ID   GUAAB_METKA             Reviewed;         314 AA.
AC   Q8TYD7;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
GN   Name=guaAB; Synonyms=guaA_1; OrderedLocusNames=MK0363;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000305}.
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DR   EMBL; AE009439; AAM01578.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TYD7; -.
DR   SMR; Q8TYD7; -.
DR   STRING; 190192.MK0363; -.
DR   EnsemblBacteria; AAM01578; AAM01578; MK0363.
DR   KEGG; mka:MK0363; -.
DR   PATRIC; fig|190192.8.peg.385; -.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   OMA; EGGIKSH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001826; 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:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00345; GMP_synthase_B; 1.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR026598; GMP_synthase_B.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR020536; ThiI_AANH.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02568; ThiI; 1.
DR   TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GMP biosynthesis; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN           1..314
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT                   /id="PRO_0000140242"
FT   DOMAIN          2..186
FT                   /note="GMPS ATP-PPase"
FT   BINDING         29..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  35327 MW;  B37326D571706311 CRC64;
     MFDPKKFVEE AIEELRREIG DRKAIIAVSG GVDSTTAAVL THRAIGSHLV CVFVDHGFMR
     KGEPERIREL LEEELGLNLR FVEAAEEFFE ALRGVTDPEE KRKIIGEKFI EVFERIAEEE
     EAEVLVQGTI APDIIESERG IKSHHNVGGL PEKLNLDVVE PLRDLYKDEV REVARYLGIP
     DEIVERMPFP GPGLAVRVLG EVTPEKVEIV REANAIVEEE VEKAVEEGKM SKPWQAFAAL
     LDCKATGVKG DERDYGWVIA VRIVESIDAM IADVPEVPWE VLRNIQDRIT SEVPEVTRVL
     FDITPKPPAT IEFE