ID   GUAA_MYCTO              Reviewed;         525 AA.
AC   P9WMS6; L0TCE7; P0A5A1; Q50729;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
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=MT3504;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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}.
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DR   EMBL; AE000516; AAK47841.1; -; Genomic_DNA.
DR   PIR; A70735; A70735.
DR   RefSeq; WP_003900045.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMS6; -.
DR   SMR; P9WMS6; -.
DR   MEROPS; C26.A07; -.
DR   EnsemblBacteria; AAK47841; AAK47841; MT3504.
DR   KEGG; mtc:MT3504; -.
DR   PATRIC; fig|83331.31.peg.3761; -.
DR   HOGENOM; CLU_014340_0_5_11; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001020; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..525
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000427250"
FT   DOMAIN          16..205
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          206..399
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        93
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000250"
FT   BINDING         233..239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   525 AA;  56046 MW;  73C327DF3752A08E CRC64;
     MVQPADIDVP ETPARPVLVV DFGAQYAQLI ARRVREARVF SEVIPHTASI EEIRARQPVA
     LVLSGGPASV YADGAPKLDP ALLDLGVPVL GICYGFQAMA QALGGIVAHT GTREYGRTEL
     KVLGGKLHSD LPEVQPVWMS HGDAVTAAPD GFDVVASSAG APVAAFEAFD RRLAGVQYHP
     EVMHTPHGQQ VLSRFLHDFA GLGAQWTPAN IANALIEQVR TQIGDGHAIC GLSGGVDSAV
     AAALVQRAIG DRLTCVFVDH GLLRAGERAQ VQRDFVAATG ANLVTVDAAE TFLEALSGVS
     APEGKRKIIG RQFIRAFEGA VRDVLDGKTA EFLVQGTLYP DVVESGGGSG TANIKSHHNV
     GGLPDDLKFT LVEPLRLLFK DEVRAVGREL GLPEEIVARQ PFPGPGLGIR IVGEVTAKRV
     DTLRHADSIV REELTAAGLD NQIWQCPVVL LADVRSVGVQ GDGRTYGHPI VLRPVSSEDA
     MTADWTRVPY EVLERISTRI TNEVAEVNRV VLDITSKPPA TIEWE