ID   GUAAA_SACS2             Reviewed;         188 AA.
AC   Q97VZ9;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A {ECO:0000255|HAMAP-Rule:MF_01510};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_01510};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_01510};
GN   Name=guaAA {ECO:0000255|HAMAP-Rule:MF_01510}; Synonyms=guaA;
GN   OrderedLocusNames=SSO2451;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_01510}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01510};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01510}.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000255|HAMAP-Rule:MF_01510}.
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DR   EMBL; AE006641; AAK42591.1; -; Genomic_DNA.
DR   PIR; H90416; H90416.
DR   RefSeq; WP_010923859.1; NC_002754.1.
DR   AlphaFoldDB; Q97VZ9; -.
DR   SMR; Q97VZ9; -.
DR   STRING; 273057.SSO2451; -.
DR   MEROPS; C26.A31; -.
DR   PRIDE; Q97VZ9; -.
DR   EnsemblBacteria; AAK42591; AAK42591; SSO2451.
DR   GeneID; 1453918; -.
DR   GeneID; 65559868; -.
DR   KEGG; sso:SSO2451; -.
DR   PATRIC; fig|273057.12.peg.2529; -.
DR   eggNOG; arCOG00087; Archaea.
DR   HOGENOM; CLU_014340_1_4_2; -.
DR   InParanoid; Q97VZ9; -.
DR   OMA; GPDMDRI; -.
DR   PhylomeDB; Q97VZ9; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001974; Chromosome.
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: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   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_01510; GMP_synthase_A; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR023686; GMP_synthase_A.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..188
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT                   /id="PRO_0000140233"
FT   DOMAIN          2..188
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
SQ   SEQUENCE   188 AA;  21035 MW;  DB7CC4CE03451481 CRC64;
     MKVGLVYYGG QYNHLILKNV KYLGADIEVI PPHKPVEELK KFDCVIFSGG PYSVSEEIQK
     MGNSPLYIKE LKVPMLGICL GHQLIAYVLG GVVRRALNPE YGLTRINIFD EDTILKGFSQ
     QLNVWESHND EVVEPPSGFR VLASSANARV QAMANSSNSI FGVQFHPEVK HTERGIEIFK
     NFLGVCRK