ID HSP33_SCHPO Reviewed; 261 AA.
AC O43084;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 24-JAN-2024, entry version 108.
DE RecName: Full=Probable glutathione-independent glyoxalase hsp3103 {ECO:0000250|UniProtKB:O74914};
DE EC=4.2.1.130 {ECO:0000250|UniProtKB:O74914};
DE AltName: Full=Glyoxalase 3 homolog 3 {ECO:0000250|UniProtKB:O74914};
DE AltName: Full=Heat shock protein 31 homolog 3 {ECO:0000250|UniProtKB:O74914};
GN Name=hsp3103 {ECO:0000303|PubMed:24758716};
GN ORFNames=SPBC947.09 {ECO:0000312|PomBase:SPBC947.09};
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 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 -!- SIMILARITY: Belongs to the peptidase C56 family. HSP31-like subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA17037.1; -; Genomic_DNA.
DR PIR; T40773; T40773.
DR RefSeq; NP_595267.1; NM_001021174.2.
DR AlphaFoldDB; O43084; -.
DR SMR; O43084; -.
DR BioGRID; 277807; 7.
DR STRING; 284812.O43084; -.
DR PaxDb; 4896-SPBC947-09-1; -.
DR EnsemblFungi; SPBC947.09.1; SPBC947.09.1:pep; SPBC947.09.
DR GeneID; 2541295; -.
DR KEGG; spo:SPBC947.09; -.
DR PomBase; SPBC947.09; hsp3103.
DR VEuPathDB; FungiDB:SPBC947.09; -.
DR eggNOG; ENOG502RZ3Y; Eukaryota.
DR HOGENOM; CLU_070319_1_0_1; -.
DR InParanoid; O43084; -.
DR OMA; WKRVETH; -.
DR PhylomeDB; O43084; -.
DR PRO; PR:O43084; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 CDD; cd03147; GATase1_Ydr533c_like; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR PANTHER; PTHR48094:SF11; GLUTATHIONE-INDEPENDENT GLYOXALASE HSP31-RELATED; 1.
DR PANTHER; PTHR48094; PROTEIN/NUCLEIC ACID DEGLYCASE DJ-1-RELATED; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Lyase; Reference proteome; Stress response.
FT CHAIN 1..261
FT /note="Probable glutathione-independent glyoxalase hsp3103"
FT /id="PRO_0000317305"
FT ACT_SITE 162
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 163
FT /evidence="ECO:0000250|UniProtKB:Q04432"
FT ACT_SITE 196
FT /evidence="ECO:0000250|UniProtKB:Q04432"
SQ SEQUENCE 261 AA; 28534 MW; 32C7801A9A5BA49A CRC64;
MPAKTRNVLI ACSDYYGPFY KDGENTGAFF LELLHPYLVF RDACFNVDIV TESGKIQFDD
HSVAGPAIDK GSKGEEFLSY DDHIASGPEL SKAEKYVLEN KDDMFWRIVQ NSKTADEVNP
DKYDIFFVAG GHATLFDFPK ATNLQKLGTS IYENGGVVAA VCHGPTLLPF MKRQTSDGSV
SIVCGKDVTA FDRVAEDKSK LMEALKKYNL EVLDDMLNDA GANFIKSPNP FGDFVIADGR
LVTGSNPASA TSTAKTALRV L
//
