ID I1I2T4_BRADI Unreviewed; 542 AA.
AC I1I2T4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00021562};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
DE AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356};
GN Name=100831654 {ECO:0000313|EnsemblPlants:KQJ96040};
GN ORFNames=BRADI_3g20590v3 {ECO:0000313|EMBL:KQJ96040.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ96040.1};
RN [1] {ECO:0000313|EMBL:KQJ96040.1, ECO:0000313|EnsemblPlants:KQJ96040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ96040.1,
RC ECO:0000313|EnsemblPlants:KQJ96040};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ96040.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ96040.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ96040}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ96040};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
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DR EMBL; CM000882; KQJ96040.1; -; Genomic_DNA.
DR RefSeq; XP_003573701.1; XM_003573653.2.
DR AlphaFoldDB; I1I2T4; -.
DR STRING; 15368.I1I2T4; -.
DR MEROPS; C26.A07; -.
DR EnsemblPlants; KQJ96040; KQJ96040; BRADI_3g20590v3.
DR GeneID; 100831654; -.
DR Gramene; KQJ96040; KQJ96040; BRADI_3g20590v3.
DR KEGG; bdi:100831654; -.
DR eggNOG; KOG1622; Eukaryota.
DR HOGENOM; CLU_014340_0_5_1; -.
DR InParanoid; I1I2T4; -.
DR OMA; IWQSFAV; -.
DR OrthoDB; 6206at2759; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000008810; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.30.300.10; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00884; guaA_Cterm; 1.
DR NCBIfam; TIGR00888; guaA_Nterm; 1.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT DOMAIN 215..416
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 100
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 243..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 542 AA; 59489 MW; 625764FEF47091D7 CRC64;
MGSASAASLP TSAGAGENLV LILDFGSQYT HLITRRVRQL GVLSLCVSGT APLSSLAGLR
PRAVVLSGGP HSVHAPGAPT FPEGFLEFAA DAGAHVLGVC YGMQLLVQSL GGAVESGERQ
EYGDMEVEVT APSSALYGEV GKRQTVWMSH GDEVVRLPEG FEVVARSVQG AIAAIEHRDK
RYYGLQYHPE VTHSPQGMET LRRFLFDVCG IKADWKMQDV LDEEIKTIRS MVGPDEHVIC
ALSGGVDSTV AATLVHNAIG DRLHCVFVDN GLLRYKEQER VMSTFDSDLH LPVTCIDASE
QFLSKLKGVK DPEMKRKIIG REFIAVFDDF AHMLEKKLGK RPEYLVQGTL YPDVIESCPP
PGSGRTHSHT IKSHHNVGGL PKDMKLKLIE PLKLLFKDEV RKLGSILNVP ESFLKRHPFP
GPGLAVRVLG DVTEGNALEV LRQVDEIFVQ AIKDAGLYDK IWQAFAVFLP VQTVGVQGDQ
RTHSNAVTLR AITSEDGMTA DWYYFERQFL VDVVKKICNN VRGVNRVCQD ITSKPPATVE
WE
//
