ID   GUAA_ASPOR              Reviewed;         541 AA.
AC   Q2UFN0;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=AO090026000141;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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}.
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DR   EMBL; AP007159; BAE59635.1; -; Genomic_DNA.
DR   RefSeq; XP_001821637.1; XM_001821585.2.
DR   AlphaFoldDB; Q2UFN0; -.
DR   SMR; Q2UFN0; -.
DR   STRING; 510516.Q2UFN0; -.
DR   MEROPS; C26.957; -.
DR   PRIDE; Q2UFN0; -.
DR   EnsemblFungi; BAE59635; BAE59635; AO090026000141.
DR   GeneID; 5993665; -.
DR   KEGG; aor:AO090026000141; -.
DR   VEuPathDB; FungiDB:AO090026000141; -.
DR   HOGENOM; CLU_014340_0_5_1; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000006564; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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_0000286145"
FT   DOMAIN          15..209
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          210..416
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        91
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        183
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        185
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         238..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   541 AA;  59794 MW;  EFB3F9AB66CC38AC CRC64;
     MAETPELEPH NAFDTILTLD FGSQYTHLIT RRLRELNVYS EMLPCTQKLA DLKFKPAGVI
     LSGGPYSVYE EGAPHVDPAY FDLGVPILGI CYGLQEIAYR LDSTNVIAGT SREYGLAQLK
     AKKVGGHVDH LFDGLEDEFN VWMSHGDKLG KLPEGFHTIA TTPNSEYAGI AHETKPIYGL
     QLHPEVTHTQ NGTKLLKNFA VNICGCKQNW TMARFVDQEI ARIRKLVGPT GQVLGAVSGG
     VDSTVAAKLM KEAIGDRFHA VLVDTGFMRL NECEQVKQTL AEHLGINLIV ADASQVFMEG
     LKGISDPEQK RKFIGNKFID VFEEEAKKIE DAAAHSETAG KIGFFLQGTL YPDVIESISF
     KGPSATIKTH HNVGGLPKRM TEGQGLKLIE PLRELFKDEV RDLGRQLGIA HEMVMRHPFP
     GPGIAIRILG EITPERVEMA RKADHIFISM IREAGLYDKI GQAFAALDPS RAVGVMGDKR
     VYENIVLLRA VETTDFMTAI AYPFEHEFLT RVSTRIVNEV SGVCRVAYDY TSKPPGTIEL
     E