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GUAAA_SULAC
ID   GUAAA_SULAC             Reviewed;         188 AA.
AC   Q8X239; Q4JB85;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 3.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A {ECO:0000255|HAMAP-Rule:MF_01510};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_01510};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_01510};
GN   Name=guaAA {ECO:0000255|HAMAP-Rule:MF_01510}; Synonyms=guaA;
GN   OrderedLocusNames=Saci_0548;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-188.
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RA   Komorowski L., Schaefer G.;
RT   "Genomic sequence coding for putative GMP synthase and quinolate
RT   phosphoribosyltransferase from Sulfolobus acidocaldarius.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_01510}.
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_01510};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01510}.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000255|HAMAP-Rule:MF_01510}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC80124.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000077; AAY79944.1; -; Genomic_DNA.
DR   EMBL; AJ132638; CAC80124.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011277446.1; NC_007181.1.
DR   AlphaFoldDB; Q8X239; -.
DR   SMR; Q8X239; -.
DR   STRING; 330779.Saci_0548; -.
DR   MEROPS; C26.A31; -.
DR   PRIDE; Q8X239; -.
DR   EnsemblBacteria; AAY79944; AAY79944; Saci_0548.
DR   GeneID; 3474610; -.
DR   KEGG; sai:Saci_0548; -.
DR   PATRIC; fig|330779.12.peg.533; -.
DR   eggNOG; arCOG00087; Archaea.
DR   HOGENOM; CLU_014340_1_4_2; -.
DR   OMA; GPDMDRI; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_01510; GMP_synthase_A; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR023686; GMP_synthase_A.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..188
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT                   /id="PRO_0000140232"
FT   DOMAIN          2..188
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
SQ   SEQUENCE   188 AA;  20858 MW;  4215A86117773EB7 CRC64;
     MKVAVIYFGG QYNHLIVKDL KYLGLEAVAI TPDKSVEELK EFDSVVFGGG PYSVINELDK
     MGFAPDYVKS LNVPKLGICL GHQLIAKVLG GEVRKANKPE YGLTTVNIVD EDTILRGLKP
     SIKAWESHND EVVRPPSGFR ILASSENAKV QAMVNNDNSI FGVQFHPEVK HTEKGIEVFK
     NFIKICRK
 
 
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