ID   GUAA_PHANO              Reviewed;         541 AA.
AC   Q0UHC4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=SNOG_08840;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445337; EAT84008.1; -; Genomic_DNA.
DR   RefSeq; XP_001799145.1; XM_001799093.1.
DR   AlphaFoldDB; Q0UHC4; -.
DR   SMR; Q0UHC4; -.
DR   STRING; 13684.SNOT_08840; -.
DR   MEROPS; C26.957; -.
DR   EnsemblFungi; SNOT_08840; SNOT_08840; SNOG_08840.
DR   GeneID; 5976044; -.
DR   KEGG; pno:SNOG_08840; -.
DR   eggNOG; KOG1622; Eukaryota.
DR   HOGENOM; CLU_014340_0_5_1; -.
DR   InParanoid; Q0UHC4; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 392369at2759; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
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; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 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..541
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000286153"
FT   DOMAIN          17..212
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          213..416
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        93
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        186
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        188
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         241..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   541 AA;  59923 MW;  5532D17BAEB2FDCF CRC64;
     MATDGSDPIP PHKTFDTILV LDFGSQYTHL ITRRLRELNV YSEMLPCNTK LADLPFTPKG
     IILSGGPYSV YEEGAPHVDH AVFDLGVPIL GICYGLQEMA WHFGKNAGVA AGEKREYGHA
     NLKVESHGGH MDELFKDVGN ELEVWMSHGD KLSNMPENFT TVATTTNAPF AGIAHKEKKY
     YGIQFHPEVT HTKMGKTVLK NFAVDICQST TDWTMGKFVD QEITRIRKLV GEKGQVIGAV
     SGGVDSTVAA KLMKEAIGDR FHAVMVDNGV LRLNEAKQVK ETLEKGLGIN LTVIDASDMF
     LDRLKGITDN PEQKRKVIGN TFIEIFQEKA KEIAAAAKNS SNAGEIEWLL QGTLYPDVIE
     SLSFKGPSQT IKTHHNVGGL PANMNLKLIE PLRELFKDEV RALGVELGIP EDLVWRHPFP
     GPGIAIRILG EVTREQVRIA READYIFIEE IKAAGLYRNI SQAFAALLPV KAVGVMGDKR
     VHDQVIALRA VETTDFMTAD WYPFDGEFLK RVSRRIVNEV NGVCRVVYDI TSKPPGTIEM
     E