HSP31_SCHPO
ID HSP31_SCHPO Reviewed; 244 AA.
AC O74914;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glutathione-independent glyoxalase hsp3101 {ECO:0000303|PubMed:24758716};
DE EC=4.2.1.130 {ECO:0000269|PubMed:24758716};
DE AltName: Full=Glyoxalase 3 homolog 1 {ECO:0000305|PubMed:24758716};
DE AltName: Full=Heat shock protein 31 homolog 1 {ECO:0000303|PubMed:24758716};
GN Name=hsp3101 {ECO:0000303|PubMed:24758716};
GN ORFNames=SPCC757.03c {ECO:0000312|PomBase:SPCC757.03c};
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
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).
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:24758716};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for methylglyoxal {ECO:0000269|PubMed:24758716};
CC Note=kcat is 31.1 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. HSP31-like subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA21228.1; -; Genomic_DNA.
DR PIR; T41594; T41594.
DR RefSeq; NP_587678.1; NM_001022673.2.
DR AlphaFoldDB; O74914; -.
DR SMR; O74914; -.
DR BioGRID; 276029; 2.
DR STRING; 4896.SPCC757.03c.1; -.
DR MEROPS; C56.A05; -.
DR MaxQB; O74914; -.
DR PaxDb; O74914; -.
DR EnsemblFungi; SPCC757.03c.1; SPCC757.03c.1:pep; SPCC757.03c.
DR GeneID; 2539466; -.
DR KEGG; spo:SPCC757.03c; -.
DR PomBase; SPCC757.03c; hsp3101.
DR VEuPathDB; FungiDB:SPCC757.03c; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; O74914; -.
DR OMA; DTIKSWN; -.
DR PhylomeDB; O74914; -.
DR BRENDA; 4.2.1.130; 5613.
DR PRO; PR:O74914; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
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:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; 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 Cytoplasm; Lyase; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..244
FT /note="Glutathione-independent glyoxalase hsp3101"
FT /id="PRO_0000317306"
FT ACT_SITE 139
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 140
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 173
FT /evidence="ECO:0000250|UniProtKB:Q04432"
SQ SEQUENCE 244 AA; 26743 MW; 297E24AB85765EE0 CRC64;
MASEGKVLLV ASSYYGPFYP DGMNTGVHFA ELLIPYQVFR EAGYEVQLTS ETGKCKFDDH
SIKKSALGEV ERDAFDNKDN EFWYALKDIK PADKINYKEF CIMFIAGGHA AMFDLPHATN
LQTLAQQIYA SNGVLAAVCH GPVMLPFVDD TKSPEGRSVV YGKKVTAFNS TGELVMGVSS
ALRERNMQDL NSLFREAGAE FVDPPTPMSD FTQVDGRIVT GVNPMSAKST AEAAIKVSQS
LRKT
