ID   GUAAB_SULIN             Reviewed;         367 AA.
AC   C3NMG4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B {ECO:0000255|HAMAP-Rule:MF_00345};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00345};
DE   AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00345};
GN   Name=guaAB {ECO:0000255|HAMAP-Rule:MF_00345};
GN   OrderedLocusNames=YN1551_0655;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_00345}.
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:0000255|HAMAP-Rule:MF_00345};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00345}.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000255|HAMAP-Rule:MF_00345}.
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DR   EMBL; CP001404; ACP47784.1; -; Genomic_DNA.
DR   RefSeq; WP_012712098.1; NC_012623.1.
DR   AlphaFoldDB; C3NMG4; -.
DR   SMR; C3NMG4; -.
DR   EnsemblBacteria; ACP47784; ACP47784; YN1551_0655.
DR   GeneID; 7813310; -.
DR   GeneID; 7939065; -.
DR   KEGG; sin:YN1551_0655; -.
DR   HOGENOM; CLU_014340_0_0_2; -.
DR   OMA; EGGIKSH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000006818; 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   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; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GMP biosynthesis; Ligase; Nucleotide-binding;
KW   Purine biosynthesis.
FT   CHAIN           1..367
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT                   /id="PRO_1000205318"
FT   DOMAIN          2..190
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00345"
FT   BINDING         29..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00345"
SQ   SEQUENCE   367 AA;  41219 MW;  1F02275CCD735032 CRC64;
     MFDPASFVKE IGPQLKQKVG NERVLAAVSG GVDSTTAAVL AYNLLGNKVI PVLIDTGFLR
     KNEAEKIKAY LSNVLPNLIV VDERETFTSE IEGMEEAEAK RKKFRELFYS SISSLMRKFN
     AKYLMQGTIA ADWVETQGGI KTQHNVLVQI GIDTEKEWGF TLIEPLADLY KNEVRELARY
     LKLPKEISER QPFPGPGLLV RTIGKLTREK LEVVREANDI VEKYLDPFNY SQYFAVSFES
     DGNFVILDGI DAFLYKARAT GVKGDVRAYG NIAKVECSDI NAAKSFVDTL VKYDITHVLC
     SLDERSNGKY SIAIRAVITE DFMTADYARI PKEVLEKISS EILQKIPNVK EVLYDVTSKP
     PATIEFE