GUAA_SPIKU
ID GUAA_SPIKU Reviewed; 512 AA.
AC P60502;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
OS Spiroplasma kunkelii.
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=47834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CR2-3x;
RX PubMed=12845528; DOI=10.1007/s00438-003-0878-3;
RA Zhao Y., Hammond R.W., Jomantiene R., Dally E.L., Lee I.-M., Jia H., Wu H.,
RA Lin S., Zhang P., Kenton S., Najar F.Z., Hua A., Roe B.A., Fletcher J.,
RA Davis R.E.;
RT "Gene content and organization of an 85-kb DNA segment from the genome of
RT the phytopathogenic mollicute Spiroplasma kunkelii.";
RL Mol. Genet. Genomics 269:592-602(2003).
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; AY198133; AAP58945.1; -; Genomic_DNA.
DR AlphaFoldDB; P60502; -.
DR SMR; P60502; -.
DR UniPathway; UPA00189; UER00296.
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.
FT CHAIN 1..512
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140174"
FT DOMAIN 6..195
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 196..387
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 169
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 171
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 223..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 512 AA; 57490 MW; 8C419F7E3E7231A6 CRC64;
MKTTNKIIIL DFGSQYTQLI ARRIRDLEVY CEVWPYNTAL EKIKTTSMKG IILSGGPASV
YEEDAFLIDK QLFELKVPVL GICYGMQIIS HLHEGTVQRA TKQEFGFSEL IIDNQEDLFA
NIPVKSQVWM SHADYIEGMP TNFIQIAHSE NSISAIKHSE KKIYGLQFHP EVTHTLIGQQ
LLSNFVFNIC GCQPKWKITE FISAAITEIK NKVGTDNVVL ALSGGVDSSV CAVLLHKAIG
KQLTCIFVDT GLLRQNSGWN DLQKFQEKFK LNIIKINAQE RFLTALKGVT NPEEKRKIIG
NLFIEIFNEE AIKIQNVKWL GQGTIYPDVI ESVSVKGPSA TIKSHHNVGG LPKDLPFQLI
EPLRELFKDE VRRTGEALGI DFKFVYKHPF PGPGLAVRII GEITAEKIAL LQAADQIFID
ELYQANLYDQ VAQAFVVLLP VQSVGVMGDV RTYGYTAVVR SVDTTDFMTA NWSRLPFELL
EKVSARIVSE VHGINRITYD ITSKPPGTIE WE