YBEM_ECO57
ID YBEM_ECO57 Reviewed; 262 AA.
AC P58054;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Deaminated glutathione amidase {ECO:0000250|UniProtKB:A0A140NCB4};
DE Short=dGSH amidase {ECO:0000250|UniProtKB:A0A140NCB4};
DE EC=3.5.1.128 {ECO:0000250|UniProtKB:A0A140NCB4};
DE AltName: Full=Nitrilase homolog 1;
GN Name=ybeM; OrderedLocusNames=Z0771, ECs0664;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Hydrolyzes deaminated glutathione (dGSH) to 2-oxoglutarate
CC and L-cysteinylglycine, and no activity on glutathione or L-glutamine.
CC May function as a metabolite repair enzyme.
CC {ECO:0000250|UniProtKB:A0A140NCB4}.
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:A0A140NCB4};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC NIT1/NIT2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG54960.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG54960.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB34087.1; -; Genomic_DNA.
DR PIR; D85562; D85562.
DR PIR; H90711; H90711.
DR RefSeq; NP_308691.1; NC_002695.1.
DR RefSeq; WP_000959109.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58054; -.
DR SMR; P58054; -.
DR STRING; 155864.EDL933_0698; -.
DR EnsemblBacteria; AAG54960; AAG54960; Z0771.
DR EnsemblBacteria; BAB34087; BAB34087; ECs_0664.
DR GeneID; 66671100; -.
DR GeneID; 917024; -.
DR KEGG; ece:Z0771; -.
DR KEGG; ecs:ECs_0664; -.
DR PATRIC; fig|386585.9.peg.775; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_030130_1_2_6; -.
DR OMA; MTCYDVR; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..262
FT /note="Deaminated glutathione amidase"
FT /id="PRO_0000213259"
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 /note="Proton donor"
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
