ID   GUAA_DICDI              Reviewed;         718 AA.
AC   P32073; Q54TQ7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=guaA; Synonyms=gua2; ORFNames=DDB_G0281551;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX3;
RX   PubMed=1885577; DOI=10.1016/s0021-9258(18)55320-5;
RA   van Lookeren Campagne M.M., Franke J., Kessin R.H.;
RT   "Functional cloning of a Dictyostelium discoideum cDNA encoding GMP
RT   synthetase.";
RL   J. Biol. Chem. 266:16448-16452(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
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   -!- DEVELOPMENTAL STAGE: Produced during growth but not during development.
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DR   EMBL; M64282; AAA33213.1; -; mRNA.
DR   EMBL; AAFI02000042; EAL66537.1; -; Genomic_DNA.
DR   PIR; A41164; A41164.
DR   RefSeq; XP_640534.1; XM_635442.1.
DR   AlphaFoldDB; P32073; -.
DR   SMR; P32073; -.
DR   STRING; 44689.P32073; -.
DR   MEROPS; C26.962; -.
DR   PaxDb; 44689-DDB0215334; -.
DR   EnsemblProtists; EAL66537; EAL66537; DDB_G0281551.
DR   GeneID; 8623144; -.
DR   KEGG; ddi:DDB_G0281551; -.
DR   dictyBase; DDB_G0281551; guaA.
DR   eggNOG; KOG1622; Eukaryota.
DR   HOGENOM; CLU_014340_0_2_1; -.
DR   InParanoid; P32073; -.
DR   OMA; IVRKADH; -.
DR   PhylomeDB; P32073; -.
DR   Reactome; R-DDI-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   Reactome; R-DDI-9748787; Azathioprine ADME.
DR   UniPathway; UPA00189; UER00296.
DR   PRO; PR:P32073; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; ISS:dictyBase.
DR   GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; ISS:dictyBase.
DR   GO; GO:0046037; P:GMP metabolic process; ISS:dictyBase.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 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   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   1: Evidence at protein level;
KW   ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..718
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140256"
FT   DOMAIN          43..247
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   DOMAIN          248..457
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT   ACT_SITE        128
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        221
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        223
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         275..281
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT   CONFLICT        535
FT                   /note="G -> V (in Ref. 1; AAA33213)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   718 AA;  79562 MW;  DCB5DCDE84793DEA CRC64;
     MTITSPVIKT PPLNSEIRLE SNLTVESGDI EINEKDIVNA SEVIVILDAG SQYSKVIDRR
     VRELNVASEI HPLNIDLLEL IKIKSKSGST IKGIIISGGP ESVYGENAPK FDKSLFSEKL
     NLPIFGICYG MQLMNYIFGG KVESNSQRED GVHNIEILKD ENQQLVSKLF KNLNQTEQVL
     LTHGDSVTKI ADGFKIICKS DDGIVSGIEN ERLGYYGVQF HPEVDLTTNG KKMFSNFLID
     ICGCSANYTL DDREQQAITY IKSIVSNKKV LVLVSGGVDS TVCAALISKA IGPENVIALH
     IDNGFMRKDE SLNVEKALSV LGLHLIVVDA SQTFYNSTTT IKGHLTSSLK ETISPEERRK
     IIGDTFMRVA ENEVKKLGLQ PEDVYLAQGT LRPDLIESSS KTVSGVADVI KTHHNDTELV
     RILRDSGRVV EPLKDYHKDE VRELGKSLGL SDSLVWRQPF PGPGLAIRII CADEPYLVNY
     DFTNNVVQYL VTGEASSELE SEVKIKIDKQ LTEMKCKRQD KITIKPVLLP IQTVGVQGDG
     RTYSYLLGLY SSENSTIDQI PWSYIFNLAR TIPKICHNIN RVVFIFSQNA TKHTNIKVSN
     EPVKHITPTR LTPDVIKQLQ HADSIVSEQL YKYNLIKSLS QVPVVSLPID FGVTGNRSIA
     IRTFITNDFM TGVPAIPGKN ISFDCLQEIT NNILTSVNGI SKVLFDCTSK PPGTTEFL
//