ID R4UD73_9MOLU Unreviewed; 513 AA.
AC R4UD73;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000256|HAMAP-Rule:MF_00344};
DE AltName: Full=GMP synthetase {ECO:0000256|HAMAP-Rule:MF_00344};
DE AltName: Full=Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00344};
GN Name=guaA {ECO:0000256|HAMAP-Rule:MF_00344,
GN ECO:0000313|EMBL:AGM25864.1};
GN ORFNames=SSYRP_v1c02680 {ECO:0000313|EMBL:AGM25864.1};
OS Spiroplasma syrphidicola EA-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276229 {ECO:0000313|EMBL:AGM25864.1, ECO:0000313|Proteomes:UP000013963};
RN [1] {ECO:0000313|EMBL:AGM25864.1, ECO:0000313|Proteomes:UP000013963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EA-1 {ECO:0000313|EMBL:AGM25864.1};
RX PubMed=23711669; DOI=10.1093/gbe/evt084;
RA Ku C., Lo W.S., Chen L.L., Kuo C.H.;
RT "Complete genomes of two dipteran-associated spiroplasmas provided insights
RT into the origin, dynamics, and impacts of viral invasion in spiroplasma.";
RL Genome Biol. Evol. 5:1151-1164(2013).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC {ECO:0000256|ARBA:ARBA00002332, ECO:0000256|HAMAP-Rule:MF_00344}.
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 Evidence={ECO:0000256|HAMAP-Rule:MF_00344};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153, ECO:0000256|HAMAP-
CC Rule:MF_00344}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00344}.
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DR EMBL; CP005078; AGM25864.1; -; Genomic_DNA.
DR RefSeq; WP_016340513.1; NC_021284.1.
DR AlphaFoldDB; R4UD73; -.
DR STRING; 1276229.SSYRP_v1c02680; -.
DR MEROPS; C26.957; -.
DR KEGG; ssyr:SSYRP_v1c02680; -.
DR PATRIC; fig|1276229.3.peg.267; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_14; -.
DR OrthoDB; 9802219at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000013963; Chromosome.
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; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00344; GMP_synthase; 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; IPR022955; GMP_synthase.
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; 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; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00344};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00344};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW Rule:MF_00344};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00344};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00344};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00344}; Reference proteome {ECO:0000313|Proteomes:UP000013963}.
FT DOMAIN 197..388
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 170
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 172
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 224..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 513 AA; 57949 MW; 6954DD8743BABAA1 CRC64;
MKEKNFIVIL DFGSQYTQLI ARRIRDLEVY CEVWPYNVEL EKLKAPGIKG VILSGGPASV
YAEDAFLIGK EIYHLGVPVL GICYGMQLTC HLFEGKVSRA AKQEFGFASL MLDETNDELF
YQIKDNEQVW MSHADHIEIL PPEFKQLGHS VNSISAIKHN SLPIYGLQFH PEVTHTVIGK
QLLANFVFKI AKCSPDWQLS SFIETTVENI RTIVKEDKVI LALSGGVDSS VCAVLLNQAI
GTQLQCIFID TGLLRLDSGW NDIQQLQQQF GLNVMRIDAK ERYFNSLKGV TDPEQKRKII
GQLFIEIFNE EAQKIKDVKW LGQGTIYPDI IESVSVKGPS ATIKSHHNVG GLPKEMPFQL
IEPLRELFKD EVRKTGELLG IGHDFVYKHP FPGPGLAVRI IGEVSPEKVD ILQQADHIFM
EELHKNHLYH EVSQAFVVLL PVQSVGVMGD VRTYGYTVVL RSVNTTDFMT AHWSELPYDF
LAHVSRRIVS EVSNINRVTY DITSKPPATI EWE
//
