ID   GUAA_SYNY3              Reviewed;         542 AA.
AC   P49057;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 146.
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; OrderedLocusNames=slr0213;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA10210.1; -; Genomic_DNA.
DR   PIR; S76358; S76358.
DR   AlphaFoldDB; P49057; -.
DR   SMR; P49057; -.
DR   IntAct; P49057; 3.
DR   STRING; 1148.1001583; -.
DR   MEROPS; C26.957; -.
DR   PaxDb; P49057; -.
DR   EnsemblBacteria; BAA10210; BAA10210; BAA10210.
DR   KEGG; syn:slr0213; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   InParanoid; P49057; -.
DR   OMA; KRKIIGH; -.
DR   PhylomeDB; P49057; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..542
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140196"
FT   DOMAIN          28..218
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          219..417
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000250"
FT   BINDING         246..252
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   542 AA;  61009 MW;  A0C6F05EFA4C4863 CRC64;
     MTTQIPVPPV VSDQALPDRI SDRLKGQIIV ILDFGSQYSE LIARRIRETE VYSEVLSYRT
     TAQQLREIKP KGIILSGGPN SVYDQGAPEC DPEIFQLGVP VLGVCYGMQL MVKQLGGRVE
     RAKRGEYGKA SLHIDDPTDL LTNVENDSTM WMSHGDSCVD LPTGFEILAH TDNTPCAAIA
     DHQKALFGVQ FHPEVVHSVG GIALIRNFVY HICHCEPTWT TAAFIEESIR EVRSQVGDRR
     VLLALSGGVD SSTLAFLLHR AIGDNLTCMF IDQGFMRKGE PERLVELFDH QFHIPVQYVN
     ARDRFLKQLE GVTDPEEKRR LIGHEFIQVF EEESNRLGPF DYLAQGTLYP DVIESADSNV
     DPKTGERVAV KIKSHHNVGG LPKNLRFKLV EPLRKLFKDE VRKLGRSIGL PEEIVRRHPF
     PGPGLAIRII GEVTSERLNI LRDADFIVRD EISKRGIYHD YWQAFAVLLP IRSVGVMGDK
     RTYAHPVVLR FITSEDGMTA DWARVPYDIL EAISNRIVNE VKGVNRVVYD ITSKPPGTIE
     WE