GUAA_DICDI
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 03-AUG-2022, entry version 139.
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 (Slime mold).
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.DDB0215334; -.
DR MEROPS; C26.962; -.
DR PaxDb; P32073; -.
DR PRIDE; P32073; -.
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; HIVHRHP; -.
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: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; 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; 3.40.50.620; -; 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 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
