ID A0A2P6FBN7_9MOLU Unreviewed; 512 AA.
AC A0A2P6FBN7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:PQM30794.1};
GN ORFNames=SMSRO_SF005830 {ECO:0000313|EMBL:PQM30794.1};
OS Spiroplasma poulsonii.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=2138 {ECO:0000313|EMBL:PQM30794.1, ECO:0000313|Proteomes:UP000031565};
RN [1] {ECO:0000313|EMBL:PQM30794.1, ECO:0000313|Proteomes:UP000031565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSRO {ECO:0000313|EMBL:PQM30794.1,
RC ECO:0000313|Proteomes:UP000031565};
RX PubMed=25827421;
RA Paredes J.C., Herren J.K., Schupfer F., Marin R., Claverol S., Kuo C.H.,
RA Lemaitre B., Beven L.;
RT "Genome sequence of the Drosophila melanogaster male-killing Spiroplasma
RT strain MSRO endosymbiont.";
RL MBio 6:e02437-e02414(2015).
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}.
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:PQM30794.1}.
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DR EMBL; JTLV02000001; PQM30794.1; -; Genomic_DNA.
DR RefSeq; WP_040092979.1; NZ_PETG01000001.1.
DR AlphaFoldDB; A0A2P6FBN7; -.
DR STRING; 2138.SMSRO_v1c05530; -.
DR OrthoDB; 9802219at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000031565; 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; -; 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; PR00099; CPSGATASE.
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}.
FT DOMAIN 196..387
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 169
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT 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 512 AA; 57498 MW; 2A8D2CCE0F0CE46A CRC64;
MKTENKIIIL DFGSQYTQLI ARRIRDLEVY CEVWPYNTPL EKIKTTPMKG IILSGGPASV
YAEDAFLIDS ELLQLDLPIL GICYGMQLIS HLSGGKVQRA AKQEFGFSEL VIDDHHDLFA
NVPVKSQVWM SHADHIEVMP KDFVQIAHSA NSISAIRHTT KKIYGLQFHS EVTHTLIGEQ
LLKNFVFKIC QCEADWKISE FITMSTREIK TKVGSHNVVL ALSGGVDSSV CAVLLHQAIG
QQLTCIFVDT GLLRQDSGWH DLQKFQKQFG LSILKIDAKE RFLTALKGVT NPEQKRKIIG
NLFIEIFNEE AQKIKNVKWL GQGTIYPDVI ESVSVKGPSA TIKSHHNVGG LPKDLPFQLI
EPLRELFKDE VRKTGEALGI DHQFVYKHPF PGPGLAVRII GEITSEKVTL LQAADQIFID
ELYNFDLYDQ VAQAFVVLLP VQSVGVMGDV RTYGYTAVIR SVDTTDFMTA NWSRLPFELL
DKVSSRIVSE VRGINRVTYD ITSKPPGTIE WE
//
