ID   GUAA_CHLMU              Reviewed;         512 AA.
AC   Q9PKM3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
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=TC_0442;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39296.1; -; Genomic_DNA.
DR   PIR; D81701; D81701.
DR   RefSeq; WP_010230464.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKM3; -.
DR   SMR; Q9PKM3; -.
DR   STRING; 243161.TC_0442; -.
DR   PRIDE; Q9PKM3; -.
DR   EnsemblBacteria; AAF39296; AAF39296; TC_0442.
DR   GeneID; 1245795; -.
DR   KEGG; cmu:TC_0442; -.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_0; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 504464at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000800; Chromosome.
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..512
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140109"
FT   DOMAIN          3..196
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          197..387
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        80
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000250"
FT   BINDING         225..231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   512 AA;  57122 MW;  788068FFAD9C5611 CRC64;
     MSNILILDFG SQYTNVLAKK IRLLSVFCEV LPWNTPLEKI LQKSPSGLIF SGGPHSVYQN
     NSPEVDKEIY NSNIPILGVC YGMQLIARDF GSEVQGGKSE FGYTPIVFYP SELFKGLADQ
     DAFHTEIRMS HCDCVVVPPK DFFVIASSQH CPIAAIECPK KKLFGLQFHP EVSDSQDIGD
     KILSNFVKHI CQTSETWKIE TIEKQLIQGI REKVGETERV LLGLSGGVDS SVLAVLLHNA
     LGDRLSCVFV DTGLLRKNEV EEVKQQFSSL GLEILVVDAS EKFFHDLSGI EDPEQKRKVI
     GAAFIEVFDE ASKNLDVQWL AQGTIYSDVI ESAKSCDATQ VIKSHHNVGG LPEKLNLKLL
     EPLRFLFKDE VRALGKVLGL PDVLISRHPF PGPGLGVRVL GEVRREYVEI VKNADSIFIE
     ELKKANLYHK VSQAFAVFLP CKSVAVKGDC RHYGYTIALR AVESTDFMTA CWPSLSREFL
     NRCSSRIINE IPEVCRVVYD ISDKPPATIE WE