ID   GUAA_CORAM              Reviewed;         524 AA.
AC   O52831; Q9RHY6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 109.
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=guaA;
OS   Corynebacterium ammoniagenes (Brevibacterium ammoniagenes).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1697;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BA 17-2;
RA   Han J.K.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399;
RA   Yonetani Y., Teshiba S.;
RT   "Cloning and sequence analysis of Corynebacterium ammoniagenes guaA gene.";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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}.
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DR   EMBL; Y10499; CAA71524.1; -; Genomic_DNA.
DR   EMBL; AB003155; BAA89456.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52831; -.
DR   SMR; O52831; -.
DR   MEROPS; C26.A07; -.
DR   UniPathway; UPA00189; UER00296.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
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; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..524
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140116"
FT   DOMAIN          10..199
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          200..398
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        87
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000250"
FT   BINDING         228..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        110
FT                   /note="G -> R (in Ref. 1; CAA71524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277..278
FT                   /note="KL -> NV (in Ref. 1; CAA71524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346
FT                   /note="G -> R (in Ref. 1; CAA71524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378..386
FT                   /note="FKDEVRAVG -> LRRSPCRS (in Ref. 1; CAA71524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446..466
FT                   /note="PVVLLADVRSVGVQGDGRTYG -> QSYCLPMSAPSSPRRRPHLR (in
FT                   Ref. 1; CAA71524)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   524 AA;  56180 MW;  2ABE1AB9305641C5 CRC64;
     MTQPATTPRP VLVVDFGAQY AQLIARRVRE ASIYSEVVPH SATVKEIKAK NPAALILSGG
     PSSVYADGAP QLKPELLELG VPVFGICYGF QAMNHALGGN VAQTGDREYG RTEITHTGGV
     LHDGLEENHK VWMSHGDAVD KAPEGFTVTA SSAGAPVAAM ECVAKQMAGV QYHPEVMHSP
     HGQEVLVRFL TEVAGLEQTW TSANIAQQLI DDVRAQIGPE GRAICGLSGG VDSAVAAALV
     QRAIGDRLTC VFVDHGLLRA GEREQVEKDF VASTGAKLIT AHEADAFLSK LAGVTDPEAK
     RKAIGAEFIR SFERAVAQAL EESPEDSTVD FLVQGTLYPD VVESGGGDGT ANIKSHHNVG
     GLPDDVEFEL VEPLRLLFKD EVRAVGRELG LPEEIVARQP FPGPGLGIRI IGEVTEERLE
     ILRQADLIAR TELTNAGLDG DIWQCPVVLL ADVRSVGVQG DGRTYGHPIV LRPVSSEDAM
     TADWTRVPYD VLEKISTRIT NEVNDVNRVV VDITSKPPGT IEWE