HSP34_SCHPO
ID HSP34_SCHPO Reviewed; 222 AA.
AC Q10092;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable glutathione-independent glyoxalase hsp3104 {ECO:0000250|UniProtKB:O74914};
DE EC=4.2.1.130 {ECO:0000250|UniProtKB:O74914};
DE AltName: Full=Glyoxalase 3 homolog 4 {ECO:0000250|UniProtKB:O74914};
DE AltName: Full=Heat shock protein 31 homolog 4 {ECO:0000250|UniProtKB:O74914};
GN Name=hsp3104 {ECO:0000303|PubMed:24758716};
GN ORFNames=SPAC11D3.13 {ECO:0000312|PomBase:SPAC11D3.13};
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.
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. May play a role in
CC 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}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. HSP31-like subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA92314.1; -; Genomic_DNA.
DR PIR; T37522; T37522.
DR RefSeq; NP_592808.1; NM_001018208.2.
DR AlphaFoldDB; Q10092; -.
DR SMR; Q10092; -.
DR STRING; 4896.SPAC11D3.13.1; -.
DR PaxDb; Q10092; -.
DR EnsemblFungi; SPAC11D3.13.1; SPAC11D3.13.1:pep; SPAC11D3.13.
DR GeneID; 2542927; -.
DR KEGG; spo:SPAC11D3.13; -.
DR PomBase; SPAC11D3.13; hsp3104.
DR VEuPathDB; FungiDB:SPAC11D3.13; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; Q10092; -.
DR OMA; NSAYNIA; -.
DR PhylomeDB; Q10092; -.
DR PRO; PR:Q10092; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; 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; Reference proteome; Stress response.
FT CHAIN 1..222
FT /note="Probable glutathione-independent glyoxalase hsp3104"
FT /id="PRO_0000157856"
FT ACT_SITE 124
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 125
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 155
FT /evidence="ECO:0000250|UniProtKB:Q04432"
SQ SEQUENCE 222 AA; 24226 MW; 9A466BE06AF17AD6 CRC64;
MVLFMKTVQR PEHISLKSCI PFKSLQRQGI VFRLSVRMVM LADDHSISDS ALSDSDKNAF
KDKNNDFWKA IKNAKNASDI NFSDYSIFFA AGGHGTLFDF PSATNLHKGA AKIYSMGGVI
AAVCHGPVIL PCIKDSTGFS IVKGKTVTAF NEIAEQQMNL MPTFEKYHFK TLNKLFQEAG
SNFVDPQEPF DDFVKTDGKL VTGANPASAA STAKAALNSL NS
