GUAA_HAEDU
ID GUAA_HAEDU Reviewed; 523 AA.
AC Q7VLE9; Q9ZHL2;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=HD_1504;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 156-523.
RC STRAIN=35000HP / ATCC 700724;
RX PubMed=9811662; DOI=10.1128/jb.180.22.6013-6022.1998;
RA Ward C.K., Lumbley S.R., Latimer J.L., Cope L.D., Hansen E.J.;
RT "Haemophilus ducreyi secretes a filamentous hemagglutinin-like protein.";
RL J. Bacteriol. 180:6013-6022(1998).
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; AE017143; AAP96299.1; -; Genomic_DNA.
DR EMBL; AF057695; AAC79759.1; -; Genomic_DNA.
DR PIR; T31103; T31103.
DR RefSeq; WP_010945344.1; NC_002940.2.
DR AlphaFoldDB; Q7VLE9; -.
DR SMR; Q7VLE9; -.
DR STRING; 233412.HD_1504; -.
DR EnsemblBacteria; AAP96299; AAP96299; HD_1504.
DR KEGG; hdu:HD_1504; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_6; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001022; 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..523
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140130"
FT DOMAIN 8..205
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 206..398
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 179
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 181
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 233..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 523 AA; 58283 MW; 590F209389B0B3EA CRC64;
MNNIHNHKIL ILDFGSQYTQ LIARRIREIG VYCELWAWDV TEKQIREFNP TGIILSGGPE
STTETNSPHA PEYVFKAGVP VLGICYGMQT MAMQLGGLTE ASEQREFGYA AVELQHADQL
FAKLNDDLTA SQPKLDVWMS HGDKVTRLPA GFQTTAVTPT CPIAAMSDEK RRFYGVQFHP
EVTHTKSGLA LLTNFVENIC GCARSWTPEN IIEDAVAKIK QKVGNDQVIL GLSGGVDSSV
TALLLHRAIG KNLHCVFVDN GLLRLNEGDQ VMEMFGDKFG LNIIRVNAEE RFLEALKGID
EPEAKRKIIG KVFIDIFDDE AKKLTDVKWL AQGTIYPDVI ESAASKTGKA HVIKSHHNVG
GLPDYMKLGL VEPLRELFKD EVRKIGLTLG LPAEMLNRHP FPGPGLGVRV LGEIKKEYCD
LLRNADAIFI EELYKSGWYY KVSQAFTVFL PVKSVGVMGD GRKYDWVVSL RAVETIDFMT
AHWAHLPYEL LGKISNRIIN EVNGISRVVY DVSGKPPATI EWE
