GUAA_PROM3
ID GUAA_PROM3 Reviewed; 528 AA.
AC A2C5P2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=P9303_00451;
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000554; ABM76802.1; -; Genomic_DNA.
DR AlphaFoldDB; A2C5P2; -.
DR SMR; A2C5P2; -.
DR STRING; 59922.P9303_00451; -.
DR MEROPS; C26.957; -.
DR PRIDE; A2C5P2; -.
DR EnsemblBacteria; ABM76802; ABM76802; P9303_00451.
DR KEGG; pmf:P9303_00451; -.
DR HOGENOM; CLU_014340_0_5_3; -.
DR OMA; KRKIIGH; -.
DR BioCyc; PMAR59922:G1G80-48-MON; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002274; 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.
FT CHAIN 1..528
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_1000120360"
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; 59069 MW; 6240C8DB6406E70B CRC64;
MSNSQSEGQR QPAIVILDFG SQYSELIARR VRETEVYSLV MSYSTSADEL RQLAPKGIIL
SGGPSSVYAE RAPLCDPNIW DLGIPVLGVC YGMQLMVQQL GGRVEMATGK AEYGKAPLEI
DDPTDLLTNV ENGSTMWMSH GDSVRALPEG FVRLAHTANT PDAAVAYHTR SLYGVQFHPE
VVHSTDGMSL IRNFVYHICG CEPDWTTTAF IEEAVSQVRS QVGDKRVLLA LSGGVDSSTL
AFLLKKAIGD QLTCMFIDQG FMRKGEPEFL MDFFDRKFNI NVEYINARQR FISKLNGIVD
PEEKRKIIGT EFIRVFEEES NRLGPFDYLA QGTLYPDVIE SAGTNIDPKT GERVAVKIKS
HHNVGGLPKD LQFKLVEPLR RLFKDEVRKV GRSLGLPEEI VRRHPFPGPG LAIRILGEVT
DEKLNCLRDA DLIVREEIRE AGLYHEIWQA FAVLLPVRSV GVMGDQRTYA WPIVLRCVSS
EDGMTADWSR LPDELLERIS NRIVNEVRGV NRVVLDITSK PPGTIEWE