ID A0A6V7UEY2_MELEN Unreviewed; 671 AA.
AC A0A6V7UEY2;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
DE AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356};
GN ORFNames=MENT_LOCUS11029 {ECO:0000313|EMBL:CAD2153174.1};
OS Meloidogyne enterolobii (Root-knot nematode worm) (Meloidogyne
OS mayaguensis).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC Meloidogyne.
OX NCBI_TaxID=390850 {ECO:0000313|EMBL:CAD2153174.1, ECO:0000313|Proteomes:UP000580250};
RN [1] {ECO:0000313|EMBL:CAD2153174.1, ECO:0000313|Proteomes:UP000580250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Koutsovoulos G., Danchin GJ E.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAD2153174.1}.
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DR EMBL; CAJEWN010000052; CAD2153174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6V7UEY2; -.
DR OrthoDB; 1724632at2759; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000580250; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; 3.40.50.620:FF:000044; 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; IPR001763; Rhodanese-like_dom.
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; 2.
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.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
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};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW ProRule:PRU00886}.
FT DOMAIN 216..425
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT DOMAIN 235..278
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT BINDING 243..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 671 AA; 75582 MW; A4C638AEA2D4CF4F CRC64;
MEDNSPTKEQ TKVANLEDAQ EEKIAILDFG AQYGKLIDRR VRECNVYSSI LPFDTKMEQL
LRDKYSAIII SGGPNSVYVD NSPLYDAAIF NGQLPVLGIC YGFQLINKHF GGNVCLHARR
EDGRTNIKID PQSEIFNGLQ AEQNVLLTHG DGVTKDSIPP NGFRIIAMSG EFVAGIEQVE
KRIFGLQFHP EVDLTENGTL ILSNFLRRVC RLTCRYTFLN REHKCIELIR QTVGDKHVLV
LCSGGVDSTV CAALCIKALG FEKVHAIHID NGFMRYNESS SIIKSLSAIG LVVNRFDFLS
EFLNARIIDK GVETLPLKFV TCPEHKRKII GDTFIRCKDA AIEKLGLYND DLYLVQGTLR
PDLIESASQI ASGCANVIKT HHNDSALVRE LRDLGKVVEP LQDFHKDEVR ELGRTLGLPE
AIVNRHPFPG PGLAIRILCA EVPFICENFD ATQNQLRSIV SNFSPNFDCI LLPIRAVGVQ
GDRRSYSYVA ALTFCKKDEP IPWDKIHYLA KILPNEVKNV NRVVFVFHET TTNLIKDITV
THINEATIEI IQKADKIVYQ TLRGLDSLDN PNPLLKDSLK CIEQMPVVLV PIHFNRFYTL
PQVFPSTKRS IVLRPFLTRD FMTGEPAIPG KDIPFETIME MVRRIEEEMP TTISRVMIDM
TAKPPGTTEW E
//
