ID A0A9E0SPF7_UNCPS Unreviewed; 574 AA. AC A0A9E0SPF7; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 24-JUL-2024, entry version 5. DE RecName: Full=Glutathione hydrolase proenzyme {ECO:0000256|RuleBase:RU368036}; DE EC=2.3.2.2 {ECO:0000256|RuleBase:RU368036}; DE EC=3.4.19.13 {ECO:0000256|RuleBase:RU368036}; DE Contains: DE RecName: Full=Glutathione hydrolase large chain {ECO:0000256|RuleBase:RU368036}; DE Contains: DE RecName: Full=Glutathione hydrolase small chain {ECO:0000256|RuleBase:RU368036}; GN Name=ggt {ECO:0000313|EMBL:MBS0444417.1}; GN ORFNames=JSR59_00565 {ECO:0000313|EMBL:MBS0444417.1}; OS Pseudomonadota bacterium. OC Bacteria; Pseudomonadota. OX NCBI_TaxID=1977087 {ECO:0000313|EMBL:MBS0444417.1, ECO:0000313|Proteomes:UP000811002}; RN [1] {ECO:0000313|EMBL:MBS0444417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZAS AMP-55 {ECO:0000313|EMBL:MBS0444417.1}; RX PubMed=33819658; RA Wang Y., Zhao R., Liu L., Li B., Zhang T.; RT "Selective enrichment of comammox from activated sludge using RT antibiotics."; RL Water Res. 197:0-0(2021). RN [2] {ECO:0000313|EMBL:MBS0444417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZAS AMP-55 {ECO:0000313|EMBL:MBS0444417.1}; RA Wang Y., Cao Y., Meng X., Hu T., Wang S., Cao K.; RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=an S-substituted glutathione + H2O = an S-substituted L- CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, CC ChEBI:CHEBI:143103; EC=3.4.19.13; CC Evidence={ECO:0000256|ARBA:ARBA00001049, CC ECO:0000256|RuleBase:RU368036}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, CC ChEBI:CHEBI:78608; EC=2.3.2.2; CC Evidence={ECO:0000256|ARBA:ARBA00000250, CC ECO:0000256|RuleBase:RU368036}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; CC Evidence={ECO:0000256|ARBA:ARBA00001089, CC ECO:0000256|RuleBase:RU368036}; CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism. CC {ECO:0000256|RuleBase:RU368036}. CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are CC synthesized in precursor form from a single polypeptide. CC {ECO:0000256|RuleBase:RU368036}. CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit. CC {ECO:0000256|RuleBase:RU368036}. CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family. CC {ECO:0000256|ARBA:ARBA00009381, ECO:0000256|RuleBase:RU368036}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBS0444417.1}. 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; JAFEEF010000001; MBS0444417.1; -; Genomic_DNA. DR Proteomes; UP000811002; Unassembled WGS sequence. DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006751; P:glutathione catabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.246.130; -; 1. DR Gene3D; 3.60.20.40; -; 1. DR InterPro; IPR051792; GGT-related_enzyme. DR InterPro; IPR043138; GGT_lsub_C. DR InterPro; IPR000101; GGT_peptidase. DR InterPro; IPR043137; GGT_ssub. DR InterPro; IPR029055; Ntn_hydrolases_N. DR NCBIfam; TIGR00066; g_glut_trans; 1. DR PANTHER; PTHR43199; GLUTATHIONE HYDROLASE; 1. DR PANTHER; PTHR43199:SF1; GLUTATHIONE HYDROLASE PROENZYME; 1. DR Pfam; PF01019; G_glu_transpept; 1. DR PRINTS; PR01210; GGTRANSPTASE. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, KW ECO:0000256|RuleBase:RU368036}; KW Glutathione biosynthesis {ECO:0000256|RuleBase:RU368036}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368036}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368036}; KW Zymogen {ECO:0000256|RuleBase:RU368036}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..574 FT /note="Glutathione hydrolase proenzyme" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5038802774" FT ACT_SITE 375 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1" SQ SEQUENCE 574 AA; 60529 MW; 1AC41A281110A658 CRC64; MLTTTHRIAL IASVTAFACG AVEAASQAPV AAEHGMVVSA QHLATQVGVD VLKEGGNAID AAVAVGYALA VVYPAAGNLG GGGFMTIQLA DGRKTFLDFR EKAPLGATPN MYLDKDGNVI KGASTTGHLA VGVPGTVSGL ETARAKYGTL PRKALIAPAI AYAERGFTLD QGDVDLLVTS TDDFKKDPAS APIFLNKGEA FQPGQKLVQK DLAKTLQAIS DKGEDGFYKG WVGSAIVASS QAGKGLITQA DLDQYKTREL APVECDYRGF HVVSAPPPSS GGVVICEILN VLEGYPLKDL GFRSAQAVQY QIEAMRHAYV DRNSYLGDPD FVKNPLDRLL SKDYAAKIRG VIEPNKAGIS KDIKPGVAPH EGSNTTHYSI VDQMGNAVSV TYTLNDWFGA KVLAAGTGVL LNDEMDDFTA KVGVPNLYGL VQGEANKVEP GKRPLSSMSP TIVTKDGKPV MVVGTPGGSR IITAVLHTII NVIDYGMNVQ EAVDAPRFHQ QWLPETTNIE TFALSPDTKK ILEGWGQKFS GPQPANHVAA ILVGAPTLGG KPVGNNKFYG ANDPRRNSGL ALGY //