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
//