ID   GUAA_FRUSA              Reviewed;          20 AA.
AC   P83540;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
DE   Flags: Fragments;
GN   Name=guaA;
OS   Fructilactobacillus sanfranciscensis (Lactobacillus sanfranciscensis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Fructilactobacillus.
OX   NCBI_TaxID=1625;
RN   [1]
RP   PROTEIN SEQUENCE, AND INDUCTION.
RC   STRAIN=ATCC 27651 / DSM 20451 / JCM 5668 / KCTC 3205 / NCIMB 702811 / NRRL
RC   B-3934 / L-12;
RX   PubMed=12112860;
RX   DOI=10.1002/1615-9861(200206)2:6<765::aid-prot765>3.0.co;2-v;
RA   Drews O., Weiss W., Reil G., Parlar H., Wait R., Goerg A.;
RT   "High pressure effects step-wise altered protein expression in
RT   Lactobacillus sanfranciscensis.";
RL   Proteomics 2:765-774(2002).
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}.
CC   -!- INDUCTION: Repressed by elevated hydrostatic pressure.
CC       {ECO:0000269|PubMed:12112860}.
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DR   AlphaFoldDB; P83540; -.
DR   UniPathway; UPA00189; UER00296.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Glutamine amidotransferase;
KW   GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           <1..>20
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140140"
FT   DOMAIN          <1..>20
FT                   /note="GMPS ATP-PPase"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2141 MW;  E06670CB3D361399 CRC64;
     ALGDQLLSVF VDHTLVDEVA