ID A0AA36ITW9_9DINO Unreviewed; 376 AA.
AC A0AA36ITW9;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
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 ORFNames=EVOR1521_LOCUS18666 {ECO:0000313|EMBL:CAJ1393903.1};
OS Effrenium voratum.
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Effrenium.
OX NCBI_TaxID=2562239 {ECO:0000313|EMBL:CAJ1393903.1, ECO:0000313|Proteomes:UP001178507};
RN [1] {ECO:0000313|EMBL:CAJ1393903.1}
RP NUCLEOTIDE SEQUENCE.
RA Chen Y., Shah S., Dougan E. K., Thang M., Chan C.;
RL Submitted (AUG-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAJ1393903.1}.
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DR EMBL; CAUJNA010002669; CAJ1393903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA36ITW9; -.
DR Proteomes; UP001178507; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR CDD; cd01997; GMP_synthase_C; 1.
DR FunFam; 3.30.300.10:FF:000002; GMP synthase [glutamine-hydrolyzing]; 1.
DR Gene3D; 3.30.300.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00884; guaA_Cterm; 1.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
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:UP001178507}.
FT DOMAIN 53..250
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT BINDING 80..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 376 AA; 41658 MW; 57C3B385C4CDFE1D CRC64;
MYSVVAKVGG AFCAVTKVIG QIFSSLITII EKLVMFLIDV VVNSLKLVRA IFFSIFRLIH
KDLGGMRAWT EECPAVSPAL PSSEEIAASS VMEADSESFC LHGTLQRCAS LSTSAREEFL
TGWSEWDAKF LAELVLDASN DFYKELAGVS EPEKKRKIIG RLFVEAFEKA VSEMGLPHEK
CLLLQGTLYP DVIESTSYKG PSSVIKTHHN VGGLPDRMKM EVIEPLRLLF KDEVRKLGNE
LGLPVTSVMR HPFPGPGLGI RIIGEVTKES AVTLSAADDI YIEELRKAGH YDKIGQAFAV
LLPTVRSVGV MGDHRTYENV CVLRAVTTTD FMTADWYDMP HDLLARISNR IINEVKGINR
VCYDVSSKPP ATIEWE
//