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Database: UniProt
Entry: A0A7G9G2W5_9FIRM
LinkDB: A0A7G9G2W5_9FIRM
Original site: A0A7G9G2W5_9FIRM 
ID   A0A7G9G2W5_9FIRM        Unreviewed;       430 AA.
AC   A0A7G9G2W5;
DT   10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2021, sequence version 1.
DT   18-JUN-2025, entry version 20.
DE   RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE            EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356};
GN   Name=guaA {ECO:0000313|EMBL:QNM05147.1};
GN   ORFNames=H9Q78_11955 {ECO:0000313|EMBL:QNM05147.1};
OS   Qiania dongpingensis.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC   Lachnospiraceae; Qiania.
OX   NCBI_TaxID=2763669 {ECO:0000313|EMBL:QNM05147.1, ECO:0000313|Proteomes:UP000515823};
RN   [1] {ECO:0000313|EMBL:QNM05147.1, ECO:0000313|Proteomes:UP000515823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSJ-38 {ECO:0000313|EMBL:QNM05147.1,
RC   ECO:0000313|Proteomes:UP000515823};
RA   Liu C., Sun Q.;
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC       {ECO:0000256|ARBA:ARBA00002332}.
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
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DR   EMBL; CP060634; QNM05147.1; -; Genomic_DNA.
DR   RefSeq; WP_249301955.1; NZ_CP060634.1.
DR   AlphaFoldDB; A0A7G9G2W5; -.
DR   KEGG; qdo:H9Q78_11955; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000515823; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   FunFam; 3.30.300.10:FF:000002; GMP synthase [glutamine-hydrolyzing]; 1.
DR   FunFam; 3.40.50.620:FF:000001; GMP synthase [glutamine-hydrolyzing]; 1.
DR   Gene3D; 3.30.300.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00884; guaA_Cterm; 1.
DR   NCBIfam; NF000848; PRK00074.1; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:QNM05147.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW   ProRule:PRU00886}; Reference proteome {ECO:0000313|Proteomes:UP000515823}.
FT   DOMAIN          116..305
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   BINDING         143..149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   430 AA;  48119 MW;  E3883FA5B0AA9AE5 CRC64;
     MKQDMIVILD LGSTENTVLA RAIRDMGVYS EIHPHDITVK ELQALQNVKG IILNGGENRI
     VDGEAVDVAP ELYGCGYPVI SIDHPTAKCE KRYDRIPEEP VLKSFVFDEC GAEANWNMKN
     FVADQIELVK QQVGGRKVLL ALSGGVDSSV VAALLLKAIG QQLVCVHVNH GLMRKNESEN
     VVSVFRDQLS ANLIYVDATE RFLTKLANVS DPEVKRKIIG GEFINVFQEE ARKLEGIDFL
     GQGTIYPDII ESGTKTAKMV KSHHNVGGLP EDMKFELVEP LKQLFKDEVR ACGIELGLPD
     YMVYRQPFPG PGLGVRCLGA ITRERLEAVR ESDAILREEF EKAGLDKKVW QYFTVVPDFK
     SVGMRNHARC FDYMVIIRAI NTVDAMTASI EKVDWDVLEV ITNRILNEVD HVNRVCYDMS
     PKPPATIEFE
//
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