ID W0JKT0_9EURY Unreviewed; 184 AA.
AC W0JKT0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A {ECO:0000256|HAMAP-Rule:MF_01510};
DE EC=6.3.5.2 {ECO:0000256|HAMAP-Rule:MF_01510};
DE AltName: Full=Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01510};
GN Name=guaAA {ECO:0000256|HAMAP-Rule:MF_01510};
GN ORFNames=HALLA_10455 {ECO:0000313|EMBL:AHF99208.1};
OS Halostagnicola larsenii XH-48.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHF99208.1, ECO:0000313|Proteomes:UP000019024};
RN [1] {ECO:0000313|EMBL:AHF99208.1, ECO:0000313|Proteomes:UP000019024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XH-48 {ECO:0000313|EMBL:AHF99208.1,
RC ECO:0000313|Proteomes:UP000019024};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01510};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_01510}.
CC -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC (A) and a GMP-binding subunit (B). {ECO:0000256|HAMAP-Rule:MF_01510}.
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DR EMBL; CP007055; AHF99208.1; -; Genomic_DNA.
DR RefSeq; WP_049952420.1; NZ_CP007055.1.
DR AlphaFoldDB; W0JKT0; -.
DR STRING; 797299.HALLA_10455; -.
DR GeneID; 25144883; -.
DR KEGG; hlr:HALLA_10455; -.
DR PATRIC; fig|797299.3.peg.1120; -.
DR eggNOG; arCOG00087; Archaea.
DR HOGENOM; CLU_014340_1_4_2; -.
DR OrthoDB; 10772at2157; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000019024; 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-UniRule.
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 NCBIfam; TIGR00888; guaA_Nterm; 1.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01510};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_01510};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW Rule:MF_01510};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01510};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01510};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01510}; Reference proteome {ECO:0000313|Proteomes:UP000019024}.
FT DOMAIN 5..178
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 161
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 163
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 184 AA; 19981 MW; 18234B8FA096AD0A CRC64;
MTKIVVVDNH GQFTHLEDRA LRDLGVDSEL IDNDTPPEEV DADGVVLSGG PDMDRTGQSA
AYLESDMPVL GICLGMQLIA EELGGRVGSG EYGGYADVTV DLLSENDPLT GSLYPETRVW
ASHADEVKEV PEGFERTASS DVCGVEAMSD TDRDLYGVQW HPEVAHTEEG DEVFENFLEI
CTDD
//
