ID A0A0S7YFR3_9BACT Unreviewed; 311 AA.
AC A0A0S7YFR3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
GN ORFNames=AMJ48_01970 {ECO:0000313|EMBL:KPJ73211.1};
OS Parcubacteria bacterium DG_74_1.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1703765 {ECO:0000313|EMBL:KPJ73211.1, ECO:0000313|Proteomes:UP000051540};
RN [1] {ECO:0000313|EMBL:KPJ73211.1, ECO:0000313|Proteomes:UP000051540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_74_1 {ECO:0000313|EMBL:KPJ73211.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ73211.1}.
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DR EMBL; LJNE01000006; KPJ73211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YFR3; -.
DR STRING; 1703765.AMJ48_01970; -.
DR PATRIC; fig|1703765.3.peg.565; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000051540; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR Gene3D; 3.30.300.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
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; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-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}; 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 1..190
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT BINDING 28..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 311 AA; 35239 MW; DAFE4A4E894FC2B9 CRC64;
MNYKKFIKEK IKEIREIVGE EKALSVLSGG VDSSAVTLLG YKALERNLKV VFVDNGLMRE
GEPESVVKNF QKLGIKVEIV NAQNIFFKAL KGKTDPEEKR KAVATAFYKD IFREIIKEKK
IKFLFQGTIL TDIEETVAGI KRQHNVLAQI GINPQKEFGY QVIEPLIKLR KDGVRKVSKL
LGLPRSICQR MPFPGPALSA RVIGEANRQK ITVVRKATKV VEKELKNSGA FQYFPVLMED
RATGLRNNKR EFGSIIILRC VESVDARKAQ PTKLPWKLLE KITKRLTTEI PGVNRVCYDI
TPKPPATIEY I
//