ID A0A1G2KVV9_9BACT Unreviewed; 534 AA.
AC A0A1G2KVV9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
GN ORFNames=A3J58_00340 {ECO:0000313|EMBL:OHA03575.1};
OS Candidatus Sungbacteria bacterium RIFCSPHIGHO2_02_FULL_52_23.
OC Bacteria; Candidatus Sungbacteria.
OX NCBI_TaxID=1802274 {ECO:0000313|EMBL:OHA03575.1, ECO:0000313|Proteomes:UP000178510};
RN [1] {ECO:0000313|EMBL:OHA03575.1, ECO:0000313|Proteomes:UP000178510}
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:OHA03575.1}.
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DR EMBL; MHQM01000023; OHA03575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2KVV9; -.
DR STRING; 1802274.A3J58_00340; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000178510; 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 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 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; PR00099; CPSGATASE.
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; 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 208..399
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 235..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 534 AA; 59434 MW; 9EEAF2321534439A CRC64;
MPVHHRFYSG TREYAQVVIL ECGSKSTPLI AGVCRDAGVC TRTMAPADFE HYAAASIPKA
VFVSGGPDSV YDFAALQIPY GLLMYLNHNH GTAIFGICYG AQALAHAAGG KVKKASFAEV
GTHMLKMKHV IGGYLGGPVV MNHSDEIASL PFGWERWGST ERSAYALFGT DNILCTLFHP
EMGDTQDGEK LIAHFLYSLA RCRQDHTTGP EAFVADAIPF ISDAAPEGGM VVGVSGGVDS
AVTLELCRQV LGRERVYGIH VDNGFLCEGE TEEVRRLLGE DGMIYEDAAR LFWRTCERIN
WRNRHEKDYF SELRQKVGER FISVFEKRAR RIGGIRYLGQ GTNFSDIQET NTGLVRHHNV
GGLPDRMELE VVEPLAGLHK FEIREVAEYL GLDQEIVWRQ PSPGPANSLR MWPPVTRAKA
SPVARANRIL EEEVRRYYPD PRDRPSQYYA ALISGRMAGI VGDKEVYGYA ILVRAVKRNP
RESYASAEPF SFPDDLWRTI DTRIRAEVVL QDGMPIVAVC WHGTGKPPAR IECH
//
