ID   GUAA_STRCO              Reviewed;         526 AA.
AC   Q9L0H2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=SCO4785; ORFNames=SCD63.17;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(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; AL939121; CAB82024.1; -; Genomic_DNA.
DR   RefSeq; NP_628943.1; NC_003888.3.
DR   RefSeq; WP_003974187.1; NZ_VNID01000016.1.
DR   AlphaFoldDB; Q9L0H2; -.
DR   SMR; Q9L0H2; -.
DR   STRING; 100226.SCO4785; -.
DR   MEROPS; C26.A07; -.
DR   GeneID; 1100226; -.
DR   KEGG; sco:SCO4785; -.
DR   PATRIC; fig|100226.15.peg.4859; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_11; -.
DR   InParanoid; Q9L0H2; -.
DR   OMA; KRKIIGH; -.
DR   PhylomeDB; Q9L0H2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001973; 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; 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; Reference proteome.
FT   CHAIN           1..526
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140186"
FT   DOMAIN          13..204
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          205..400
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        90
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000250"
FT   BINDING         232..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  56613 MW;  43ACC404EE19EEA3 CRC64;
     MSSATPAAAA PDTVLVVDFG AQYAQLIARR VREARVYSEI VPSSMPVEEI LAKNPAAIIL
     SGGPSSVYEA GAPTLDRSLF EAGVPVFGMC YGFQLMAQTL GGTVDNSGAR EYGRTELAVS
     KPSSTLFEGT PAEQSVWMSH GDACSAAPEG FTVTGSTDVV PVAAFENDEK KLYGVQYHPE
     VMHSTHGQQV LEHFLYRGAG LSPDWTTGNV IEEQVAAIRA QVGDRRAICG LSGGVDSAVA
     AALVQKAIGS QLTCVYVDHG LMRKGETEQV EKDFVAATGV QLKVVDASER FLGALAGVSD
     PEQKRKIIGR EFIRVFEQAQ LEIMREDGPE VAFLVQGTLY PDVVESGGGT GTANIKSHHN
     VGGLPDDIEF ELVEPLRQLF KDEVRMVGQE LGLPDEIVQR QPFPGPGLGI RIVGEVTKER
     LDLLREADAI AREELTAAGL DRDIWQCPVV LLADVRSVGV QGDGRTYGHP IVLRPVSSED
     AMTADWSRLP YEVLSKISTR ITNEVTDVNR VVLDVTSKPP GTIEWE