ID   GUAA2_BACTN             Reviewed;         435 AA.
AC   Q8A525;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Putative GMP synthase [glutamine-hydrolyzing] 2;
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase 2;
DE   AltName: Full=Glutamine amidotransferase 2;
GN   Name=guaA2; OrderedLocusNames=BT_2419;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- CAUTION: Could be the product of a pseudogene. Contains an internal
CC       deletion relative to its orthologs. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE015928; AAO77526.1; -; Genomic_DNA.
DR   RefSeq; NP_811332.1; NC_004663.1.
DR   RefSeq; WP_008764094.1; NZ_UYXG01000015.1.
DR   AlphaFoldDB; Q8A525; -.
DR   SMR; Q8A525; -.
DR   STRING; 226186.BT_2419; -.
DR   PaxDb; Q8A525; -.
DR   PRIDE; Q8A525; -.
DR   EnsemblBacteria; AAO77526; AAO77526; BT_2419.
DR   GeneID; 60923590; -.
DR   KEGG; bth:BT_2419; -.
DR   PATRIC; fig|226186.12.peg.2480; -.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_10; -.
DR   InParanoid; Q8A525; -.
DR   OMA; IVRKADH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
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   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   5: Uncertain;
KW   ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..435
FT                   /note="Putative GMP synthase [glutamine-hydrolyzing] 2"
FT                   /id="PRO_0000140095"
FT   DOMAIN          1..120
FT                   /note="Glutamine amidotransferase type-1; truncated"
FT   DOMAIN          121..310
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT   BINDING         148..154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   435 AA;  48286 MW;  3CAAB1D45B35D62C CRC64;
     MKQDMIVILD LGSHENTVLA RAIRALGVYS EIYPHDITVE ELKALPNVKG IIINGGLNNV
     IDGVAIDVNP SIYTMGIPVM AAGHDKATCA VKLPAFTDDI EAIKAAIKSF VFDTCQAEAN
     WNMANFVNDQ IELIRRQVGD KKVLLALSGG VDSSVVAALL LKAIGENLVC VHVNHGLMRK
     GESEDVVEVF SNQLKANLVY VDVTDRFLDK LAGVEDPEQK RKIIGGEFIR VFEEEARKLD
     GIDFLGQGTI YPDIVESGTK TAKMVKSHHN VGGLPEDLKF QLVEPLRQLF KDEVRACGLE
     LGLPYEMVYR QPFPGPGLGV RCLGAITRDR LEAVRESDAI LREEFQIAGL DKKVWQYFTV
     VPDFKSVGVR DNARSFDWPV IIRAVNTVDA MTATIEPVDW PILMKITDRI LKEVKNVNRV
     CYDMSPKPNA TIEWE