ID   GGHA_DICDI              Reviewed;         317 AA.
AC   Q54LN4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Gamma-glutamyl hydrolase A;
DE            EC=3.4.19.9;
DE   AltName: Full=Conjugase A;
DE   AltName: Full=GH A;
DE   AltName: Full=Gamma-Glu-X carboxypeptidase A;
DE   Flags: Precursor;
GN   Name=gghA; ORFNames=DDB_G0286535;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000088; EAL64169.1; -; Genomic_DNA.
DR   RefSeq; XP_637673.1; XM_632581.1.
DR   AlphaFoldDB; Q54LN4; -.
DR   SMR; Q54LN4; -.
DR   STRING; 44689.DDB0266399; -.
DR   MEROPS; C26.001; -.
DR   PaxDb; Q54LN4; -.
DR   PRIDE; Q54LN4; -.
DR   EnsemblProtists; EAL64169; EAL64169; DDB_G0286535.
DR   GeneID; 8625666; -.
DR   KEGG; ddi:DDB_G0286535; -.
DR   dictyBase; DDB_G0286535; gghA.
DR   eggNOG; KOG1559; Eukaryota.
DR   HOGENOM; CLU_058704_1_1_1; -.
DR   InParanoid; Q54LN4; -.
DR   OMA; APYEWGK; -.
DR   PhylomeDB; Q54LN4; -.
DR   PRO; PR:Q54LN4; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0008242; F:omega peptidase activity; ISS:UniProtKB.
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; IPR015527; Pept_C26_g-glut_hydrolase.
DR   InterPro; IPR011697; Peptidase_C26.
DR   PANTHER; PTHR11315; PTHR11315; 1.
DR   Pfam; PF07722; Peptidase_C26; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   PROSITE; PS51275; PEPTIDASE_C26_GGH; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..317
FT                   /note="Gamma-glutamyl hydrolase A"
FT                   /id="PRO_0000327993"
FT   DOMAIN          23..317
FT                   /note="Gamma-glutamyl hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        130
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT   ACT_SITE        242
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   317 AA;  35661 MW;  42D132E7B4ADF836 CRC64;
     MNKLIVVIIS IILMVGIVKV NGQTKINNRP IIGILTQPTD GDMTTFGSQY IAASYVKYIE
     SAGARVVPIL YDIDIKSLTE LMGSINGVFF PGGGVDFNNQ TVYTDTIQSI WSQVVEFNNN
     GDYFPLWGTC MGFQELALLS ADNFNLLSSY NSENYTVPLN FTSLAAGSRL FSLASSSIMQ
     SLASEPITMN NHQFGLSPQT YQQTSSINTF FDVLSTNVDR DGNTFISTIE AKNYPIYGTQ
     WHPEKPIFEW WDQEVMNHSF DSIMANQYTS NFFVNECRKS LHSFSDPSVE ASTLIYNYTP
     QYSESTVPDF EQIYYFN