HSP32_SCHPO
ID HSP32_SCHPO Reviewed; 240 AA.
AC Q09675;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glutathione-independent glyoxalase hsp3102 {ECO:0000303|PubMed:24758716};
DE EC=4.2.1.130 {ECO:0000269|PubMed:24758716};
DE AltName: Full=Glyoxalase 3 homolog 2 {ECO:0000305|PubMed:24758716};
DE AltName: Full=Heat shock protein 31 homolog 2 {ECO:0000303|PubMed:24758716};
GN Name=hsp3102 {ECO:0000303|PubMed:24758716};
GN ORFNames=SPAC5H10.02c {ECO:0000312|PomBase:SPAC5H10.02c};
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=2.7 mM for methylglyoxal {ECO:0000269|PubMed:24758716};
CC Note=kcat is 58.0 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 -!- SIMILARITY: Belongs to the peptidase C56 family. HSP31-like subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA89952.1; -; Genomic_DNA.
DR PIR; S55480; S55480.
DR RefSeq; NP_592815.1; NM_001018215.2.
DR AlphaFoldDB; Q09675; -.
DR SMR; Q09675; -.
DR BioGRID; 278290; 2.
DR STRING; 4896.SPAC5H10.02c.1; -.
DR MEROPS; C56.A05; -.
DR MaxQB; Q09675; -.
DR PaxDb; Q09675; -.
DR EnsemblFungi; SPAC5H10.02c.1; SPAC5H10.02c.1:pep; SPAC5H10.02c.
DR GeneID; 2541799; -.
DR KEGG; spo:SPAC5H10.02c; -.
DR PomBase; SPAC5H10.02c; hsp3102.
DR VEuPathDB; FungiDB:SPAC5H10.02c; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; Q09675; -.
DR OMA; ASDYKVF; -.
DR PhylomeDB; Q09675; -.
DR BRENDA; 4.2.1.130; 5613.
DR PRO; PR:Q09675; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA: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..240
FT /note="Glutathione-independent glyoxalase hsp3102"
FT /id="PRO_0000157854"
FT ACT_SITE 141
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 142
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 175
FT /evidence="ECO:0000250|UniProtKB:Q04432"
SQ SEQUENCE 240 AA; 26117 MW; 22C5614F06D56296 CRC64;
MSIAKGKNAL LVASSYYGPF YPDGKNTGVH FSELLIPYNV FKKAGFNVQF VSENGSYKFD
DHSIEESKLG DFERKVFNDK NDDFWTNLNN MKKASDIVGK DYQLLFVAGG HAAMFDLPKA
TNLQAVAREV FTNGGVLSAV CHGPVLLANV KNPQSVEGKT VVYHKHVTAF NKAGEEKMGV
MDELKKRGMK SLNEIFAEAG ATFIDPPNPN VNFTQIDGKI VTGVNPQSAK STAEAAVSAL
