ID A0A8D2Q7U7_VARKO Unreviewed; 693 AA.
AC A0A8D2Q7U7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
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 Name=GMPS {ECO:0000313|Ensembl:ENSVKKP00000025215.1};
OS Varanus komodoensis (Komodo dragon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Anguimorpha; Paleoanguimorpha; Varanoidea; Varanidae; Varanus.
OX NCBI_TaxID=61221 {ECO:0000313|Ensembl:ENSVKKP00000025215.1, ECO:0000313|Proteomes:UP000694545};
RN [1] {ECO:0000313|Ensembl:ENSVKKP00000025215.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSVKKP00000025215.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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:ARBA00051135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11681;
CC Evidence={ECO:0000256|ARBA:ARBA00051135};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
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DR RefSeq; XP_044288775.1; XM_044432840.1.
DR AlphaFoldDB; A0A8D2Q7U7; -.
DR Ensembl; ENSVKKT00000025826.1; ENSVKKP00000025215.1; ENSVKKG00000016572.1.
DR GeneID; 123024740; -.
DR CTD; 8833; -.
DR OMA; IWQSFAV; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000694545; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR FunFam; 3.30.300.10:FF:000008; GMP synthase [glutamine-hydrolyzing]; 1.
DR FunFam; 3.30.300.10:FF:000009; GMP synthase [glutamine-hydrolyzing]; 1.
DR FunFam; 3.40.50.620:FF:000044; GMP synthase [glutamine-hydrolyzing]; 1.
DR FunFam; 3.40.50.880:FF:000013; GMP synthase [glutamine-hydrolyzing]; 1.
DR Gene3D; 3.30.300.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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 Pfam; PF02540; NAD_synthase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
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; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Reference proteome {ECO:0000313|Proteomes:UP000694545}.
FT DOMAIN 217..435
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT BINDING 244..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 693 AA; 76737 MW; 21F10D78A4107942 CRC64;
MALCNGEAKL ENAGEDLKDG ICRYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP
AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV LGICYGMQMM NKVFGGTVHK
KDVREDGVFN ITVDNTCSLF RGLQKEEIVL LTHGDSVDKV ADGFKVVAQS GNVVAAIANE
SKKLYGAQFH PEVSLTVNGK AMLKNFLYDI AGCSGTFTVQ NREQECIRDI KEKVGSSKVL
VLLSGGVDST VCTALLNRAL NQEQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVVNAA
HWFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMNLKPE
EVFLAQGTLR PDLIESASLV ASGKAEVIKT HHNDTELIRK LREKGKVIEP LKDFHKDEVR
VLGRELGLPE ELVSRHPFPG PGLAIRVICA EEPYVCKDFP ETNNILKIIA DFSASVKKPH
TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPVKTVGVQ GDGRSYSYVC GISSKDAPHW
ESLMFLSRLI PRMCHNINRV VYVFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
ESGYSGKISQ MPIILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIA ATPGNEIPEE
VVLKMVTEIK KIPGISRVMY DLTSKPPGTT EWE
//
