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Database: UniProt
Entry: D2ZS92_METSM
LinkDB: D2ZS92_METSM
Original site: D2ZS92_METSM 
ID   D2ZS92_METSM            Unreviewed;       190 AA.
AC   D2ZS92;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 57.
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   Synonyms=guaA {ECO:0000313|EMBL:EFC92692.1};
GN   ORFNames=METSMIF1_03726 {ECO:0000313|EMBL:EFC92692.1};
OS   Methanobrevibacter smithii DSM 2374.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=521002 {ECO:0000313|EMBL:EFC92692.1, ECO:0000313|Proteomes:UP000004028};
RN   [1] {ECO:0000313|EMBL:EFC92692.1, ECO:0000313|Proteomes:UP000004028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2374 {ECO:0000313|EMBL:EFC92692.1,
RC   ECO:0000313|Proteomes:UP000004028};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2010) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFC92692.1}.
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DR   EMBL; ABYV02000011; EFC92692.1; -; Genomic_DNA.
DR   RefSeq; WP_004034560.1; NZ_GG704759.1.
DR   AlphaFoldDB; D2ZS92; -.
DR   SMR; D2ZS92; -.
DR   MEROPS; C26.A31; -.
DR   GeneID; 78816967; -.
DR   PATRIC; fig|521002.11.peg.1672; -.
DR   HOGENOM; CLU_014340_1_4_2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000004028; Unassembled WGS sequence.
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}.
FT   DOMAIN          4..180
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        76
FT                   /note="Nucleophile"
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"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   190 AA;  21329 MW;  9B30ACC7F65697A1 CRC64;
     MTILVINNKG QYNHRIQRSL QYLKIPTELV PNTLSIEEIE AKNPIGLILG GGPSIEGAGN
     SEEYIKHFDI PILGICLGHQ LIAKAYGGQI DTSNTESYAK VEINIVNDEN LFSGLAPKME
     VWSSHKDEVK SIPDDFEILA NSNLCDVESF KHTEKDVYGI QFHPEVHHTP KGSTIFENFY
     EICKKRCNND
//
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