ID   GGP4_ARATH              Reviewed;         251 AA.
AC   F4INN2; O82224;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Gamma-glutamyl peptidase 4 {ECO:0000305};
DE            EC=3.4.19.- {ECO:0000305};
GN   Name=GGP4 {ECO:0000305};
GN   OrderedLocusNames=At2g23960 {ECO:0000312|Araport:AT2G23960};
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).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC63681.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC005170; AAC63681.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07508.1; -; Genomic_DNA.
DR   PIR; H84630; H84630.
DR   RefSeq; NP_001323529.1; NM_001335877.1.
DR   RefSeq; NP_179974.2; NM_127958.3.
DR   AlphaFoldDB; F4INN2; -.
DR   SMR; F4INN2; -.
DR   STRING; 3702.AT2G23960.1; -.
DR   MEROPS; C26.A05; -.
DR   PaxDb; F4INN2; -.
DR   PRIDE; F4INN2; -.
DR   EnsemblPlants; AT2G23960.1; AT2G23960.1; AT2G23960.
DR   GeneID; 816929; -.
DR   Gramene; AT2G23960.1; AT2G23960.1; AT2G23960.
DR   KEGG; ath:AT2G23960; -.
DR   Araport; AT2G23960; -.
DR   TAIR; locus:2061481; AT2G23960.
DR   eggNOG; KOG3179; Eukaryota.
DR   HOGENOM; CLU_054974_0_1_1; -.
DR   InParanoid; F4INN2; -.
DR   OMA; WQKICKN; -.
DR   OrthoDB; 1450344at2759; -.
DR   PRO; PR:F4INN2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4INN2; 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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..251
FT                   /note="Gamma-glutamyl peptidase 4"
FT                   /id="PRO_0000435503"
FT   DOMAIN          16..213
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        100
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   251 AA;  28755 MW;  0B3009148EE1A368 CRC64;
     MAEQKKYLLF LATPDSEFAK KTYGGYHNVF VSLLGDEGEQ WDSFRVVDGE FPEEKDLEKY
     EGFVISGSSH DAFQDTDWIL KLCDIIKKLD DMNKKVLGIC FGHQLIARAK GGKVARARKG
     PELCLGNITI VKEAVMPENY FGEEVPANLR IIKCHQDEVL ELPENAKLLA YSSMYEVEMY
     SIKDNFLCIQ GHPEYNRDIL FDIIDRVLAG GHIKQNFAET SKATMEKNEA DRKFWQKICK
     NFLKRQPSLL V