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Protein

Probable hydroxyacylglutathione hydrolase C13B11.03c

Gene

SPCC13B11.03c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Pathwayi: methylglyoxal degradation

This protein is involved in step 2 of the subpathway that synthesizes (R)-lactate from methylglyoxal.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Lactoylglutathione lyase (glo1)
  2. Probable hydroxyacylglutathione hydrolase C824.07 (SPAC824.07), Probable hydroxyacylglutathione hydrolase C13B11.03c (SPCC13B11.03c)
This subpathway is part of the pathway methylglyoxal degradation, which is itself part of Secondary metabolite metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-lactate from methylglyoxal, the pathway methylglyoxal degradation and in Secondary metabolite metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Zinc 1; via tele nitrogenBy similarity
Metal bindingi65 – 651Zinc 1; via pros nitrogenBy similarity
Metal bindingi67 – 671Zinc 2By similarity
Metal bindingi68 – 681Zinc 2; via tele nitrogenBy similarity
Metal bindingi118 – 1181Zinc 1; via tele nitrogenBy similarity
Metal bindingi139 – 1391Zinc 1By similarity
Metal bindingi139 – 1391Zinc 2By similarity
Metal bindingi178 – 1781Zinc 2; via tele nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-70268. Pyruvate metabolism.
UniPathwayiUPA00619; UER00676.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable hydroxyacylglutathione hydrolase C13B11.03c (EC:3.1.2.6)
Alternative name(s):
Glyoxalase II
Short name:
Glx II
Gene namesi
ORF Names:SPCC13B11.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC13B11.03c.
PomBaseiSPCC13B11.03c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Probable hydroxyacylglutathione hydrolase C13B11.03cPRO_0000337690Add
BLAST

Interactioni

Protein-protein interaction databases

BioGridi275559. 11 interactions.
MINTiMINT-4682587.

Structurei

3D structure databases

ProteinModelPortaliO94250.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1503Substrate bindingBy similarity
Regioni178 – 1803Substrate bindingBy similarity
Regioni250 – 2534Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000058041.
InParanoidiO94250.
KOiK01069.
OMAiIDAPCHT.
OrthoDBiEOG7RRFJR.
PhylomeDBiO94250.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01374. Glyoxalase_2.
InterProiIPR032282. HAGH_C.
IPR017782. Hydroxyacylglutathione_Hdrlase.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF16123. HAGH_C. 1 hit.
PF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR03413. GSH_gloB. 1 hit.

Sequencei

Sequence statusi: Complete.

O94250-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFQILPIPM WVGTQDNYAY LLLCEETRQA AIVDPAEVNV VMPILKKKLK
60 70 80 90 100
NKEIDLQAIL TTHHHADHSG GNLNLKKEFP HVTIYGGSDQ NGVSHVLQDK
110 120 130 140 150
ETLRIGNVQI EALHTPCHTR DSICFYAHSS NEHAVFTGDT LFNAGCGRFF
160 170 180 190 200
EGTAAEMHIA LNAVLSSLPN NTVIYPGHEY TKSNVKFASK HLQSEALNHL
210 220 230 240 250
EGLCNHNQFI AGHITMGQEK QFNPFMRVTD PELQKHLGLN DPIKVMDELR

TLKNQG
Length:256
Mass (Da):28,629
Last modified:May 1, 1999 - v1
Checksum:i4605904BE2CDF006
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA21784.1.
PIRiT40964.
RefSeqiNP_588246.1. NM_001023236.2.

Genome annotation databases

EnsemblFungiiSPCC13B11.03c.1; SPCC13B11.03c.1:pep; SPCC13B11.03c.
GeneIDi2538985.
KEGGispo:SPCC13B11.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA21784.1.
PIRiT40964.
RefSeqiNP_588246.1. NM_001023236.2.

3D structure databases

ProteinModelPortaliO94250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275559. 11 interactions.
MINTiMINT-4682587.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC13B11.03c.1; SPCC13B11.03c.1:pep; SPCC13B11.03c.
GeneIDi2538985.
KEGGispo:SPCC13B11.03c.

Organism-specific databases

EuPathDBiFungiDB:SPCC13B11.03c.
PomBaseiSPCC13B11.03c.

Phylogenomic databases

HOGENOMiHOG000058041.
InParanoidiO94250.
KOiK01069.
OMAiIDAPCHT.
OrthoDBiEOG7RRFJR.
PhylomeDBiO94250.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00676.
ReactomeiR-SPO-70268. Pyruvate metabolism.

Miscellaneous databases

PROiO94250.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01374. Glyoxalase_2.
InterProiIPR032282. HAGH_C.
IPR017782. Hydroxyacylglutathione_Hdrlase.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF16123. HAGH_C. 1 hit.
PF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR03413. GSH_gloB. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLO22_SCHPO
AccessioniPrimary (citable) accession number: O94250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.