GUAAA_THEAC
ID GUAAA_THEAC Reviewed; 200 AA.
AC Q9HJM3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 118.
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}; OrderedLocusNames=Ta0944;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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=CAC12073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL445066; CAC12073.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_010901354.1; NC_002578.1.
DR PDB; 2A9V; X-ray; 2.24 A; A/B/C/D=1-200.
DR PDBsum; 2A9V; -.
DR AlphaFoldDB; Q9HJM3; -.
DR SMR; Q9HJM3; -.
DR STRING; 273075.Ta0944m; -.
DR MEROPS; C26.A31; -.
DR EnsemblBacteria; CAC12073; CAC12073; CAC12073.
DR GeneID; 1457057; -.
DR KEGG; tac:Ta0944; -.
DR eggNOG; arCOG00087; Archaea.
DR HOGENOM; CLU_014340_1_4_2; -.
DR OMA; GPDMDRI; -.
DR OrthoDB; 79931at2157; -.
DR UniPathway; UPA00189; UER00296.
DR EvolutionaryTrace; Q9HJM3; -.
DR Proteomes; UP000001024; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glutamine amidotransferase; GMP biosynthesis;
KW Ligase; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..200
FT /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT /id="PRO_0000140235"
FT DOMAIN 3..193
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 167
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 169
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2A9V"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:2A9V"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2A9V"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:2A9V"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2A9V"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2A9V"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2A9V"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:2A9V"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:2A9V"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:2A9V"
FT STRAND 93..110
FT /evidence="ECO:0007829|PDB:2A9V"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2A9V"
FT STRAND 121..135
FT /evidence="ECO:0007829|PDB:2A9V"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2A9V"
FT STRAND 152..166
FT /evidence="ECO:0007829|PDB:2A9V"
FT HELIX 176..195
FT /evidence="ECO:0007829|PDB:2A9V"
SQ SEQUENCE 200 AA; 22471 MW; 747E9F28574E7C6A CRC64;
MLKIYVVDNG GQWTHREWRV LRELGVDTKI VPNDIDSSEL DGLDGLVLSG GAPNIDEELD
KLGSVGKYID DHNYPILGIC VGAQFIALHF GASVVKAKHP EFGKTKVSVM HSENIFGGLP
SEITVWENHN DEIINLPDDF TLAASSATCQ VQGFYHKTRP IYATQFHPEV EHTQYGRDIF
RNFIGICASY REIQKENFQH
