ID A0A1F7BYY3_9BACT Unreviewed; 607 AA.
AC A0A1F7BYY3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
GN ORFNames=A3C52_01790 {ECO:0000313|EMBL:OGJ62711.1};
OS Candidatus Peribacteria bacterium RIFCSPHIGHO2_02_FULL_51_15.
OC Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria.
OX NCBI_TaxID=1801919 {ECO:0000313|EMBL:OGJ62711.1, ECO:0000313|Proteomes:UP000178956};
RN [1] {ECO:0000313|EMBL:OGJ62711.1, ECO:0000313|Proteomes:UP000178956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGJ62711.1}.
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DR EMBL; MFXU01000012; OGJ62711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7BYY3; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000178956; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.30.300.10; -; 2.
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; IPR004739; GMP_synth_GATase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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 Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
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; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 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 ECO:0000256|PROSITE-ProRule:PRU00605};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Ligase {ECO:0000256|ARBA:ARBA00022598};
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}.
FT DOMAIN 196..400
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 223..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 607 AA; 67361 MW; 3BDA25C4139B38E4 CRC64;
MSRKGAIIVL DFGGQYAHLI ASRVRRFGYF SEILPAETDV KDLKSAAGII LSGGPQSVYE
AGSPQADPEI LKLGIPILGL CYGHQWIAQI AGGTVQPGAV KEYGKTPIEL GKSILFKNVP
PSSVVWMSHG DEVKELPPPE YGHFKTIASS SSCKIAGMAD EEKKIFGLQF HIEVAHTEHG
LTILRNFVDL CKPEPWSVES YAKHVGEQIK SEAGDKKVFM LVSGGVDSSV AFMLLNKVLG
KERVQGLLID TGLMRKNEIK AVRDAFGKLG IDNLEVVDAS EEFFSNLKEI YDPEEKREII
GNTFINDQQR IFKEMDLEPK ATSQKPQAKW LLGQGTIYPD TIETGGTKHA DKIKTHHNRV
EVIQKMIEKG LVIEPLKEFY KDEVRKLGEE LGLPHELVWR HPFPGPGLGV RILCAKESTL
PEKIDETDLK LNGSYAVLPI RSVGVQGDGR TYRHAIAFFH SKPTEITERD MELATLVPNS
IPAFNRVLIC LTHEKSFVPE ISPGYITKER ADLLREADAI VDEEMRAAGL YEKIWQFPVV
LLPVGTRKGG QSIVLRPIES QDAMTANAVQ LPSNVLKKMT DRIMKLEGID AVFLDLTNKP
PGTIEWE
//
