ID   GUAA_CALBD              Reviewed;         511 AA.
AC   B9MS76;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; OrderedLocusNames=Athe_1432;
OS   Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS   (Anaerocellum thermophilum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=521460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_00344}.
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_00344};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR   EMBL; CP001393; ACM60530.1; -; Genomic_DNA.
DR   RefSeq; WP_015907894.1; NC_012034.1.
DR   AlphaFoldDB; B9MS76; -.
DR   SMR; B9MS76; -.
DR   STRING; 521460.Athe_1432; -.
DR   MEROPS; C26.957; -.
DR   EnsemblBacteria; ACM60530; ACM60530; Athe_1432.
DR   GeneID; 31772777; -.
DR   KEGG; ate:Athe_1432; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_9; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 504464at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000007723; 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..511
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_1000205289"
FT   DOMAIN          5..195
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          196..386
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         223..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   511 AA;  57661 MW;  D09AF3B8999B129E CRC64;
     MQHEIVIVLD FGGQYNQLIA RRVRECGVYC EIWPYDTPLE KIISKNPKGI IFTGGPSSVY
     EPNAPMIDKE LFEKGIPILG ICYGNQLIAH IMGGKVSRAL FREYGKTHIK YDISSPLFSG
     IPEHSVCWMS HTDFVEKLPE GFKALASTEN CSIAAFGDDT RKIYGVQFHP EVVHTEYGQK
     IIENFLFNIC NCHGDWKTSS FIEEKVNEIK DIVGNQKVVC ALSGGVDSSV AAVLVHKAIG
     KNLYCIFVDH GLLRKGEAEE VVSVFKDKFD MNVIKVDAKD RFLEALKGVT DPEEKRKIIG
     REFIRVFEEE AEKLGDIKFL VQGTIYPDVV ESGVGKAATI KSHHNVGGLP EKIKFKQIIE
     PLRDLFKDEV RRVGIELGIP EKIVKRQPFP GPGLAIRIIG EVTEEKLDIL REVDWIFRKE
     IEQSGLDNEI WQYFAVLTNM KSVGVMGDER TYDYTVALRA VTSIDGMTAD WAKIPYEILE
     RVSNEIVNSV KKVNRVVYDI TSKPPATIEW E