ID   NIT1_YEREN              Reviewed;         286 AA.
AC   P0DP68;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Deaminated glutathione amidase {ECO:0000305};
DE            Short=dGSH amidase {ECO:0000305};
DE            EC=3.5.1.128 {ECO:0000269|PubMed:28373563};
DE   AltName: Full=Nitrilase homolog 1;
DE            Short=yeNit1 {ECO:0000303|PubMed:28373563};
GN   Name=nit1 {ECO:0000303|PubMed:28373563}; ORFNames=CH48_2098;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516-87;
RA   Davenport K.W., Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O.,
RA   Coyne S.R., Daligault H.E., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=2516-87;
RX   PubMed=28373563; DOI=10.1073/pnas.1613736114;
RA   Peracchi A., Veiga-da-Cunha M., Kuhara T., Ellens K.W., Paczia N.,
RA   Stroobant V., Seliga A.K., Marlaire S., Jaisson S., Bommer G.T., Sun J.,
RA   Huebner K., Linster C.L., Cooper A.J.L., Van Schaftingen E.;
RT   "Nit1 is a metabolite repair enzyme that hydrolyzes deaminated
RT   glutathione.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:E3233-E3242(2017).
CC   -!- FUNCTION: Hydrolyzes deaminated glutathione (dGSH, 2-oxoglutaramate) to
CC       alpha-ketoglutarate (alpha-KG) and cysteinylglycine (specific activity
CC       6.50 umol/min/mg), has less activity against alpha-ketoglutaramate (a-
CC       KGM, specific activity 0.20 umol/min/mg), very little activity on
CC       glutathione and none on L-glutamine. May function as a metabolite
CC       repair enzyme. {ECO:0000269|PubMed:28373563}.
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:0000269|PubMed:28373563};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000305}.
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DR   EMBL; CP009838; AJJ28584.1; -; Genomic_DNA.
DR   RefSeq; WP_005163159.1; NZ_UHIX01000001.1.
DR   AlphaFoldDB; P0DP68; -.
DR   SMR; P0DP68; -.
DR   STRING; 1443113.LC20_00606; -.
DR   KEGG; yet:CH48_2098; -.
DR   eggNOG; COG0388; Bacteria.
DR   OMA; GNTYRES; -.
DR   BRENDA; 3.5.1.128; 6741.
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   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..286
FT                   /note="Deaminated glutathione amidase"
FT                   /id="PRO_0000440697"
FT   DOMAIN          4..252
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   286 AA;  31894 MW;  BF3CEF36D90EACEF CRC64;
     MKNANVALLQ LCSGENTRDN LAQIEQQIKQ LNSGIQLVMT PENALLFANA ASYRHHAEQH
     NDGPLQQEVR EMARRYGVWI QVGSMPMISR ESPDLITTSS LLFDSQGELK ARYDKIHMFD
     VDIKDIHGRY RESDTYQPGE HLTVADTPVG RLGMTVCYDL RFPGLFQALR AQGAEIISVP
     AAFTKVTGEA HWEILLRARA IENQCVILAA AQVGRHGATR RTWGHTMAVD AWGKIIGQNP
     DAVSALKVKI ETTGLKTIRN QMPVLQHNRF VSSLVPRLSD SKQSSK