GUAA_MESFL
ID GUAA_MESFL Reviewed; 513 AA.
AC Q6F1C4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; OrderedLocusNames=Mfl342;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_00344};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR EMBL; AE017263; AAT75699.1; -; Genomic_DNA.
DR RefSeq; WP_011183239.1; NC_006055.1.
DR RefSeq; YP_053583.1; NC_006055.1.
DR AlphaFoldDB; Q6F1C4; -.
DR SMR; Q6F1C4; -.
DR STRING; 265311.Mfl342; -.
DR MEROPS; C26.957; -.
DR EnsemblBacteria; AAT75699; AAT75699; Mfl342.
DR GeneID; 2897992; -.
DR KEGG; mfl:Mfl342; -.
DR PATRIC; fig|265311.5.peg.342; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_14; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000006647; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.880; -; 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 Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..513
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000229442"
FT DOMAIN 5..196
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 197..388
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 172
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 224..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 513 AA; 57744 MW; 475AD88DE27AC929 CRC64;
MKNTQILILD FGSQYTQLLA RRVREANIYT EVLPFDTSIE KIKEYPLLKG IILSGGPSSV
YLQNAYKIDS EILNLDIAIL GVCYGMQLLT QYFQGAVELA DEQEFGKAII TIDDKKNPLF
KNVTTESQVW MSHADHVTEL PVDFKQIAHS NASIAAIAHN TKPIYGIQFH AEVTHSLQGK
EMLENFLYDI AKCNKDWNLD DFIDQQIKEI KETVKDKQVI LGLSGGVDSS VAAAIIGKAI
GKQLTCIFVD TGLLRKNETI EVMKAYETNF DINIKLVEAS DLFFSELKGI KEPEAKRKII
GKCFIDVFTD AARQHKDADF LAQGTIYPDV IESSSHGASS KTIKSHHNVG GLPEDLKFRL
IEPLRNLFKD EVRQVGFKLG LPEEMINRHP FPGPGLGIRV IEEVTKDKVE ILQEADAIFI
KKLREWNLYN TVSQAFVTLL PVKTVGVMGD NRTYDYVVAL RSVNTIDFMT ATSTHLPWEF
LDEVVNEIIN KVDNVNRVVY DVTSKPPGTI EWE
