ID A0A291JNY0_9STAP Unreviewed; 513 AA.
AC A0A291JNY0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:SUM56198.1};
GN ORFNames=BJD96_13040 {ECO:0000313|EMBL:ATH61146.1}, BUZ60_11935
GN {ECO:0000313|EMBL:RIO39943.1}, BUZ61_00200
GN {ECO:0000313|EMBL:PTK60989.1}, CD130_04615
GN {ECO:0000313|EMBL:PNZ99164.1}, NCTC13834_02604
GN {ECO:0000313|EMBL:SUM56198.1};
OS Staphylococcus nepalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=214473 {ECO:0000313|EMBL:ATH61146.1, ECO:0000313|Proteomes:UP000217956};
RN [1] {ECO:0000313|Proteomes:UP000240400, ECO:0000313|Proteomes:UP000265695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 4025 {ECO:0000313|EMBL:RIO39943.1,
RC ECO:0000313|Proteomes:UP000265695}, and SNUC 4337
RC {ECO:0000313|EMBL:PTK60989.1, ECO:0000313|Proteomes:UP000240400};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
RN [2] {ECO:0000313|EMBL:ATH61146.1, ECO:0000313|Proteomes:UP000217956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1 {ECO:0000313|EMBL:ATH61146.1,
RC ECO:0000313|Proteomes:UP000217956};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Staphylococcus nepalensis JS1.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PNZ99164.1, ECO:0000313|Proteomes:UP000236280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15150 {ECO:0000313|EMBL:PNZ99164.1,
RC ECO:0000313|Proteomes:UP000236280};
RA Cole K., Golubchik T., Russell J., Foster D., Llewelyn M., Wilson D.,
RA Crook D., Paul J.;
RT "Draft genome sequences of 64 type strains of genus Staph aureus.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PTK60989.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SNUC 4337 {ECO:0000313|EMBL:PTK60989.1};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:SUM56198.1, ECO:0000313|Proteomes:UP000254412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13834 {ECO:0000313|EMBL:SUM56198.1,
RC ECO:0000313|Proteomes:UP000254412};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:RIO39943.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SNUC 4025 {ECO:0000313|EMBL:RIO39943.1};
RA Parvin R., Begum J.A., Chowdhury E.H., Islam M.R., Harder T.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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; CP017460; ATH61146.1; -; Genomic_DNA.
DR EMBL; PPRR01000055; PNZ99164.1; -; Genomic_DNA.
DR EMBL; PZHR01000001; PTK60989.1; -; Genomic_DNA.
DR EMBL; QXVN01000076; RIO39943.1; -; Genomic_DNA.
DR EMBL; UHDS01000001; SUM56198.1; -; Genomic_DNA.
DR KEGG; snl:BJD96_13040; -.
DR OrthoDB; 9802219at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000217956; Chromosome.
DR Proteomes; UP000236280; Unassembled WGS sequence.
DR Proteomes; UP000240400; Unassembled WGS sequence.
DR Proteomes; UP000254412; Unassembled WGS sequence.
DR Proteomes; UP000265695; 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; 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; PF03054; tRNA_Me_trans; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
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 199..388
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 86
FT /note="Nucleophile"
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 ACT_SITE 174
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 226..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 513 AA; 58136 MW; 874AC3A3113938B1 CRC64;
MEMAKEQELI LVLDFGSQYN QLITRRIREM GVYSELHDHE ISIEEIKRLN PKGIILSGGP
NSVYEEDSFT IDPEIYNLGV PILGICYGMQ LTTKLLGGKV ERANEREYGK AVINAKTDEL
FFGLPEEQNV WMSHSDKVIE IPEGFEVIAD SPSTNYAAIE DKSRRIYGVQ FHPEVRHTEF
GNDLLRNFVR RVCDCTGEWS MENFIDIEVE KIRGLVGDRR VLCAMSGGVD SSVVAVLLHK
AIGDQLTCIF VDHGLLRKGE GDMVMEQFGE GFNMNIIRVN AQERFMSKLQ GVSDPEQKRK
IIGNEFVYVF DDEASKLEGV DFLAQGTLYT DVIESGTKTA QTIKSHHNVG GLPEDMEFQL
IEPINTLFKD EVRELGIELG IPEHLVWRQP FPGPGLGIRV LGEITEDKLE IVRESDAILR
QVIREEGLER EVWQYFTVLP GIQSVGVMGD YRTYDHTVGI RAVTSIDGMT SDFARIDWEV
LQKISSRIVN EVDHVNRVVY DITSKPPSTI EWE
//
