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O94250 (GLO22_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable hydroxyacylglutathione hydrolase C13B11.03c
EC=3.1.2.6
Alternative name(s):
Glyoxalase II
Short name=Glx II
Gene names
ORF Names:SPCC13B11.03c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid By similarity.

Catalytic activity

S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.

Subcellular location

Cytoplasm. Nucleus Ref.2.

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Probable hydroxyacylglutathione hydrolase C13B11.03c
PRO_0000337690

Regions

Region178 – 1803Substrate By similarity
Region250 – 2534Substrate By similarity

Sites

Metal binding631Zinc 1 By similarity
Metal binding651Zinc 1 By similarity
Metal binding671Zinc 2 By similarity
Metal binding681Zinc 2 By similarity
Metal binding1181Zinc 1 By similarity
Metal binding1391Zinc 1 By similarity
Metal binding1391Zinc 2 By similarity
Metal binding1781Zinc 2 By similarity
Binding site1481Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O94250 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4605904BE2CDF006

FASTA25628,629
        10         20         30         40         50         60 
MSFQILPIPM WVGTQDNYAY LLLCEETRQA AIVDPAEVNV VMPILKKKLK NKEIDLQAIL 

        70         80         90        100        110        120 
TTHHHADHSG GNLNLKKEFP HVTIYGGSDQ NGVSHVLQDK ETLRIGNVQI EALHTPCHTR 

       130        140        150        160        170        180 
DSICFYAHSS NEHAVFTGDT LFNAGCGRFF EGTAAEMHIA LNAVLSSLPN NTVIYPGHEY 

       190        200        210        220        230        240 
TKSNVKFASK HLQSEALNHL EGLCNHNQFI AGHITMGQEK QFNPFMRVTD PELQKHLGLN 

       250 
DPIKVMDELR TLKNQG

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329672 Genomic DNA. Translation: CAA21784.1.
PIRT40964.
RefSeqNP_588246.1. NM_001023236.1.

3D structure databases

HSSPHSSP built from PDB template 1QH5 based on UniProtKB Q16775.
ProteinModelPortalO94250.
ModBaseSearch...

Protein-protein interaction databases

STRINGO94250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC13B11.03c.1; SPCC13B11.03c.1:pep; SPCC13B11.03c.
GeneID2538985.
KEGGspo:SPCC13B11.03c.
NMPDRfig|4896.1.peg.584.

Organism-specific databases

GeneDB_SpombeSPCC13B11.03c.

Phylogenomic databases

eggNOGfuNOG07131.
GeneTreeEFGT00050000003859.
HOGENOMHBG753931.
OMAGSLNVKC.
OrthoDBEOG4PK5J1.

Gene expression databases

ArrayExpressO94250.

Family and domain databases

InterProIPR001279. Beta-lactamas-like.
IPR017782. Hydroxyacylglutathione_Hdrlase.
[Graphical view]
KOK01069.
PANTHERPTHR11935:SF7. PTHR11935:SF7. 1 hit.
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
TIGRFAMsTIGR03413. GSH_gloB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLO22_SCHPO
AccessionPrimary (citable) accession number: O94250
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 1, 1999
Last modified: December 14, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents