ID D7MX13_ARALL Unreviewed; 210 AA.
AC D7MX13;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=folate gamma-glutamyl hydrolase {ECO:0000256|PROSITE-ProRule:PRU00607};
DE EC=3.4.19.9 {ECO:0000256|PROSITE-ProRule:PRU00607};
DE Flags: Fragment;
GN ORFNames=ARALYDRAFT_359459 {ECO:0000313|EMBL:EFH38916.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate;
CC Xref=Rhea:RHEA:56784, Rhea:RHEA-COMP:14738, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:141005;
CC EC=3.4.19.9; Evidence={ECO:0000256|PROSITE-ProRule:PRU00607};
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DR EMBL; GL348903; EFH38916.1; -; Genomic_DNA.
DR RefSeq; XP_002862658.1; XM_002862612.1.
DR AlphaFoldDB; D7MX13; -.
DR MEROPS; C26.002; -.
DR MEROPS; C26.A01; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_262000001; fgenesh1_pg.C_scaffold_262000001; fgenesh1_pg.C_scaffold_262000001.
DR GeneID; 9298738; -.
DR Gramene; fgenesh1_pg.C_scaffold_262000001; fgenesh1_pg.C_scaffold_262000001; fgenesh1_pg.C_scaffold_262000001.
DR KEGG; aly:9298738; -.
DR eggNOG; KOG1559; Eukaryota.
DR HOGENOM; CLU_058704_1_1_1; -.
DR OrthoDB; 102889at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR015527; Pept_C26_g-glut_hydrolase.
DR PANTHER; PTHR11315:SF15; GAMMA-GLUTAMYL HYDROLASE 1; 1.
DR PANTHER; PTHR11315; PROTEASE FAMILY C26 GAMMA-GLUTAMYL HYDROLASE; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51275; PEPTIDASE_C26_GGH; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00607};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 10..141
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 18
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT ACT_SITE 131
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFH38916.1"
SQ SEQUENCE 210 AA; 23907 MW; 330B57095EB8A528 CRC64;
KALERNDAGE HFPVYGICLG FELMSIIISQ NRDILERFDA EDNASTLQFV DNVNIDGTLF
QRFPPELLKK LSTDCLVMQK HKYGITPANF QGNPALSSFF EILTTCIDEN SKTYVSTVKA
KRYPITGFQW HPEKNAFEWG SSAIPHSEDA IQVTQHAASY LVSEARKSLN RPPSKKVLSN
LIYNYKPTYC GYAGRGYDEV YIFTQPRSRF
//
