ID C4IXY5_DROME Unreviewed; 283 AA.
AC C4IXY5;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=MIP06849p {ECO:0000313|EMBL:ACQ89825.1};
GN Name=bur-RA {ECO:0000313|EMBL:ACQ89825.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ACQ89825.1};
RN [1] {ECO:0000313|EMBL:ACQ89825.1}
RP NUCLEOTIDE SEQUENCE.
RA Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.;
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; BT083416; ACQ89825.1; -; mRNA.
DR AlphaFoldDB; C4IXY5; -.
DR MEROPS; C26.A21; -.
DR PeptideAtlas; C4IXY5; -.
DR EnsemblMetazoa; FBtr0301342; FBpp0290556; FBgn0000239.
DR VEuPathDB; VectorBase:FBgn0000239; -.
DR HOGENOM; CLU_014340_0_2_1; -.
DR Bgee; FBgn0000239; Expressed in egg cell and 25 other cell types or tissues.
DR ExpressionAtlas; C4IXY5; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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; PF02540; NAD_synthase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 2: Evidence at transcript level;
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}.
FT DOMAIN 209..283
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 236..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 283 AA; 31748 MW; D58388BF0FC20B48 CRC64;
MNSNIFLGTA ENGLRHDKIV ILDAGAQYGK VIDRKVRELF VETDILPLDT PAATIRNNGY
RGIIISGGPN SVYAEDAPSY DPDLFKLKIP MLGICYGMQL INKEFGGTVL KKDVREDGQQ
NIEIETSCPL FSRLSRTQSV LLTHGDSVER VGENLKIGGW STNRIVTAIY NEVLRIYGVQ
FHPEVDLTIN GKQMLSNFLY EICELTPNFT MGSRKEECIR YIREKVGNNK VLLLVSGGVD
SSVCAALLRR ALYPHQIIAV HVDNGMTVDR LAKFIHLYFF YVK
//
