(data stored in SCRATCH zone)

SWISSPROT: D3VHN2_XENNA

ID   D3VHN2_XENNA            Unreviewed;       319 AA.
AC   D3VHN2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Bifunctional ligase/repressor BirA {ECO:0000256|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin operon repressor {ECO:0000256|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000256|HAMAP-Rule:MF_00978};
DE            EC=6.3.4.15 {ECO:0000256|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin--protein ligase {ECO:0000256|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase {ECO:0000256|HAMAP-Rule:MF_00978};
GN   Name=birA {ECO:0000256|HAMAP-Rule:MF_00978,
GN   ECO:0000313|EMBL:CBJ88371.1};
GN   OrderedLocusNames=XNC1_0288 {ECO:0000313|EMBL:CBJ88371.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88371.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88371.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase
CC       and a biotin-operon repressor. In the presence of ATP, BirA
CC       activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-
CC       5'-AMP or holoBirA) complex. HoloBirA can either transfer the
CC       biotinyl moiety to the biotin carboxyl carrier protein (BCCP)
CC       subunit of acetyl-CoA carboxylase, or bind to the biotin operator
CC       site and inhibit transcription of the operon. {ECO:0000256|HAMAP-
CC       Rule:MF_00978}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate +
CC         H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756,
CC         Rhea:RHEA-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|HAMAP-Rule:MF_00978};
CC   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00978}.
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DR   EMBL; FN667742; CBJ88371.1; -; Genomic_DNA.
DR   RefSeq; WP_010847799.1; NC_014228.1.
DR   STRING; 406817.XNC1_0288; -.
DR   EnsemblBacteria; CBJ88371; CBJ88371; XNC1_0288.
DR   KEGG; xne:XNC1_0288; -.
DR   eggNOG; ENOG4105HJX; Bacteria.
DR   eggNOG; COG0340; LUCA.
DR   eggNOG; COG1654; LUCA.
DR   HOGENOM; HOG000041812; -.
DR   KO; K03524; -.
DR   OMA; RAAVWKH; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009305; P:protein biotinylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd16442; BPL; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00978; Bifunct_BirA; 1.
DR   InterPro; IPR030855; Bifunct_BirA.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR004409; Biotin_operon_repress_HTH.
DR   InterPro; IPR003142; BPL_C.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR008988; Transcriptional_repressor_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF02237; BPL_C; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF50037; SSF50037; 1.
DR   TIGRFAMs; TIGR00121; birA_ligase; 1.
DR   TIGRFAMs; TIGR00122; birA_repr_reg; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VHN2.
DR   SWISS-2DPAGE; D3VHN2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Biotin {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00978, ECO:0000313|EMBL:CBJ88371.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Repressor {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00978}.
FT   DOMAIN       66    254       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
FT   DNA_BIND     22     41       H-T-H motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
FT   REGION       89     91       Biotin binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
FT   REGION      116    118       Biotin binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
FT   BINDING     112    112       Biotin. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
FT   BINDING     183    183       Biotin. {ECO:0000256|HAMAP-Rule:
FT                                MF_00978}.
SQ   SEQUENCE   319 AA;  35268 MW;  5A2639392C6B60B5 CRC64;
     MKDISIPLRL IKVLSDGETH SGQQLGQELG MSRAAINKHI QTIREWGVEI LTLPGKGYHF
     PAPMNLLDKD IIANYLPNDC IAVIPVIDST NQYLLDQLAS LNSGDACVAE YQYAGRGRRG
     RQWVSAFGRN LYLSMYWRLD QGPAAAVGLS LVVGIVIAEV LNRLGAERVK VKWPNDLYLD
     DKKLAGILVE LTGKTGDAAQ IVIGIGMNIS MSSEQQELIN QQWTNLQQAG MSVERNKLIA
     EIIVELKEAL LQFENEGLVP FISRWLKLDN FINRKVKLII GEQEIYGIAR GIDQQGALLL
     DINGVITPHI GGEISLRGC
//

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