DJ1_SCHPO
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 03-AUG-2022, entry version 127.
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; 4896.SPAC22E12.03c.1; -.
DR MaxQB; Q10356; -.
DR PaxDb; Q10356; -.
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; TSYPAMK; -.
DR PhylomeDB; Q10356; -.
DR BRENDA; 4.2.1.130; 5613.
DR Reactome; R-SPO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-SPO-9646399; Aggrephagy.
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:0036525; P:protein deglycation; ISO:PomBase.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; SSF52317; 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
