ID   DJ1_SCHPO               Reviewed;         191 AA.
AC   Q10356;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Glutathione-independent glyoxalase DJ-1 {ECO:0000303|PubMed:24758716};
DE            EC=4.2.1.130 {ECO:0000269|PubMed:24302734, ECO:0000269|PubMed:24758716};
DE   AltName: Full=Heat shock protein 31 homolog 6 {ECO:0000250|UniProtKB:O74914};
DE   AltName: Full=Protein DJ-1 homolog;
GN   Name=hsp3106 {ECO:0000312|PomBase:SPAC22E12.03c};
GN   Synonyms=spDJ-1 {ECO:0000303|PubMed:24758716};
GN   ORFNames=SPAC22E12.03c {ECO:0000312|PomBase:SPAC22E12.03c};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP   AND MUTAGENESIS OF GLU-16; CYS-111 AND HIS-130.
RX   PubMed=24758716; DOI=10.1186/1471-2148-14-86;
RA   Zhao Q., Su Y., Wang Z., Chen C., Wu T., Huang Y.;
RT   "Identification of glutathione (GSH)-independent glyoxalase III from
RT   Schizosaccharomyces pombe.";
RL   BMC Evol. Biol. 14:86-86(2014).
RN   [4]
RP   CATALYTIC ACTIVITY.
RX   PubMed=24302734; DOI=10.1074/jbc.m113.505784;
RA   Hasim S., Hussin N.A., Alomar F., Bidasee K.R., Nickerson K.W.,
RA   Wilson M.A.;
RT   "A glutathione-independent glyoxalase of the DJ-1 superfamily plays an
RT   important role in managing metabolically generated methylglyoxal in Candida
RT   albicans.";
RL   J. Biol. Chem. 289:1662-1674(2014).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
RX   PubMed=22971103; DOI=10.1111/febs.12004;
RA   Madzelan P., Labunska T., Wilson M.A.;
RT   "Influence of peptide dipoles and hydrogen bonds on reactive cysteine pKa
RT   values in fission yeast DJ-1.";
RL   FEBS J. 279:4111-4120(2012).
CC   -!- FUNCTION: Catalyzes the conversion of methylglyoxal (MG) to D-lactate
CC       in a single glutathione (GSH)-independent step (PubMed:24758716). May
CC       play a role in detoxifying endogenously produced glyoxals. Involved in
CC       protection against reactive oxygen species (ROS) (By similarity).
CC       {ECO:0000250|UniProtKB:Q04432, ECO:0000269|PubMed:24758716}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + methylglyoxal = (R)-lactate + H(+);
CC         Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130;
CC         Evidence={ECO:0000269|PubMed:24302734, ECO:0000269|PubMed:24758716};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10.8 mM for methylglyoxal {ECO:0000269|PubMed:24758716};
CC         Note=kcat is 85.7 min(-1) with methylglyoxal as substrate.
CC         {ECO:0000269|PubMed:24758716};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:24758716}. Nucleus {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:24758716}.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93890.1; -; Genomic_DNA.
DR   PIR; T38160; T38160.
DR   RefSeq; NP_594829.1; NM_001020258.2.
DR   PDB; 4GE0; X-ray; 1.45 A; A/B/C/D=1-191.
DR   PDB; 4GE3; X-ray; 1.50 A; A/B/C/D=1-191.
DR   PDB; 4QYT; X-ray; 1.05 A; A/B/C/D=1-191.
DR   PDBsum; 4GE0; -.
DR   PDBsum; 4GE3; -.
DR   PDBsum; 4QYT; -.
DR   AlphaFoldDB; Q10356; -.
DR   SMR; Q10356; -.
DR   BioGRID; 278266; 145.
DR   MINT; Q10356; -.
DR   STRING; 284812.Q10356; -.
DR   iPTMnet; Q10356; -.
DR   MaxQB; Q10356; -.
DR   PaxDb; 4896-SPAC22E12-03c-1; -.
DR   EnsemblFungi; SPAC22E12.03c.1; SPAC22E12.03c.1:pep; SPAC22E12.03c.
DR   GeneID; 2541772; -.
DR   KEGG; spo:SPAC22E12.03c; -.
DR   PomBase; SPAC22E12.03c; hsp3106.
DR   VEuPathDB; FungiDB:SPAC22E12.03c; -.
DR   eggNOG; KOG2764; Eukaryota.
DR   HOGENOM; CLU_000445_44_2_1; -.
DR   InParanoid; Q10356; -.
DR   OMA; KATCYPG; -.
DR   PhylomeDB; Q10356; -.
DR   BRENDA; 4.2.1.130; 5613.
DR   Reactome; R-SPO-3899300; SUMOylation of transcription cofactors.
DR   PRO; PR:Q10356; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0019172; F:glyoxalase III activity; IDA:PomBase.
DR   GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR   GO; GO:1903189; P:glyoxal metabolic process; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   CDD; cd03135; GATase1_DJ-1; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR48094:SF12; PARKINSON DISEASE PROTEIN 7 HOMOLOG; 1.
DR   PANTHER; PTHR48094; PROTEIN/NUCLEIC ACID DEGLYCASE DJ-1-RELATED; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Lyase; Nucleus; Reference proteome;
KW   Stress response.
FT   CHAIN           1..191
FT                   /note="Glutathione-independent glyoxalase DJ-1"
FT                   /id="PRO_0000157857"
FT   ACT_SITE        16
FT                   /evidence="ECO:0000305|PubMed:24758716"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000305|PubMed:24758716"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000305|PubMed:24758716"
FT   MUTAGEN         16
FT                   /note="E->A: Nearly completely abolishes enzymatic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:24758716"
FT   MUTAGEN         111
FT                   /note="C->A: Nearly completely abolishes enzymatic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:24758716"
FT   MUTAGEN         130
FT                   /note="H->A: Leads to 5- to 6-fold reduction in catalytic
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:24758716"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           14..26
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   STRAND          31..38
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           64..70
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   STRAND          72..76
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           80..87
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           90..99
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           111..114
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           115..119
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           134..139
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   STRAND          155..158
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           164..175
FT                   /evidence="ECO:0007829|PDB:4QYT"
FT   HELIX           178..187
FT                   /evidence="ECO:0007829|PDB:4QYT"
SQ   SEQUENCE   191 AA;  21078 MW;  909817B8D554AB2E CRC64;
     MVKVCLFVAD GTDEIEFSAP WGIFKRAEIP IDSVYVGENK DRLVKMSRDV EMYANRSYKE
     IPSADDFAKQ YDIAIIPGGG LGAKTLSTTP FVQQVVKEFY KKPNKWIGMI CAGTLTAKTS
     GLPNKQITGH PSVRGQLEEG GYKYLDQPVV LEENLITSQG PGTAMLFGLK LLEQVASKDK
     YNAVYKSLSM P
//