HSP35_SCHPO
ID HSP35_SCHPO Reviewed; 251 AA.
AC Q09918;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Putative glutathione-independent glyoxalase hsp3105 {ECO:0000250|UniProtKB:O74914};
DE EC=4.2.1.130 {ECO:0000250|UniProtKB:O74914};
DE AltName: Full=Glyoxalase 3 homolog 5 {ECO:0000250|UniProtKB:O74914};
DE AltName: Full=Heat shock protein 31 homolog 5 {ECO:0000250|UniProtKB:O74914};
GN Name=hsp3105 {ECO:0000303|PubMed:24758716};
GN ORFNames=SPAC1F7.06 {ECO:0000312|PomBase:SPAC1F7.06};
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 GENE NAME, AND LACK OF ACTIVE SITE RESIDUES.
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: May catalyze the conversion of methylglyoxal (MG) to D-
CC lactate in a single glutathione (GSH)-independent step. May play a role
CC in detoxifying endogenously produced glyoxals. Involved in protection
CC against reactive oxygen species (ROS). {ECO:0000250|UniProtKB:O74914,
CC ECO:0000250|UniProtKB:Q04432}.
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:0000250|UniProtKB:O74914};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. HSP31-like subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved active site residues critical for
CC glyoxalase activity. Its enzyme activity is therefore unsure.
CC {ECO:0000305|PubMed:24758716}.
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DR EMBL; CU329670; CAA91953.1; -; Genomic_DNA.
DR PIR; S62578; S62578.
DR RefSeq; NP_594492.1; NM_001019921.2.
DR AlphaFoldDB; Q09918; -.
DR SMR; Q09918; -.
DR BioGRID; 278183; 3.
DR STRING; 4896.SPAC1F7.06.1; -.
DR PaxDb; Q09918; -.
DR EnsemblFungi; SPAC1F7.06.1; SPAC1F7.06.1:pep; SPAC1F7.06.
DR GeneID; 2541687; -.
DR KEGG; spo:SPAC1F7.06; -.
DR PomBase; SPAC1F7.06; hsp3105.
DR VEuPathDB; FungiDB:SPAC1F7.06; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; Q09918; -.
DR OMA; CWNRRIT; -.
DR PhylomeDB; Q09918; -.
DR PRO; PR:Q09918; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0019172; F:glyoxalase III activity; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Lyase; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..251
FT /note="Putative glutathione-independent glyoxalase hsp3105"
FT /id="PRO_0000157855"
SQ SEQUENCE 251 AA; 27907 MW; B5A60207D035BB34 CRC64;
MDERHEAAGE TSEKPKVLFL LNSYYGPFYD DGDNTGVNVV DLYEAFKVFE ENGFDIVIAS
DTGDYGFDDK SFRDPAIVDE TQSIFSNPDC SLMKKLKNIA RLDRLNPSDY VIVYIPGGYG
CSFDFPHAKV VQDFLYRFYE TKGIICAVAQ ANIALAYTTN SDGQALCTNR RVTGCTWKDE
VQNGVLNVMN RLNFYSFGHI AENIGAIFES PPVYVEDPFI VEDGQLFTGS NTNSAKGVAM
EAVRAVLNYD G
