GUAA_STRT2
ID GUAA_STRT2 Reviewed; 527 AA.
AC Q5M4P4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=stu0886;
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV60553.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5M4P4; -.
DR SMR; Q5M4P4; -.
DR STRING; 264199.stu0886; -.
DR MEROPS; C26.957; -.
DR EnsemblBacteria; AAV60553; AAV60553; stu0886.
DR KEGG; stl:stu0886; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_9; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001170; 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..527
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000229476"
FT DOMAIN 19..212
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 213..402
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 186
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 188
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 240..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 527 AA; 58311 MW; 629C5B6F42ECC3FB CRC64;
MQKERVIMTN ISTLNDVQKI IVLDYGSQYN QLIARRIREF GVFSELKSHK ITADEVRAIN
PIGIILSGGP NSVYAEDAFG IDEEIFELGI PILGICYGMQ LLTHKLGGKV VPAGEAGNRE
YGQSTLRLRA QSELFAGTPE EQVVLMSHGD AVTEIPEGFH LVADSVDCPF AAMEDTKKNF
YGIQFHPEVR HTVYGNDILK NFAFSICGAK GDWSMANFVD MQIAQIRETV GDRKVLLGLS
GGVDSSVVGV LLQKAIGDQL TCIFVDHGLL RKGEGDQVME MLGGKFGLNI IRVDASKRFL
DLLAGVDDPE KKRKIIGNEF VHVFDDEASK LKGVDFLAQG TLYTDIIESG TETAQTIKSH
HNVGGLPEDM QFELIEPLNT LFKDEVRALG TELGMPDEVV WRQPFPGPGL AIRIMGEITE
EKLETVRESD AILREEIAKA GLDRDVWQYF TVNTGVRSVG VMGDGRTYDY TIAIRAITSI
DGMTADFAKL PWEVLQKISV RIVNEVDHVN RIVYDITSKP PATVEWE
