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Database: UniProt
Entry: F0XTW3_GROCL
LinkDB: F0XTW3_GROCL
Original site: F0XTW3_GROCL 
ID   F0XTW3_GROCL            Unreviewed;      1139 AA.
AC   F0XTW3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
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=CMQ_4553 {ECO:0000313|EMBL:EFW98701.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFW98701.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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:0000256|ARBA:ARBA00001592};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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DR   EMBL; GL630006; EFW98701.1; -; Genomic_DNA.
DR   RefSeq; XP_014168184.1; XM_014312709.1.
DR   AlphaFoldDB; F0XTW3; -.
DR   STRING; 655863.F0XTW3; -.
DR   MEROPS; C26.957; -.
DR   GeneID; 25977777; -.
DR   eggNOG; KOG1223; Eukaryota.
DR   eggNOG; KOG1622; Eukaryota.
DR   HOGENOM; CLU_277989_0_0_1; -.
DR   InParanoid; F0XTW3; -.
DR   OrthoDB; 705at2759; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.30.300.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00344; GMP_synthase; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR015890; Chorismate_C.
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   NCBIfam; TIGR00884; guaA_Cterm; 1.
DR   NCBIfam; TIGR00888; guaA_Nterm; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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:UP000007796}.
FT   DOMAIN          214..419
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        93
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         242..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   1139 AA;  124340 MW;  68C0EB3974EC872D CRC64;
     MAAKTGAAAA PHEIFDTILL LDFGSQTSHL ILRGLRSLNV FCEIMPCTTK IKDLTWKPKG
     IILSGSPASV TDAGAPHVDP AIFDLGVPIL GICYGCQELS WREVSDSVAP GKAREYGHTD
     LTIFKVDGPD HSNKLFEGLG ESMHVYMSHD DKLIKLPNNY AVIASSQNSE YAGIVHKTKP
     IYGIQFHPEV EHTPRGIDLL KNFAVSICKA QQHWVMSDFI EHAIASIRER VGDKAQVIGA
     VSGGVDSTVV ARLMKEAIGD RFHAVLVDNG VMRLNECADV KKALQEHLGI NLTIIDGGAL
     FLGRLKGVTE PETKRKIIGG TFIDLFEEEA IRIEKAAENT ANAGKVEFFV QGTLYPDVIE
     SLSLNTNNTV KTHHNVGGLP ARMMNGQGLK LIEPLRELFK DEVRAFGRKL GIPDDLVMRH
     PFPGPGIAIR IIGEVTPERV EIARKADHIF ISMIKEAGIY DKIAQAYAGL DSNRAVGVMG
     DARVYGYIII LRAVMSTNFM TAEPYPFDFS FLTQVSRRII NEVPGVARVT YDITSKPPES
     PESSGYLTRT RQRHPIPLTL PLIQQCILCY GRTCKHAESP FPVLCFLGPP TSTLQLADMD
     GGQKDVIVPS LETVSEVLAN VVTTAKAEAA KGPGSTYRRP NLVPVYGQIS SDLITPSAAY
     LKVSAHSGSK HSFLFESAAT ERVGRYSFLA AGPRKVLETG PGFGEACDPL PGLEVELSRF
     VVAHVPGLQL PPLAGGAVGY VSYDCVRYFE PKTARPLKDV LKIPESQFCF YDTIVAFDRF
     FGIIKVITYL QLDAVAQDST TGTYEAAAVA AEYRRATGVI RALIDVLNGP TIPLPEQKEV
     VLGREYTSNV GQAGYMSHVA RLKKHIEAGD IIQAVPSQRF ARPTDLHPFN VYRHLRTVNP
     SPYLFYIDCG GRPQIVGASP ELLVKTEGGR VVTHPIAGTV KRGRTPEEDT ALAEELRQSL
     KDRAEHVMLC DLARNDVTRV CDPRETRVDR LMVVEKFSHV QHLVSQVSGV LRPGCSRFDA
     FRSIFPAGTV SGAPKVRAME LIAELEGEKR GVYAGAVGYF GYNGVAADGV TPVDGQMDTC
     IALRTMVLAD GVAYLQAGGG IVFDSDEYDE WVETMNKLGA NMHCITSAEQ LYARRQQGE
//
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