GUAA_PROMS
ID GUAA_PROMS Reviewed; 528 AA.
AC A2BNG3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=A9601_00361;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
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; CP000551; ABM69324.1; -; Genomic_DNA.
DR RefSeq; WP_011817514.1; NC_008816.1.
DR AlphaFoldDB; A2BNG3; -.
DR SMR; A2BNG3; -.
DR STRING; 146891.A9601_00361; -.
DR EnsemblBacteria; ABM69324; ABM69324; A9601_00361.
DR KEGG; pmb:A9601_00361; -.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_3; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002590; 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_1000120363"
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; 59654 MW; 307FBEDFA3802D84 CRC64;
MSQTSLKKER DPSILILDFG SQYSELIARR IRETNVFSLV VSNFISIEDI NRINPKGIIL
SGGPNSVYEQ NAPRCDEKIF NLGIPILGIC YGMQLMVKEL GGTVISATKK AEYGRAPLNI
DQESDLLFDV EDKSIMWMSH GDSINCLPDG FNKIAHTENT LHAAISNDVK KLFGVQFHPE
VVHSEFGMRV IKNFVYKISC CTADWTTETY IEETIPRIRE QVGNKKVLLA LSGGVDSSTL
AFLLNKAIGN QLTCMFIDQG FMRKGEPEFL MNFFDKKFHI KVEYINARER FIAKLKGITD
PEQKRKIIGE EFIRVFEEES NRLGPFQYLA QGTLYPDVIE SAGTNIDPKT GERIAVKIKS
HHNVGGLPKD LQFKLVEPLR KLFKDEVRKV GAALGLPDEI IKRHPFPGPG LAIRILGEVN
NEKLDCLRDA DWIVRDEIKK AGLYNDIWQA FAVLLPVKTV GVMGDKRTYS WPIVLRCVSS
EDGMTADWSK IPFQILERIA NRIVNEVISV NRVVYDITSK PPGTIEWE
