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GUAA_SYNS9
ID   GUAA_SYNS9              Reviewed;         528 AA.
AC   Q3B0W1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
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};
GN   OrderedLocusNames=Syncc9902_0042;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) 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; CP000097; ABB25017.1; -; Genomic_DNA.
DR   RefSeq; WP_011358885.1; NC_007513.1.
DR   AlphaFoldDB; Q3B0W1; -.
DR   SMR; Q3B0W1; -.
DR   STRING; 316279.Syncc9902_0042; -.
DR   MEROPS; C26.957; -.
DR   EnsemblBacteria; ABB25017; ABB25017; Syncc9902_0042.
DR   KEGG; sye:Syncc9902_0042; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_3; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 504464at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002712; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 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..528
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_1000120441"
FT   DOMAIN          13..204
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          205..403
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        90
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         232..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   528 AA;  58848 MW;  5B8E3FB9BF1251F8 CRC64;
     MSQPSSDGQR QPAIVILDFG SQYSELIARR VRETEVFSVV IGYSTTADEL RRMAPKGIIL
     SGGPSSVYAE HAPVCDPAIW DLGIPVLGVC YGMQLMVQQL GGAVEAATGK AEYGKAPLEV
     DDPTDLLNNV ENGSTMWMSH GDSVKALPEG FVRLAHTANT PEAAVANLER KFYGVQFHPE
     VVHSTCGMAL IRNFVNHICG CEQDWTTNAF IDEAVALVRE QVGQKRVLLA LSGGVDSSTL
     AFLLKKAIGD QLTCMFIDQG FMRKGEPEFL MEFFDQKFNI NVEYINARKR FIDKLKGITD
     PEDKRKIIGT EFIRVFEEES KRLGPFDYLA QGTLYPDVIE SAGTNVDPKT GERVAVKIKS
     HHNVGGLPKD LRFKLVEPLR KLFKDEVRKV GRNLGLPEEI VRRHPFPGPG LAIRILGEVT
     DEKLNCLRDA DLIVREEIRD AGLYHDIWQA FAVLLPVRSV GVMGDQRTYA WPIVLRCVSS
     EDGMTADWSR LPYDLMERIS NRIVNEVKGV NRVVMDITSK PPGTIEWE
 
 
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