GUAA_RAT
ID GUAA_RAT Reviewed; 693 AA.
AC Q4V7C6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2 {ECO:0000269|PubMed:3436958};
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=Gmps;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=3436958; DOI=10.1093/oxfordjournals.jbchem.a122130;
RA Hirai K., Matsuda Y., Nakagawa H.;
RT "Purification and characterization of GMP synthetase from Yoshida sarcoma
RT ascites cells.";
RL J. Biochem. 102:893-902(1987).
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:0000269|PubMed:3436958}.
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:0000269|PubMed:3436958};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11681;
CC Evidence={ECO:0000305|PubMed:3436958};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:3436958};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 uM for XMP {ECO:0000269|PubMed:3436958};
CC KM=120 uM for ATP {ECO:0000269|PubMed:3436958};
CC KM=300 uM for glutamine {ECO:0000269|PubMed:3436958};
CC pH dependence:
CC Optimum pH is 7.8-8.0. {ECO:0000269|PubMed:3436958};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49915}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:3436958}.
CC -!- TISSUE SPECIFICITY: Expressed in the testis, brain, thymus and ovary.
CC {ECO:0000269|PubMed:3436958}.
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DR EMBL; BC098016; AAH98016.1; -; mRNA.
DR RefSeq; NP_001019925.1; NM_001024754.1.
DR AlphaFoldDB; Q4V7C6; -.
DR SMR; Q4V7C6; -.
DR BioGRID; 254877; 1.
DR STRING; 10116.ENSRNOP00000068021; -.
DR iPTMnet; Q4V7C6; -.
DR PhosphoSitePlus; Q4V7C6; -.
DR jPOST; Q4V7C6; -.
DR PRIDE; Q4V7C6; -.
DR GeneID; 295088; -.
DR KEGG; rno:295088; -.
DR UCSC; RGD:1310063; rat.
DR CTD; 8833; -.
DR RGD; 1310063; Gmps.
DR eggNOG; KOG1622; Eukaryota.
DR InParanoid; Q4V7C6; -.
DR OrthoDB; 392369at2759; -.
DR PhylomeDB; Q4V7C6; -.
DR Reactome; R-RNO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR SABIO-RK; Q4V7C6; -.
DR UniPathway; UPA00189; UER00296.
DR PRO; PR:Q4V7C6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IDA:RGD.
DR GO; GO:0003921; F:GMP synthase activity; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0032263; P:GMP salvage; IDA:MGI.
DR GO; GO:1901367; P:response to L-cysteine; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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; 1.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Glutamine amidotransferase;
KW GMP biosynthesis; Ligase; Nucleotide-binding; Phosphoprotein;
KW Purine biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT CHAIN 2..693
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000284367"
FT DOMAIN 27..216
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT DOMAIN 217..435
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT ACT_SITE 104
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 190
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 192
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 244..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT BINDING 337
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT BINDING 522
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT BINDING 610
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT BINDING 685
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT BINDING 691
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49915"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 693 AA; 76757 MW; 03E0AA87B6CDA15D CRC64;
MALCNGDSKP ENAGGDLKDG CHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP
AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV LGICYGMQMM NKVFGGTVHK
KSVREDGVFN ISMDNTCSLF RGLQKEEIVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE
SKKLYGVQFH PEVGLTENGK VILKNFLYDI AGCSGNFTVQ NRELECIREI KEKVGTSKVL
VLLSGGVDST VCTALLNRAL NQDQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMSLKPE
EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR
ILGRELDLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH
TLLQRVKACT TEEDQEKLME ITSQHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW
ESLIFLARLI PRMCHNINRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGVP ATPGNEIPVE
VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE
