(data stored in ACNUC7421 zone)

SWISSPROT: Q8XBJ9_ECO57

ID   Q8XBJ9_ECO57            Unreviewed;       554 AA.
AC   Q8XBJ9; Q7AGM9;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   30-AUG-2017, entry version 110.
DE   SubName: Full=Asparagine synthetase B {ECO:0000313|EMBL:AAG54996.1};
GN   Name=asnB {ECO:0000313|EMBL:AAG54996.1};
GN   OrderedLocusNames=ECs0704 {ECO:0000313|EMBL:BAB34127.1}, Z0821
GN   {ECO:0000313|EMBL:AAG54996.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|Proteomes:UP000002519};
RN   [1] {ECO:0000313|EMBL:BAB34127.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558}, and Sakai
RC   {ECO:0000313|EMBL:BAB34127.1};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [2] {ECO:0000313|EMBL:AAG54996.1, ECO:0000313|Proteomes:UP000002519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EDL933 {ECO:0000313|EMBL:AAG54996.1}, and O157:H7 / EDL933 /
RC   ATCC 700927 / EHEC {ECO:0000313|Proteomes:UP000002519};
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G.III., Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
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DR   EMBL; AE005174; AAG54996.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34127.1; -; Genomic_DNA.
DR   PIR; H85566; H85566.
DR   PIR; H90716; H90716.
DR   RefSeq; NP_308731.1; NC_002695.1.
DR   RefSeq; WP_000337047.1; NZ_MWVM01000011.1.
DR   STRING; 155864.Z0821; -.
DR   EnsemblBacteria; AAG54996; AAG54996; Z0821.
DR   EnsemblBacteria; BAB34127; BAB34127; BAB34127.
DR   GeneID; 917073; -.
DR   KEGG; ece:Z0821; -.
DR   KEGG; ecs:ECs0704; -.
DR   PATRIC; fig|386585.9.peg.815; -.
DR   eggNOG; ENOG4105CAQ; Bacteria.
DR   eggNOG; COG0367; LUCA.
DR   HOGENOM; HOG000027493; -.
DR   KO; K01953; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IEA:InterPro.
DR   CDD; cd01991; Asn_Synthase_B_C; 1.
DR   CDD; cd00712; AsnB; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR006426; Asn_synth_AEB.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR033738; AsnB_N.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   PIRSF; PIRSF001589; Asn_synthetase_glu-h; 2.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01536; asn_synth_AEB; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   4: Predicted;
DR   PRODOM; Q8XBJ9.
DR   SWISS-2DPAGE; Q8XBJ9.
KW   Amino-acid biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1};
KW   Asparagine biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1};
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR001589-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558,
KW   ECO:0000313|Proteomes:UP000002519};
KW   Glutamine amidotransferase {ECO:0000256|PIRSR:PIRSR001589-1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR001589-2}.
FT   DOMAIN        2    186       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   NP_BIND     347    348       ATP. {ECO:0000256|PIRSR:PIRSR001589-2}.
FT   ACT_SITE      2      2       For GATase activity. {ECO:0000256|PIRSR:
FT                                PIRSR001589-1}.
FT   BINDING      99     99       Glutamine. {ECO:0000256|PIRSR:
FT                                PIRSR001589-2}.
FT   BINDING     233    233       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR001589-2}.
FT   BINDING     273    273       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR001589-
FT                                2}.
FT   SITE        349    349       Important for beta-aspartyl-AMP
FT                                intermediate formation.
FT                                {ECO:0000256|PIRSR:PIRSR001589-3}.
SQ   SEQUENCE   554 AA;  62673 MW;  B164A2B065D41ED1 CRC64;
     MCSIFGVFDI KTDAVELRKK ALELSRLMRH RGPDWSGIYA SDKAILAHER LSIVDVNAGA
     QPLYNQQKTH VLAVNGEIYN HQALRAEYGD RYQFQTGSDC EVILALYQEK GPEFLDDLQG
     MFAFALYDSE KDAYLIGRDH LGIIPLYMGY DEHGQLYVAS EMKALVPVCR TIKEFPAGSY
     LWSQDGEIRS YYHRDWFDFD AVKDNVTDKN ELRQALEDSV KSHLMSDVPY GVLLSGGLDS
     SIISAITKKY AARRVEDQER SEAWWPQLHS FAVGLPGSPD LKAAQEVANH LGTVHHEIHF
     TVQEGLDAIR DVIYHIETYD VTTIRASTPM YLMSRKIKAM GIKMVLSGEG SDEVFGGYLY
     FHKAPNAKEL HEETVRKLLA LHMYDCARAN KAMSAWGVEA RVPFLDKKFL DVAMRINPQD
     KMCGNGKMEK HILRECFESY LPASVAWRQK EQFSDGVGYS WIDTLKEVAA QQVSDQQLET
     ARFRFPYNTP TSKEAYLYRE IFEELFPLPS AAECVPGGPS VACSSAKAIE WDEAFKKMDD
     PSGRAVGVHQ SAYK
//

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