(data stored in SCRATCH zone)

SWISSPROT: B7UKU6_ECO27

ID   B7UKU6_ECO27            Unreviewed;       554 AA.
AC   B7UKU6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   SubName: Full=Asparagine synthetase B {ECO:0000313|EMBL:CAS08104.1};
GN   Name=asnB {ECO:0000313|EMBL:CAS08104.1};
GN   OrderedLocusNames=E2348C_0556 {ECO:0000313|EMBL:CAS08104.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08104.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08104.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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DR   EMBL; FM180568; CAS08104.1; -; Genomic_DNA.
DR   RefSeq; WP_000337076.1; NC_011601.1.
DR   EnsemblBacteria; CAS08104; CAS08104; E2348C_0556.
DR   KEGG; ecg:E2348C_0556; -.
DR   HOGENOM; HOG000027493; -.
DR   KO; K01953; -.
DR   OMA; ELKCLHP; -.
DR   BioCyc; ECOL574521:E2348C_RS02950-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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; B7UKU6.
DR   SWISS-2DPAGE; B7UKU6.
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:UP000008205};
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;  62643 MW;  5391B27B93BC8DDE CRC64;
     MCSIFGVFDI KTDAVELRKK ALELSRLMRH RGPDWSGIYA SDNAILAHER LSIVDVNAGA
     QPLYNQQKTH VLAVNGEIYN HQALRAEYGD RYQFQTGSDC EVILALYQEK GPEFLDDLQG
     MFAFALYDSE KDAYLIGRDH LGIIPLYMGY DEHGQLYVAS EMKALVPVCR TIKEFPAGSY
     LWSQDGEIRS YYHRDWFDYD AVKDNVTDKN ELRQALEDSV KSHLMSDVPY GVLLSGGLDS
     SIISAITKKY AARRVEDQER SEAWWPQLHS FAVGLPGSPD LKAAQEVANH LGTVHHEIHF
     TVQEGLDAIR DVIYHIETYD VTTIRASTPM YLMSRKIKAM GIKMVLSGEG SDEVFGGYLY
     FHKAPNAKEL HEETVRKLLA LHMYDCARAN KAMSAWGVEA RVPFLDKKFL DVAMRINPQD
     KMCGNGKMEK HILRECFEAY LPASVAWRQK EQFSDGVGYS WIDTLKEVAA QQVSDQQLET
     ARFRFPFNTP TSKEAYLYRE IFEELFPLPS AAECVPGGPS VACSSAKAIE WDEAFKKMDD
     PSGRAVGVHQ SAYK
//

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