GUAA_PSEAE
ID GUAA_PSEAE Reviewed; 525 AA.
AC Q9HXM6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=guaA; OrderedLocusNames=PA3769;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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 -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; AE004091; AAG07156.1; -; Genomic_DNA.
DR PIR; G83173; G83173.
DR RefSeq; NP_252458.1; NC_002516.2.
DR RefSeq; WP_003105901.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXM6; -.
DR SMR; Q9HXM6; -.
DR STRING; 287.DR97_4101; -.
DR MEROPS; C26.957; -.
DR PaxDb; Q9HXM6; -.
DR PRIDE; Q9HXM6; -.
DR EnsemblBacteria; AAG07156; AAG07156; PA3769.
DR GeneID; 880552; -.
DR KEGG; pae:PA3769; -.
DR PATRIC; fig|208964.12.peg.3946; -.
DR PseudoCAP; PA3769; -.
DR HOGENOM; CLU_014340_0_5_6; -.
DR InParanoid; Q9HXM6; -.
DR OMA; KRKIIGH; -.
DR PhylomeDB; Q9HXM6; -.
DR BioCyc; PAER208964:G1FZ6-3840-MON; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
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..525
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140162"
FT DOMAIN 9..207
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 208..400
FT /note="GMPS ATP-PPase"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 181
FT /evidence="ECO:0000250"
FT ACT_SITE 183
FT /evidence="ECO:0000250"
FT BINDING 235..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 525 AA; 57960 MW; CDBE1CCE73C32C40 CRC64;
MSQDIHAHRI LILDFGSQYT QLIARRVREI GVYCEIHPFD MSNEAIIAFA PRGIILAGGP
ESVHEADSPR APQAVFDLKV PLFGICYGMQ TMAEQMGGKV QGSDLREFGY ARVDVVGKAR
LLDGIEDHVD DDGVLGLDVW MSHGDKVTEM PAGFHILAST PSCPIAAMAD DARAYYGVQF
HPEVTHTKQG LRILSRFVLD ICGCAALWTP SNIVDDAIAT VRAQVGSSKV LLGLSGGVDS
SVVAALLHKA IGDQLTCVFV DNGLLRLHEG DQVMAMFAEN MGVKVIRANA EDKFLGRLAG
VADPEEKRKI IGRTFIEVFD EEATKLQDVK FLAQGTIYPD VIESAGAKTG KAHVIKSHHN
VGGLPEDMQF ELVEPLRELF KDEVRKIGLE LGLPYDMVYR HPFPGPGLGV RILGEVKKEY
ADLLRQADHI FIEELRAFDW YHKTSQAFVV FQPVKSVGVV GDGRRYAWVV ALRAVETIDF
MTARWAHLPY ELLEKVSNRI INEIAGISRV TYDVSSKPPA TIEWE
