CHAC_ECOLI
ID CHAC_ECOLI Reviewed; 231 AA.
AC P39163; P77176;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glutathione-specific gamma-glutamylcyclotransferase {ECO:0000305|PubMed:27913623};
DE Short=Gamma-GCG {ECO:0000303|PubMed:27913623};
DE EC=4.3.2.7 {ECO:0000269|PubMed:27913623};
DE AltName: Full=Cation transport regulatory protein ChaC {ECO:0000305|Ref.1};
GN Name=chaC {ECO:0000312|EMBL:AAA20198.1}; OrderedLocusNames=b1218, JW1209;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NM8191;
RA Ivey D.M., Guffanti A.A., Zemsky J., Pinner E., Karpel R., Padan E.,
RA Schuldiner S., Krulwich T.A.;
RT "Accessory and regulatory proteins associated with the Ca2+/H+ antiporter
RT of Escherichia coli.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27913623; DOI=10.1074/jbc.m116.727479;
RA Kaur A., Gautam R., Srivastava R., Chandel A., Kumar A., Karthikeyan S.,
RA Bachhawat A.K.;
RT "ChaC2, an enzyme for slow turnover of cytosolic glutathione.";
RL J. Biol. Chem. 292:638-651(2017).
CC -!- FUNCTION: Catalyzes the cleavage of glutathione into 5-oxo-L-proline
CC and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on
CC other gamma-glutamyl peptides. {ECO:0000269|PubMed:27913623}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione = 5-oxo-L-proline + L-cysteinylglycine;
CC Xref=Rhea:RHEA:47724, ChEBI:CHEBI:57925, ChEBI:CHEBI:58402,
CC ChEBI:CHEBI:61694; EC=4.3.2.7;
CC Evidence={ECO:0000269|PubMed:27913623};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 mM for glutathione {ECO:0000269|PubMed:27913623};
CC Note=kcat is 13 min(-1) for glutathione.
CC {ECO:0000269|PubMed:27913623};
CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family. ChaC
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20198.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA36076.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L28709; AAA20198.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74302.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA36076.1; ALT_INIT; Genomic_DNA.
DR PIR; G64868; G64868.
DR RefSeq; NP_415736.2; NC_000913.3.
DR RefSeq; WP_001336325.1; NZ_SSZK01000010.1.
DR AlphaFoldDB; P39163; -.
DR SMR; P39163; -.
DR BioGRID; 4261606; 11.
DR IntAct; P39163; 2.
DR STRING; 511145.b1218; -.
DR PaxDb; P39163; -.
DR PRIDE; P39163; -.
DR EnsemblBacteria; AAC74302; AAC74302; b1218.
DR EnsemblBacteria; BAA36076; BAA36076; BAA36076.
DR GeneID; 945793; -.
DR KEGG; ecj:JW1209; -.
DR KEGG; eco:b1218; -.
DR PATRIC; fig|511145.12.peg.1269; -.
DR EchoBASE; EB2303; -.
DR eggNOG; COG3703; Bacteria.
DR HOGENOM; CLU_070703_1_0_6; -.
DR InParanoid; P39163; -.
DR OMA; LLWYTDF; -.
DR PhylomeDB; P39163; -.
DR BioCyc; EcoCyc:EG12403-MON; -.
DR BioCyc; MetaCyc:EG12403-MON; -.
DR PRO; PR:P39163; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IDA:EcoCyc.
DR GO; GO:0061928; F:glutathione specific gamma-glutamylcyclotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
DR CDD; cd06661; GGCT_like; 1.
DR InterPro; IPR006840; ChaC.
DR InterPro; IPR013024; GGCT-like.
DR InterPro; IPR036568; GGCT-like_sf.
DR PANTHER; PTHR12192; PTHR12192; 1.
DR Pfam; PF04752; ChaC; 1.
DR SUPFAM; SSF110857; SSF110857; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..231
FT /note="Glutathione-specific gamma-glutamylcyclotransferase"
FT /id="PRO_0000089636"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O75223"
FT BINDING 49..54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O75223"
FT CONFLICT 15
FT /note="A -> V (in Ref. 1; AAA20198)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="C -> F (in Ref. 1; AAA20198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25512 MW; 9D7088566D553A7C CRC64;
MITRDFLMNA DCKTAFGAIE ESLLWSAEQR AASLAATLAC RPDEGPVWIF GYGSLMWNPA
LEFTESCTGT LVGWHRAFCL RLTAGRGTAH QPGRMLALKE GGRTTGVAYR LPEETLEQEL
TLLWKREMIT GCYLPTWCQL DLDDGRTVNA IVFIMDPRHP EYESDTRAQV IAPLIAAASG
PLGTNAQYLF SLEQELIKLG MQDDGLNDLL VSVKKLLAEN FPDGVLRPGF A
