ID   GGH_SOYBN               Reviewed;         342 AA.
AC   P93164;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Gamma-glutamyl hydrolase;
DE            EC=3.4.19.9;
DE   AltName: Full=Conjugase;
DE   AltName: Full=GH;
DE   AltName: Full=Gamma-Glu-X carboxypeptidase;
DE   Flags: Precursor;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Williams 82;
RX   PubMed=8912628; DOI=10.1006/bbrc.1996.1608;
RA   Huangpu J., Pak J.H., Burkhart W., Graham M.C., Rickle S.A., Graham J.S.;
RT   "Purification and molecular analysis of an extracellular gamma-glutamyl
RT   hydrolase present in young tissues of the soybean plant.";
RL   Biochem. Biophys. Res. Commun. 228:1-6(1996).
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. Secreted, cell
CC       wall. Note=Extracellular or cell-wall bound.
CC   -!- TISSUE SPECIFICITY: Expressed only in young (1-15 day old) leaf, stem
CC       and root tissue.
CC   -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Cys residue in position 155 and the
CC       conserved His residue in position 268 essential for carbopeptidase
CC       activity. Its enzyme activity is therefore unsure. {ECO:0000305}.
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DR   EMBL; U63726; AAB26960.1; -; mRNA.
DR   PIR; T08837; T08837.
DR   RefSeq; NP_001235549.1; NM_001248620.1.
DR   AlphaFoldDB; P93164; -.
DR   SMR; P93164; -.
DR   STRING; 3847.GLYMA13G34290.1; -.
DR   MEROPS; C26.002; -.
DR   PRIDE; P93164; -.
DR   GeneID; 547881; -.
DR   KEGG; gmx:547881; -.
DR   eggNOG; KOG1559; Eukaryota.
DR   OrthoDB; 877490at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0009505; C:plant-type cell wall; IDA: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; IDA: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   2: Evidence at transcript level;
KW   Cell wall; Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..342
FT                   /note="Gamma-glutamyl hydrolase"
FT                   /id="PRO_0000026543"
FT   DOMAIN          45..342
FT                   /note="Gamma-glutamyl hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00607"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   342 AA;  37676 MW;  515CBAD1E5BA258C CRC64;
     MPNDSVLSLF FFVTLFTCLL SATSHDDHIF LPSQLHDDDS VSCTATDPSL NYKPVIGILT
     HPGDGASGRL SNATGVSYIA ASYVKFVESG GARVIPLIYN ESPENLNKKL DLVNGVLFTG
     GWAVSGPYLD TLGNIFKKAL ERNDAGDHFP VIAFNLGGNL VIRIVSEQTD ILEPFTASSL
     PSSLVLWNEA NAKGSLFQRF PSDLLTQLKT DCLVLHNHRY AISPRKLQYN TKLSDFFEIL
     ATSGDRDGKT FVSTARGRKY PVTVNLWQPE KNAFEWATSL KAPHTEDAIR VTQSTANFFI
     SEARKSTNTP DAQKVRDSLI YNYKPTFGGT AGKGYDQVYL FE