ID   B9GWS1_POPTR            Unreviewed;       534 AA.
AC   B9GWS1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00021562};
DE            EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
DE   AltName: Full=GMP synthetase {ECO:0000256|ARBA:ARBA00030464};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356};
GN   ORFNames=POPTR_003G128200 {ECO:0000313|EMBL:PNT45276.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT45276.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT45276.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
CC   -!- FUNCTION: Catalyzes the conversion of xanthine monophosphate (XMP) to
CC       GMP in the presence of glutamine and ATP through an adenyl-XMP
CC       intermediate. {ECO:0000256|ARBA:ARBA00044933}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP +
CC         diphosphate + 2 H(+); 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:0000256|ARBA:ARBA00049404};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
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DR   EMBL; CM009292; PNT45276.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9GWS1; -.
DR   SMR; B9GWS1; -.
DR   FunCoup; B9GWS1; 4759.
DR   STRING; 3694.B9GWS1; -.
DR   MEROPS; C26.A07; -.
DR   Gramene; Potri.003G128200.1.v4.1; Potri.003G128200.1.v4.1; Potri.003G128200.v4.1.
DR   KEGG; pop:7458178; -.
DR   eggNOG; KOG1622; Eukaryota.
DR   HOGENOM; CLU_014340_0_5_1; -.
DR   InParanoid; B9GWS1; -.
DR   OMA; IWQSFAV; -.
DR   OrthoDB; 1724632at2759; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000006729; Chromosome 3.
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:0006177; P:GMP biosynthetic process; IBA:GO_Central.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   FunFam; 3.30.300.10:FF:000002; GMP synthase [glutamine-hydrolyzing]; 1.
DR   FunFam; 3.40.50.620:FF:000001; GMP synthase [glutamine-hydrolyzing]; 1.
DR   FunFam; 3.40.50.880:FF:000001; GMP synthase [glutamine-hydrolyzing]; 1.
DR   Gene3D; 3.30.300.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00884; guaA_Cterm; 1.
DR   NCBIfam; TIGR00888; guaA_Nterm; 1.
DR   NCBIfam; NF000848; PRK00074.1; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW   ProRule:PRU00886}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW   ProRule:PRU00886}; Reference proteome {ECO:0000313|Proteomes:UP000006729}.
FT   DOMAIN          207..408
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        91
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         235..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   534 AA;  59375 MW;  37F35E818E324168 CRC64;
     MDPKAVKSDL VLILDYGSQY THLITRRIRS LNIFSLCISG TSSLETITSH NPKVVILSGG
     PHSVHSANSP TFPSGFVEWA QKGGIFVLGV CYGLQLIVQR LGGQVDVGQR QEYGRMEIEV
     EKNLGVFGNK KVGDKQVVWM SHGDETVKLP YGFEVVARSQ QGAVAAVENR EMRFFGLQYH
     PEVTHSPEGM DTLRYFLFDV CGVSPGWNME NVLDEEIRVI NDAVGPEEHV ICALSGGVDS
     TVAATLVHKA IGDRLHCIFV DNGLLRYKER ERVAETFESD LHLPVTCVDA SNEFLSKLKG
     VVDPEMKRKI IGKEFISIFD AFAHELEQKL GKKPAYLVQG TLYPDVIESC PPPGSGRTHS
     HTIKSHHNVG GLPKDMKLKL IEPLKLLFKD EVRQLGRILN VPDAFLKRHP FPGPGLAVRV
     LGDVTEGNAL DILRQVDEIF IQSIKDAGLY DSIWQAFAVF LPVRSVGVQG DQRTHSHVVA
     LRAVTSQDGM TADWYYFEHK FLDDVARKIC NSVRGVNRVV QDITSKPPST IEWE
//