ID   GUAA_SCHPO              Reviewed;         539 AA.
AC   Q9P772;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=gua1; ORFNames=SPAP7G5.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC         H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329670; CAB88269.1; -; Genomic_DNA.
DR   RefSeq; NP_594312.1; NM_001019735.2.
DR   AlphaFoldDB; Q9P772; -.
DR   SMR; Q9P772; -.
DR   BioGRID; 279029; 3.
DR   STRING; 4896.SPAP7G5.02c.1; -.
DR   MEROPS; C26.957; -.
DR   iPTMnet; Q9P772; -.
DR   MaxQB; Q9P772; -.
DR   PaxDb; Q9P772; -.
DR   PRIDE; Q9P772; -.
DR   EnsemblFungi; SPAP7G5.02c.1; SPAP7G5.02c.1:pep; SPAP7G5.02c.
DR   GeneID; 2542573; -.
DR   KEGG; spo:SPAP7G5.02c; -.
DR   PomBase; SPAP7G5.02c; -.
DR   VEuPathDB; FungiDB:SPAP7G5.02c; -.
DR   eggNOG; KOG1622; Eukaryota.
DR   HOGENOM; CLU_014340_0_5_1; -.
DR   InParanoid; Q9P772; -.
DR   OMA; KRKIIGH; -.
DR   PhylomeDB; Q9P772; -.
DR   Reactome; R-SPO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   Reactome; R-SPO-9748787; Azathioprine ADME.
DR   UniPathway; UPA00189; UER00296.
DR   PRO; PR:Q9P772; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006543; P:glutamine catabolic process; IC:PomBase.
DR   GO; GO:0006177; P:GMP biosynthetic process; ISO:PomBase.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00344; GMP_synthase; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR022955; GMP_synthase.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR   TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glutamine amidotransferase; GMP biosynthesis;
KW   Ligase; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..539
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000286154"
FT   DOMAIN          20..215
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          216..413
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        96
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        189
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        191
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         244..250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   539 AA;  60044 MW;  F83A1C4575F71723 CRC64;
     MSSTEVPGEV STSVSSYFDT ILILDFGSQY SHLIARRLRE IHVYAELLPC TQKIEALPFK
     PIGVILSGGP YSVYDDIAPH VDPAVFELGV PVLGICYGMQ EIAWLNGRCV EPGIEREYGP
     ATVSMEPEIK TEVFKSFFNS MPKEFEVWMS HGDRLSALPN GYETIGRTKN SPFAVIAHVT
     KPIIGLQFHP EVTHTPLGLQ LIKNFAIEIC HAKPNWSMEN FVDKEILRIR KMIGPSDHVI
     GAVSGGVDST VASKVLKEAI GDRFHAIMVD NGLLRLNEAE IVRETLNKHL GIQLTVVDAS
     EEFIGKLKGV TDPEKKRKII GNTFIHVFER EAERIVKETN GKVEYLLQGT LYPDVIESIS
     FKGPSQTIKT HHNVGGLLKD MKLKLIEPLR ELFKDEVRAL GELLGIEHSL VWRHPFPGPG
     LGIRILGEVN AAQLEIARKA DHIFITEIRN HGYYDKISQA FAALLPVKAV GVMGDKRTHE
     QVIALRAITT SDFMTADWYD GFSIKFLKLV SSRICNEVSG VNRVLYDISS KPPATVEME