ID M1LVH4_9PROT Unreviewed; 278 AA.
AC M1LVH4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=CDSE_0132 {ECO:0000313|EMBL:AGF47239.1};
OS Candidatus Kinetoplastibacterium desouzaii TCC079E.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208919 {ECO:0000313|EMBL:AGF47239.1, ECO:0000313|Proteomes:UP000011547};
RN [1] {ECO:0000313|EMBL:AGF47239.1, ECO:0000313|Proteomes:UP000011547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC079E {ECO:0000313|EMBL:AGF47239.1,
RC ECO:0000313|Proteomes:UP000011547};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(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; CP003803; AGF47239.1; -; Genomic_DNA.
DR RefSeq; WP_015396650.1; NC_020294.1.
DR AlphaFoldDB; M1LVH4; -.
DR STRING; 1208919.CDSE_0132; -.
DR KEGG; kde:CDSE_0132; -.
DR PATRIC; fig|1208919.3.peg.684; -.
DR eggNOG; COG0340; Bacteria.
DR HOGENOM; CLU_051096_3_1_4; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000011547; 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 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 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; 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}.
FT DOMAIN 19..204
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 278 AA; 31724 MW; 39F5523EA0351B1B CRC64;
MPSISFEKNK LLLKKIEKEL YMFNKILWTN DTSSTNLDLL NMIKNKNVEL PCLIGTNHQY
AGKGRQGKSW LSNNDLMFSC GFKIRIPSFN LSSIAIVAGI SACESLKKIA GNKGLELNLK
WPNDIQWKEK KLSGILVETI KDKKENNIHN IVLGIGVNLN DALYKSQILH RSVADWSEIT
NNIKPEQIVK IITTICISWY KDMYLLQNYG LKIFYDRFNR IDFLFGKRIN VEENGIKTQN
GIAEGINELG HLTIKTMSGK ESVYFGNVSI NCKNDHFN
//
