ID   NIT1_BOVIN              Reviewed;         328 AA.
AC   Q32LH4;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Deaminated glutathione amidase;
DE            Short=dGSH amidase;
DE            EC=3.5.1.128 {ECO:0000250|UniProtKB:Q8VDK1};
DE   AltName: Full=Nitrilase homolog 1;
DE   Flags: Precursor;
GN   Name=NIT1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of the amide bond in N-(4-
CC       oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite
CC       repair reaction to dispose of the harmful deaminated glutathione. Plays
CC       a role in cell growth and apoptosis. Has tumor suppressor properties
CC       that enhances the apoptotic responsiveness in cancer cells. It is also
CC       a negative regulator of primary T-cells.
CC       {ECO:0000250|UniProtKB:Q8VDK1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(4-oxoglutaryl)-L-cysteinylglycine = 2-oxoglutarate +
CC         L-cysteinylglycine; Xref=Rhea:RHEA:54532, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:61694, ChEBI:CHEBI:138256;
CC         EC=3.5.1.128; Evidence={ECO:0000250|UniProtKB:Q8VDK1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8VDK1}.
CC       Mitochondrion {ECO:0000250|UniProtKB:Q8VDK1}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000305}.
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DR   EMBL; BC109575; AAI09576.1; -; mRNA.
DR   RefSeq; NP_001033112.1; NM_001038023.2.
DR   AlphaFoldDB; Q32LH4; -.
DR   SMR; Q32LH4; -.
DR   STRING; 9913.ENSBTAP00000026843; -.
DR   PaxDb; Q32LH4; -.
DR   GeneID; 504199; -.
DR   KEGG; bta:504199; -.
DR   CTD; 4817; -.
DR   eggNOG; KOG0807; Eukaryota.
DR   InParanoid; Q32LH4; -.
DR   OrthoDB; 1154369at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07572; nit; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR   InterPro; IPR001110; UPF0012_CS.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS01227; UPF0012; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..328
FT                   /note="Deaminated glutathione amidase"
FT                   /id="PRO_0000290343"
FT   DOMAIN          47..299
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        162
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        204
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   328 AA;  36240 MW;  FF089069F76B54D3 CRC64;
     MLGFIIRPPH QLLSLLSCPG LRIPRFSVLC APPRLRTMAA SSSFSELPLV AVCQVTSTPD
     KEQNFKTCAE LIREAARLGA CLAFLPEAFD FIARDPEETR RLSEPLSGNL LEEYTQLARE
     CGLWLSLGGF HERGQDWEQT QKIYNCHVIM NNMGSVVATY RKTHLCDVEI PGQGPMRESN
     STIPGPSLES PISTPAGKIG LAICYDMRFP ELSLALVQAG AEILTYPSAF GSVTGPAHWE
     VLLRARAIET QCYVVAAAQC GRHHEKRASY GHSMVVDPWG TVVARCSEGP GLCLARIDLN
     YLQQLRKQLP VFQHRRPDLY GNLGHPLS