LOCUS       YP_217495                525 aa            linear   BCT 23-SEP-2008
DEFINITION  bifunctional GMP synthase/glutamine amidotransferase protein
            [Salmonella enterica subsp. enterica serovar Choleraesuis str.
            SC-B67].
ACCESSION   YP_217495
VERSION     YP_217495.1  GI:62181078
DBSOURCE    REFSEQ: accession NC_006905.1
KEYWORDS    .
SOURCE      Salmonella enterica subsp. enterica serovar Choleraesuis str.
            SC-B67
  ORGANISM  Salmonella enterica subsp. enterica serovar Choleraesuis str.
            SC-B67
            Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
            Enterobacteriaceae; Salmonella; Salmonella enterica subsp. enterica
            serovar Choleraesuis.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Chiu,C.H., Tang,P., Chu,C., Hu,S., Bao,Q., Yu,J., Chou,Y.Y.,
            Wang,H.S. and Lee,Y.S.
  TITLE     The genome sequence of Salmonella enterica serovar Choleraesuis, a
            highly invasive and resistant zoonotic pathogen
  JOURNAL   Nucleic Acids Res. 33 (5), 1690-1698 (2005)
   PUBMED   15781495
REFERENCE   2  (residues 1 to 525)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (04-APR-2005) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Chiu,C.-H., Tang,P., Chu,C., Bao,Q., Hu,S., Yu,J., Chou,Y.-Y.,
            Wang,H.-S. and Lee,Y.-S.
  TITLE     Direct Submission
  JOURNAL   Submitted (03-SEP-2004) Chang Gung Genomic Medical Center, No. 5,
            Fu-Shing St., Kweishan, Taoyuan 333, Taiwan
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AAX66414.
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Salmonella enterica subsp. enterica serovar
                     Choleraesuis str. SC-B67"
                     /strain="SC-B67"
                     /serovar="Choleraesuis"
                     /sub_species="enterica"
                     /db_xref="taxon:321314"
     Protein         1..525
                     /product="bifunctional GMP synthase/glutamine
                     amidotransferase protein"
                     /EC_number="6.3.5.2"
                     /function="converts ATP and xanthosine 5'-phosphate and
                     L-glutamine and water to AMP and pyrophosphate diphosphate
                     and GMP and L-glutamate"
                     /calculated_mol_wt=58569
     Region          4..525
                     /region_name="guaA"
                     /note="bifunctional GMP synthase/glutamine
                     amidotransferase protein; Reviewed; PRK00074"
                     /db_xref="CDD:100349"
     Region          10..198
                     /region_name="GATase1_GMP_Synthase"
                     /note="Type 1 glutamine amidotransferase (GATase1) domain
                     found in GMP synthetase. GMP synthetase is a glutamine
                     amidotransferase from the de novo purine biosynthetic
                     pathway. Glutamine amidotransferase (GATase) activity
                     catalyse the transfer of ammonia from...; cd01742"
                     /db_xref="CDD:28854"
     Site            order(17..18,58..60,86..87,142,181)
                     /site_type="other"
                     /note="AMP/PPi binding site"
                     /db_xref="CDD:28854"
     Site            order(59,87)
                     /site_type="other"
                     /note="candidate oxyanion hole"
                     /db_xref="CDD:28854"
     Site            order(86,181,183)
                     /site_type="other"
                     /note="catalytic triad"
                     /db_xref="CDD:28854"
     Site            order(90,143,179)
                     /site_type="other"
                     /note="potential glutamine specificity residues"
                     /db_xref="CDD:28854"
     Region          229..524
                     /region_name="GMP_synthase_C"
                     /note="The C-terminal domain of GMP synthetase. It
                     contains two subdomains; the ATP pyrophosphatase domain
                     which closes to the N-termial and the dimerization domain
                     at C-terminal end. The ATP-PPase is a twisted,
                     five-stranded parallel beta-sheet sandwiched...; cd01997"
                     /db_xref="CDD:30184"
     Site            order(229..253,255..265,267..277,288..325,331..345,347,
                     356..365,370..394,400..414)
                     /site_type="other"
                     /note="ATP Binding subdomain"
                     /db_xref="CDD:30184"
     Site            order(233..235,237..240,258,260,381)
                     /site_type="other"
                     /note="Ligand Binding sites"
                     /db_xref="CDD:30184"
     Site            order(423..435,444..453,456..466,470..485,492..500,
                     502..524)
                     /site_type="other"
                     /note="Dimerization subdomain"
                     /db_xref="CDD:30184"
     CDS             1..525
                     /gene="guaA"
                     /locus_tag="SC2508"
                     /coded_by="complement(NC_006905.1:2643546..2645123)"
                     /note="contains glutamine-hydrolyzing domain and glutamine
                     amidotransferase; GMP-binding domain; functions to produce
                     GMP from XMP in the IMP pathway"
                     /transl_table=11
                     /db_xref="GeneID:3335004"
ORIGIN      
        1 mtenihkhri lildfgsqyt qlvarrvrel gvycelwawd vteaqirdfn psgiilsggp
       61 estteenspr apqyvfeagv pvfgvcygmq tmamqlgghv egsnerefgy aqvevltdsa
      121 lvrgiedslt adgkplldvw mshgdkvtai psdfvtvast escpfaiman eekrfygvqf
      181 hpevthtrqg mrmlerfvrd icqcealwtp akiiddavar ireqvgddkv ilglsggvds
      241 svtamllhra igknltcvfv dngllrlnea eqvmdmfgdh fglnivhvpa eerflsalag
      301 endpeakrki igrvfvevfd eealkledvk wlaqgtiypd viesaasatg kahvikshhn
      361 vgglpkemkm glveplkelf kdevrkigle lglpydmlyr hpfpgpglgv rvlgevkkey
      421 cdllrradai fieelrkadl ydkvsqaftv flpvrsvgvm gdgrkydwvv slravetidf
      481 mtahwahlpy dflgrvsnri inevngisrv vydisgkppa tiewe
//