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
//