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Protein

Hydroxyacylglutathione hydrolase, cytoplasmic isozyme

Gene

GLO2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

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. Hydroxyacylglutathione hydrolase, mitochondrial (GLO4), Hydroxyacylglutathione hydrolase, cytoplasmic isozyme (GLO2)
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 bindingi59 – 591Zinc 1; via tele nitrogenBy similarity
Metal bindingi61 – 611Zinc 1; via pros nitrogenBy similarity
Metal bindingi63 – 631Zinc 2By similarity
Metal bindingi64 – 641Zinc 2; via tele nitrogenBy similarity
Metal bindingi121 – 1211Zinc 1; via tele nitrogenBy similarity
Metal bindingi144 – 1441Zinc 1By similarity
Metal bindingi144 – 1441Zinc 2By similarity
Binding sitei153 – 1531SubstrateBy similarity
Metal bindingi188 – 1881Zinc 2; via tele nitrogenBy similarity

GO - Molecular functioni

  • hydroxyacylglutathione hydrolase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-625.
YEAST:YDR272W-MONOMER.
ReactomeiR-SCE-70268. Pyruvate metabolism.
SABIO-RKQ05584.
UniPathwayiUPA00619; UER00676.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacylglutathione hydrolase, cytoplasmic isozyme (EC:3.1.2.6)
Alternative name(s):
Glyoxalase II
Short name:
Glx II
Gene namesi
Name:GLO2
Ordered Locus Names:YDR272W
ORF Names:D9954.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR272W.
SGDiS000002680. GLO2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274Hydroxyacylglutathione hydrolase, cytoplasmic isozymePRO_0000192346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ05584.

PTM databases

iPTMnetiQ05584.

Interactioni

Protein-protein interaction databases

BioGridi32326. 17 interactions.
IntActiQ05584. 1 interaction.
MINTiMINT-660365.

Structurei

3D structure databases

ProteinModelPortaliQ05584.
SMRiQ05584. Positions 16-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 1903Substrate bindingBy similarity
Regioni268 – 2714Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00530000063033.
HOGENOMiHOG000058041.
InParanoidiQ05584.
KOiK01069.
OMAiLCIRTPC.
OrthoDBiEOG7RRFJR.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR032282. HAGH_C.
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.

Sequencei

Sequence statusi: Complete.

Q05584-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVKSIKMRW ESGGVNYCYL LSDSKNKKSW LIDPAEPPEV LPELTEDEKI
60 70 80 90 100
SVEAIVNTHH HYDHADGNAD ILKYLKEKNP TSKVEVIGGS KDCPKVTIIP
110 120 130 140 150
ENLKKLHLGD LEITCIRTPC HTRDSICYYV KDPTTDERCI FTGDTLFTAG
160 170 180 190 200
CGRFFEGTGE EMDIALNNSI LETVGRQNWS KTRVYPGHEY TSDNVKFVRK
210 220 230 240 250
IYPQVGENKA LDELEQFCSK HEVTAGRFTL KDEVEFNPFM RLEDPKVQKA
260 270
AGDTNNSWDR AQIMDKLRAM KNRM
Length:274
Mass (Da):31,327
Last modified:November 1, 1996 - v1
Checksum:i6CD7AB9F0A9399EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221E → K in AAS56065 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10292 Genomic DNA. Translation: CAA71335.1.
U51030 Genomic DNA. Translation: AAB64450.1.
AY557739 Genomic DNA. Translation: AAS56065.1.
BK006938 Genomic DNA. Translation: DAA12114.1.
PIRiS70130.
RefSeqiNP_010558.3. NM_001180580.3.

Genome annotation databases

EnsemblFungiiYDR272W; YDR272W; YDR272W.
GeneIDi851865.
KEGGisce:YDR272W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10292 Genomic DNA. Translation: CAA71335.1.
U51030 Genomic DNA. Translation: AAB64450.1.
AY557739 Genomic DNA. Translation: AAS56065.1.
BK006938 Genomic DNA. Translation: DAA12114.1.
PIRiS70130.
RefSeqiNP_010558.3. NM_001180580.3.

3D structure databases

ProteinModelPortaliQ05584.
SMRiQ05584. Positions 16-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32326. 17 interactions.
IntActiQ05584. 1 interaction.
MINTiMINT-660365.

PTM databases

iPTMnetiQ05584.

Proteomic databases

MaxQBiQ05584.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR272W; YDR272W; YDR272W.
GeneIDi851865.
KEGGisce:YDR272W.

Organism-specific databases

EuPathDBiFungiDB:YDR272W.
SGDiS000002680. GLO2.

Phylogenomic databases

GeneTreeiENSGT00530000063033.
HOGENOMiHOG000058041.
InParanoidiQ05584.
KOiK01069.
OMAiLCIRTPC.
OrthoDBiEOG7RRFJR.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00676.
BioCyciMetaCyc:MONOMER-625.
YEAST:YDR272W-MONOMER.
ReactomeiR-SCE-70268. Pyruvate metabolism.
SABIO-RKQ05584.

Miscellaneous databases

PROiQ05584.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR032282. HAGH_C.
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and phenotypic analysis of two glyoxalase II encoding genes from Saccharomyces cerevisiae, GLO2 and GLO4, and intracellular localization of the corresponding proteins."
    Bito A., Haider M., Hadler I., Breitenbach M.
    J. Biol. Chem. 272:21509-21519(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 200060 / W303.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLO2_YEAST
AccessioniPrimary (citable) accession number: Q05584
Secondary accession number(s): D6VSQ4, E9P8T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 13700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.