ID   YBEM_ECOBD              Reviewed;         262 AA.
AC   A0A140NCB4;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Deaminated glutathione amidase {ECO:0000303|PubMed:28373563};
DE            Short=dGSH amidase {ECO:0000303|PubMed:28373563};
DE            EC=3.5.1.128 {ECO:0000269|PubMed:28373563};
DE   AltName: Full=Nitrilase homolog 1;
DE   AltName: Full=ecYbeM {ECO:0000303|PubMed:28373563};
GN   Name=ybeM; OrderedLocusNames=ECBD_3025;
OS   Escherichia coli (strain B / BL21-DE3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=469008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / BL21-DE3;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT   "Complete sequence of Escherichia coli BL21(DE3).";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=B / BL21;
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) to 2-oxoglutarate
CC       and L-cysteinylglycine (specific activity 40.63 umol/min/mg), very
CC       little activity against alpha-ketoglutaramate (a-KGM, specific activity
CC       0.178 umol/min/mg) and no activity on glutathione or L-glutamine. May
CC       function as a metabolite 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; CP001665; ACT30034.1; -; Genomic_DNA.
DR   RefSeq; WP_000959109.1; NZ_CP053602.1.
DR   AlphaFoldDB; A0A140NCB4; -.
DR   SMR; A0A140NCB4; -.
DR   STRING; 469008.B21_00584; -.
DR   GeneID; 66671100; -.
DR   KEGG; ebd:ECBD_3025; -.
DR   PATRIC; fig|469008.15.peg.590; -.
DR   eggNOG; COG0388; Bacteria.
DR   HOGENOM; CLU_030130_1_2_6; -.
DR   OMA; MTCYDVR; -.
DR   Proteomes; UP000002032; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
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..262
FT                   /note="Deaminated glutathione amidase"
FT                   /id="PRO_0000440693"
FT   DOMAIN          1..238
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        40
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        147
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   262 AA;  28681 MW;  74CF04FD3B9CC1DF CRC64;
     MLVAAGQFAV TSVWEKNAEI CASLMAQAAE NDVSLFVLPE ALLARDDHDA DLSVKSAQLL
     EGEFLGRLRR ESKRNMMTTI LTIHVPSTPG RAWNMLVALQ AGNIVARYAK LHLYDAFAIQ
     ESRRVDAGNE IAPLLEVEGM KVGLMTCYDL RFPELALAQA LQGAEILVLP AAWVRGPLKE
     HHWSTLLAAR ALDTTCYMVA AGECGNKNIG QSRIIDPFGV TIAAASEMPA LIMAEVTPER
     VRQVRAQLPV LNNRRFAPPQ LL