BPL_METJA
ID BPL_METJA Reviewed; 237 AA.
AC Q59014;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative biotin ligase;
DE EC=6.3.4.15;
GN OrderedLocusNames=MJ1619;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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;
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99640.1; -; Genomic_DNA.
DR PIR; B64502; B64502.
DR RefSeq; WP_010871144.1; NC_000909.1.
DR PDB; 2EJ9; X-ray; 2.00 A; A=1-237.
DR PDBsum; 2EJ9; -.
DR AlphaFoldDB; Q59014; -.
DR SMR; Q59014; -.
DR STRING; 243232.MJ_1619; -.
DR EnsemblBacteria; AAB99640; AAB99640; MJ_1619.
DR GeneID; 1452528; -.
DR KEGG; mja:MJ_1619; -.
DR eggNOG; arCOG01940; Archaea.
DR HOGENOM; CLU_051096_3_1_2; -.
DR InParanoid; Q59014; -.
DR OMA; AVWKHIE; -.
DR OrthoDB; 42041at2157; -.
DR PhylomeDB; Q59014; -.
DR EvolutionaryTrace; Q59014; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IBA:GO_Central.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 3.30.930.10; -; 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 Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00121; birA_ligase; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biotin; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..237
FT /note="Putative biotin ligase"
FT /id="PRO_0000064982"
FT DOMAIN 1..191
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2EJ9"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2EJ9"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:2EJ9"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:2EJ9"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2EJ9"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 103..114
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2EJ9"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:2EJ9"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:2EJ9"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:2EJ9"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2EJ9"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2EJ9"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:2EJ9"
SQ SEQUENCE 237 AA; 27185 MW; 602506218437B1F6 CRC64;
MEIIHLSEID STNDYAKELA KEGKRNFIVL ADKQNNGKGR WGRVWYSDEG GLYFSMVLDS
KLYNPKVINL LVPICIIEVL KNYVDKELGL KFPNDIMVKV NDNYKKLGGI LTELTDDYMI
IGIGINVNNQ IRNEIREIAI SLKEITGKEL DKVEILSNFL KTFESYLEKL KNKEIDDYEI
LKKYKKYSIT IGKQVKILLS NNEIITGKVY DIDFDGIVLG TEKGIERIPS GICIHVR
