ID   GUAA_AERPE              Reviewed;         512 AA.
AC   Q9Y933;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 131.
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; OrderedLocusNames=APE_2452;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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.
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DR   EMBL; BA000002; BAA81467.1; -; Genomic_DNA.
DR   PIR; C72476; C72476.
DR   AlphaFoldDB; Q9Y933; -.
DR   SMR; Q9Y933; -.
DR   STRING; 272557.APE_2452; -.
DR   MEROPS; C26.A31; -.
DR   EnsemblBacteria; BAA81467; BAA81467; APE_2452.
DR   KEGG; ape:APE_2452; -.
DR   PATRIC; fig|272557.25.peg.1628; -.
DR   eggNOG; arCOG00085; Archaea.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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   HAMAP; MF_00344; GMP_synthase; 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; IPR022955; GMP_synthase.
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; TIGR00884; guaA_Cterm; 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   ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..512
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140215"
FT   DOMAIN          9..198
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          199..387
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        87
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000250"
FT   BINDING         226..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   512 AA;  55735 MW;  7F5DE439B4C87368 CRC64;
     MAKTLDSPGV LVVDFGGQYA HLIARRIREL GVYSEIVPAT SLDALGEALP RAAGVVLSGG
     PGSVWGSRHD EAAAMVLQLG KPVLGICYGH QLLAKVLGGE VGRSPLPEFG PTEVEVLDYG
     ILLNGLPSRF KVWMSHYDAV LRPPGEAKVL ARTPGSPVAA MELWGRVFGV QWHPEVRHTQ
     YGREVLDNWL SLVGAPRTWR PGDMVSELVE SVKKEVGDAL AVAAVSGGVD STVAALIAKK
     AIGSRLYPVF IDHGLHPEGE VERVVKLLSR LGLEPVMVDA GEEFLAALEG VGDPEEKRRV
     VGRVYAEVLE RAARDIGAEY LVQGTIYPDV IESGARPGAD TIKTHHNVGG LPKDMRLKLV
     EPLRYFYKDE VRLLAEKLGV PRELIWKQPV PGPGLAVRVE GPITREKLRI VRRADAIVRE
     EVEAAGLGGK LWQYFAVLTA SMATGVRGDS RSYGYVVAVR AVESVDAMTA KPAELPWWLL
     ERIARRITSE IPEVVRVVYD ITSKPPSTIE WE