GUAA_CAEEL
ID GUAA_CAEEL Reviewed; 745 AA.
AC Q09580; Q0G842; Q7JMN1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2;
DE AltName: Full=Glutamine amidotransferase;
GN Name=gmps-1; ORFNames=M106.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b;
CC IsoId=Q09580-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q09580-2; Sequence=VSP_044290;
CC Name=c;
CC IsoId=Q09580-3; Sequence=VSP_044289;
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DR EMBL; Z46935; CAA87052.2; -; Genomic_DNA.
DR EMBL; Z46935; CAE48508.2; -; Genomic_DNA.
DR EMBL; Z46935; CAL36508.1; -; Genomic_DNA.
DR PIR; T23742; T23742.
DR RefSeq; NP_001022256.2; NM_001027085.3. [Q09580-2]
DR RefSeq; NP_001022257.2; NM_001027086.2. [Q09580-1]
DR RefSeq; NP_001076631.1; NM_001083162.3. [Q09580-3]
DR AlphaFoldDB; Q09580; -.
DR SMR; Q09580; -.
DR BioGRID; 39982; 21.
DR DIP; DIP-25638N; -.
DR IntAct; Q09580; 2.
DR STRING; 6239.M106.4b; -.
DR MEROPS; C26.A24; -.
DR EPD; Q09580; -.
DR PaxDb; Q09580; -.
DR PeptideAtlas; Q09580; -.
DR EnsemblMetazoa; M106.4a.1; M106.4a.1; WBGene00010912. [Q09580-2]
DR EnsemblMetazoa; M106.4a.2; M106.4a.2; WBGene00010912. [Q09580-2]
DR EnsemblMetazoa; M106.4b.1; M106.4b.1; WBGene00010912. [Q09580-1]
DR EnsemblMetazoa; M106.4b.2; M106.4b.2; WBGene00010912. [Q09580-1]
DR EnsemblMetazoa; M106.4c.1; M106.4c.1; WBGene00010912. [Q09580-3]
DR GeneID; 174672; -.
DR KEGG; cel:CELE_M106.4; -.
DR UCSC; M106.4a; c. elegans.
DR CTD; 174672; -.
DR WormBase; M106.4a; CE47006; WBGene00010912; gmps-1. [Q09580-2]
DR WormBase; M106.4b; CE47051; WBGene00010912; gmps-1. [Q09580-1]
DR WormBase; M106.4c; CE40394; WBGene00010912; gmps-1. [Q09580-3]
DR eggNOG; KOG1622; Eukaryota.
DR GeneTree; ENSGT00390000006591; -.
DR InParanoid; Q09580; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 392369at2759; -.
DR PhylomeDB; Q09580; -.
DR Reactome; R-CEL-73817; Purine ribonucleoside monophosphate biosynthesis.
DR Reactome; R-CEL-9748787; Azathioprine ADME.
DR UniPathway; UPA00189; UER00296.
DR PRO; PR:Q09580; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010912; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.880; -; 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 Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 2.
DR Pfam; PF02540; NAD_synthase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Glutamine amidotransferase;
KW GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..745
FT /note="Probable GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140255"
FT DOMAIN 60..252
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT DOMAIN 253..461
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 280..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 563
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 662
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 737
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 743
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_044289"
FT VAR_SEQ 39..40
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_044290"
SQ SEQUENCE 745 AA; 82606 MW; B4DD8931EAB535BC CRC64;
MKRSSSMLDI NEDSQHSTNK APPPKKAPED RFDSANMNAS GSHVTLVENL PVEKVSSGER
IAILDFGAQY GKVIDRRVRE LLVQSEMFPL NTTARTLIEL GGFKGIIISG GPNSVFEPEA
PSIDPEIFTC GLPVLGICYG FQLMNKLNGG TVTREHIRED GACEIQVDTS VHLFNGLHKT
ETVLLTHGDS VSEATVAPDF KVMAKSGHHV AGICNENRKL YGVQFHPEVD LTTNGTKMFE
NFLFKVVGCC GNFTIQNREQ SCISEINSIV GDKKVLVMVS GGVDSAVCAA LLRRALGPNR
VTAIHIDNGF MRHEESDAVE KSLAALDLPI HRYNFGTTFR SSTEHCKDGE VALDECDDPE
MKRKIIGNTF IRVKDVIMKD LNINHDEYFL AQGTLRPDLI ESASALASGH ADTIKTHHND
TFLVRELRKL GKVVEPLKDF HKDEVRELGK DLGLPESIVQ RHPFPGPGLA IRILCASDKR
PELMFNGPMY NGDVQGRIID VTEQFLNSAI NPSQGIYEHL QFEQARNNVL LSLSERDRQL
AEQQTFQISA HILPIKTVGV QGDARSYSYA VALSTEQRPI PWKLLFAYAS VIPKLFHGVN
RVVYAFGSKI EFSIEDLTRT YLVPHIVTKL QMADHIANNI LFGRVAASDG TQLPNVGHKI
QQMPVVLLPV DFDRDRDMIG SYRHSIVLRP FVTSDFMTGQ AAIPGVHLPE ETLIEMDKAI
RTNVLGISRV LLDMTCKPPG TTEWE
