(data stored in SCRATCH zone)

SWISSPROT: D3UYI4_XENBS

ID   D3UYI4_XENBS            Unreviewed;       469 AA.
AC   D3UYI4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   13-FEB-2019, entry version 51.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356};
DE            EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN   Name=glnA {ECO:0000313|EMBL:CBJ79362.1};
GN   OrderedLocusNames=XBJ1_0211 {ECO:0000313|EMBL:CBJ79362.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79362.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79362.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79362.1,
RC   ECO:0000313|Proteomes:UP000002045};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216;
CC         EC=6.3.1.2; Evidence={ECO:0000256|RuleBase:RU004356};
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexagons. {ECO:0000256|RuleBase:RU000387}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000387}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; FN667741; CBJ79362.1; -; Genomic_DNA.
DR   RefSeq; WP_012986826.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0211; -.
DR   EnsemblBacteria; CBJ79362; CBJ79362; XBJ1_0211.
DR   GeneID; 8829834; -.
DR   KEGG; xbo:XBJ1_0211; -.
DR   PATRIC; fig|406818.4.peg.192; -.
DR   eggNOG; ENOG4105C5F; Bacteria.
DR   eggNOG; COG0174; LUCA.
DR   HOGENOM; HOG000005157; -.
DR   KO; K01915; -.
DR   OMA; IEAAWNT; -.
DR   BioCyc; XBOV406818:XBJ1_RS00915-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; -; 1.
DR   InterPro; IPR008147; Gln_synt_b-grasp.
DR   InterPro; IPR036651; Gln_synt_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR004809; Gln_synth_I.
DR   InterPro; IPR001637; Gln_synth_I_adenylation_site.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; SSF54368; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR00653; GlnA; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00182; GLNA_ADENYLATION; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UYI4.
DR   SWISS-2DPAGE; D3UYI4.
KW   ATP-binding {ECO:0000256|RuleBase:RU004356};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|RuleBase:RU000387};
KW   Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:CBJ79362.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004356};
KW   Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN      102    379       Gln-synt_C. {ECO:0000259|SMART:SM01230}.
FT   MOD_RES     398    398       O-AMP-tyrosine. {ECO:0000256|PIRSR:
FT                                PIRSR604809-50}.
SQ   SEQUENCE   469 AA;  51965 MW;  8DFCBB70B02DBB74 CRC64;
     MSVEHVLSMI EEHQVKFIDL RFTDTKGKEQ HITIPSHQID EDFFEDGKMF DGSSIGGWKG
     INESDMVLMP DPTTAMRDPF FDDATLILRC DILEPGTMQG YSRDPRSIAK RAEDFLRASD
     IADTVLFGPE PEFFLFDDIR FGNSISGSYY HIDDIEAAWN SGTRYEGGNK GHRPGIKGGY
     FPVPPVDSSQ DLRSAMCLTM EKMGLVVEAH HHEVATAGQN EIATRFNTMT KKADETQIYK
     YVVHNVAHSF GKTATFMPKP LVGDNGSGMH CHMSLSKNGT NLFAGDKYGG LSELALYYIG
     GVIKHARALN AFTNPTTNSY KRLVPGFEAP VMLAYSARNR SASIRIPVVA SAKARRIEVR
     FPDPAANPYL SFSALLMAGL DGIINKIHPG DAMDKNLYDL PAEEAQEIPT VASSLDDALA
     ALDADREFLT RGGVFTDDAI DAYIKLLHGE IERVRMTPHP LEFELYYSV
//

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