ID   GGP5_ARATH              Reviewed;         251 AA.
AC   O82225;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Gamma-glutamyl peptidase 5 {ECO:0000305};
DE            EC=3.4.19.- {ECO:0000305};
GN   Name=GGP5 {ECO:0000305};
GN   OrderedLocusNames=At2g23970 {ECO:0000312|Araport:AT2G23970};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in glucosinolate biosynthesis. Hydrolyzes the gamma-
CC       glutamyl peptide bond of several glutathione (GSH) conjugates to
CC       produce Cys-Gly conjugates related to glucosinolates. The gamma-Glu-
CC       Cys-Gly-GSH conjugates are the sulfur-donating molecule in
CC       glucosinolate biosynthesis. {ECO:0000250|UniProtKB:Q9M0A7}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9M0A7}.
CC   -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
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DR   EMBL; AC005170; AAC63665.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07509.1; -; Genomic_DNA.
DR   EMBL; DQ056540; AAY78692.1; -; mRNA.
DR   PIR; A84631; A84631.
DR   RefSeq; NP_179975.1; NM_127959.2.
DR   AlphaFoldDB; O82225; -.
DR   SMR; O82225; -.
DR   STRING; 3702.AT2G23970.1; -.
DR   MEROPS; C26.A05; -.
DR   PaxDb; O82225; -.
DR   PRIDE; O82225; -.
DR   ProteomicsDB; 224784; -.
DR   EnsemblPlants; AT2G23970.1; AT2G23970.1; AT2G23970.
DR   GeneID; 816930; -.
DR   Gramene; AT2G23970.1; AT2G23970.1; AT2G23970.
DR   KEGG; ath:AT2G23970; -.
DR   Araport; AT2G23970; -.
DR   TAIR; locus:2061496; AT2G23970.
DR   eggNOG; KOG3179; Eukaryota.
DR   HOGENOM; CLU_054974_0_1_1; -.
DR   InParanoid; O82225; -.
DR   OMA; YITVQGH; -.
DR   OrthoDB; 1450344at2759; -.
DR   PhylomeDB; O82225; -.
DR   PRO; PR:O82225; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O82225; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01741; GATase1_1; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR044992; ChyE-like.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   PANTHER; PTHR42695; PTHR42695; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..251
FT                   /note="Gamma-glutamyl peptidase 5"
FT                   /id="PRO_0000435504"
FT   DOMAIN          17..214
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   251 AA;  28312 MW;  81F98F0E5E861D8F CRC64;
     MVNEQKRFAL FLATSDSTFV KKAYGGYFNV FVSTFGEDGE QWDLFRVIDG EFPDDKDLDK
     YDGFVISGSL NDAFGDDDWI VKLCSLCQKL DDMKKKVLGI CFGHQILSRI KGGKVGRASR
     GLDMGLRSIT MVTDAVKPGG YFGSQIPKSL AIIKCHQDEV LELPESATLL AYSDKYNVEM
     CSYGNHLLGI QGHPEYNKEI LFEIIDRVVN LKLMEQDFAD KAKATMENAE PDRKQWQTLC
     KNFLKGRSEQ V