMBL:AGH47777.1};
RX   PubMed=23682148;
RA   Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT   "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT   Bacterium Sphingomonas sp. Strain MM-1.";
RL   Genome Announc. 1:E00247-13(2013).
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};
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DR   EMBL; CP004036; AGH47777.1; -; Genomic_DNA.
DR   AlphaFoldDB; M4SAS6; -.
DR   STRING; 745310.G432_00235; -.
DR   KEGG; sphm:G432_00235; -.
DR   PATRIC; fig|745310.14.peg.50; -.
DR   eggNOG; COG0340; Bacteria.
DR   HOGENOM; CLU_051096_3_3_5; -.
DR   Proteomes; UP000011816; Chromosome.
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   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR003142; BPL_C.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR008988; Transcriptional_repressor_C.
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:AGH47777.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011816}.
FT   DOMAIN          1..98
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   163 AA;  17117 MW;  2553B7813D002D8D CRC64;
     MVAALALHQV AIAYGGEGRT SLKWPNDLLL DGAKLSGILL ESCDGAIVIG FGVNLAHSPE
     GLDRTTASFA AAGLGAPDPD AFLMDLADAF ARWLGRWRNE GLAAIRREWL ARAHPPGTPL
     RTTGPDGQVV DGLFEGLDES GALKLRLADG SVHLLHAGDV FLI
//
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