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Database: UniProt
Entry: E9GEB1_DAPPU
LinkDB: E9GEB1_DAPPU
Original site: E9GEB1_DAPPU 
ID   E9GEB1_DAPPU            Unreviewed;       305 AA.
AC   E9GEB1;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=folate gamma-glutamyl hydrolase {ECO:0000256|PROSITE-ProRule:PRU00607};
DE            EC=3.4.19.9 {ECO:0000256|PROSITE-ProRule:PRU00607};
GN   ORFNames=DAPPUDRAFT_302567 {ECO:0000313|EMBL:EFX82339.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX82339.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX82339.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(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; GL732540; EFX82339.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9GEB1; -.
DR   STRING; 6669.E9GEB1; -.
DR   MEROPS; C26.001; -.
DR   EnsemblMetazoa; EFX82339; EFX82339; DAPPUDRAFT_302567.
DR   KEGG; dpx:DAPPUDRAFT_302567; -.
DR   eggNOG; KOG1559; Eukaryota.
DR   HOGENOM; CLU_058704_1_1_1; -.
DR   InParanoid; E9GEB1; -.
DR   PhylomeDB; E9GEB1; -.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046900; P:tetrahydrofolylpolyglutamate metabolic process; IBA:GO_Central.
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:SF0; GAMMA-GLUTAMYL HYDROLASE; 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:UP000000305};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..305
FT                   /note="folate gamma-glutamyl hydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003237402"
FT   DOMAIN          72..251
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        134
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615527-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        245
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615527-1"
FT   ACT_SITE        247
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   305 AA;  33373 MW;  5461DD0033F635AE CRC64;
     MASFHFGWLV LTWAIIGHPD YIQGQSAVIT GPVIGILTQE VDSDLISVPP GAISFHLISY
     VKWLQTQNAT IVPIRINQTD YYYTTIFNSI NGLVIPGGSA NIRSSGYSKA GSILYNLAIT
     ANNNGDFFPI WGTCLGFQLL LYLSAGKKSY LASFPAQKKA LPLNFSPGAS TSRLYQNAPL
     DVMDLLASNQ STPNYHNYGI SPQNLTLSGL DKFYTNLATS IDDNGSTFVA SIEAKSYPIW
     GSQFHPEATS SWPAAVKPGL YFAEFFVNQS RKNQHRFTLE ASYVLTNLTS AVYQGPGKPS
     AFFFN
//
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