GUAA_PSEA6
ID GUAA_PSEA6 Reviewed; 525 AA.
AC Q15R63;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=Patl_3119;
OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=342610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6c / ATCC BAA-1087;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA Bartlett D., Higgins B.P., Richardson P.;
RT "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL Submitted (JUN-2006) 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; CP000388; ABG41625.1; -; Genomic_DNA.
DR RefSeq; WP_011575863.1; NC_008228.1.
DR AlphaFoldDB; Q15R63; -.
DR SMR; Q15R63; -.
DR STRING; 342610.Patl_3119; -.
DR EnsemblBacteria; ABG41625; ABG41625; Patl_3119.
DR KEGG; pat:Patl_3119; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_6; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001981; 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..525
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_1000120365"
FT DOMAIN 9..207
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 208..400
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 181
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 183
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 235..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 525 AA; 58547 MW; 15D199E406F03DBB CRC64;
MTTNIHDQRI LILDFGSQYT QLIARRVREI GVYCELWAWD VTEEQIREFN PNGIILSGGP
ESVHAKDSPR APQYVFDAGV PVFGICYGMQ TMAEQLGGAV LGSDMREFGY AQVEVVEQMA
LLNNIEDHVS PNGNALLDVW MSHGDKVAAV PDGFITAAKT DSCPFAAIVH PEKQFYGVQF
HPEVTHTRQG QRMLSHFVLD ICQCEKLWTP DAIIEDAVAR MKKQIGDDEV ILGLSGGVDS
SVVAMLLHRA IGKNLTCVFV DNGLLRLNEG QQVMDMFGDH FGLNIIKIDA EERFLSALAG
TDEPEAKRKI IGRVFVEVFD EESKKLKNAK WLAQGTIYPD VIESAGSATG KAHVIKSHHN
VGGLPDDMAM GLVEPLRELF KDEVRKIGLE LGLPYDMLYR HPFPGPGLGV RVLGEVKKEY
CDLLRRADAI FIDELHKHDL YNKVSQAFTV FLPVKSVGVM GDARKYDWVV SLRAVETIDF
MTAHWAHLPY EFLGKVSNRI INEIDGISRV VYDISGKPPA TIEWE
