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Protein

Hydroxyacylglutathione hydrolase, mitochondrial

Gene

Hagh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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 (Hagh)
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)DescriptionActionsGraphical viewLength
Metal bindingi103Zinc 1; via tele nitrogenBy similarity1
Metal bindingi105Zinc 1; via pros nitrogenBy similarity1
Metal bindingi107Zinc 2By similarity1
Metal bindingi108Zinc 2; via tele nitrogenBy similarity1
Metal bindingi159Zinc 1; via tele nitrogenBy similarity1
Metal bindingi183Zinc 1By similarity1
Metal bindingi183Zinc 2By similarity1
Metal bindingi222Zinc 2; via tele nitrogenBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • carbohydrate metabolic process Source: RGD
  • glutathione biosynthetic process Source: RGD
  • glutathione metabolic process Source: RGD
  • methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione Source: InterPro
  • spermatogenesis Source: RGD

Keywordsi

Molecular functionHydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.2.6. 5301.
SABIO-RKiO35952.
UniPathwayiUPA00619; UER00676.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacylglutathione hydrolase, mitochondrial (EC:3.1.2.6)
Alternative name(s):
Glyoxalase II
Short name:
Glx II
Round spermatid protein RSP29
Gene namesi
Name:Hagh
Synonyms:Rsp29
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2779. Hagh.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2262.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24MitochondrionSequence analysisAdd BLAST24
ChainiPRO_000019234425 – 309Hydroxyacylglutathione hydrolase, mitochondrialAdd BLAST285

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei90N6-acetyllysineBy similarity1
Modified residuei117N6-acetyllysineBy similarity1
Modified residuei230N6-acetyllysine; alternateBy similarity1
Modified residuei230N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO35952.
PRIDEiO35952.

PTM databases

iPTMnetiO35952.
PhosphoSitePlusiO35952.

Expressioni

Tissue specificityi

Strongly expressed in testis, skeletal muscle and heart. Weakly expressed in placenta, pancreas, spleen and peripheral blood leukocytes.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020192.

Chemistry databases

BindingDBiO35952.

Structurei

3D structure databases

SMRiO35952.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni192 – 194Substrate bindingBy similarity3
Regioni222 – 224Substrate bindingBy similarity3
Regioni298 – 301Substrate bindingBy similarity4

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0813. Eukaryota.
COG0491. LUCA.
HOGENOMiHOG000058041.
HOVERGENiHBG001152.
InParanoidiO35952.
KOiK01069.
PhylomeDBiO35952.

Family and domain databases

CDDicd07723. hydroxyacylglutathione_hydrola. 1 hit.
Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01374. Glyoxalase_2. 1 hit.
InterProiView protein in InterPro
IPR035680. Clx_II_MBL.
IPR032282. HAGH_C.
IPR017782. Hydroxyacylglutathione_Hdrlase.
IPR001279. Metallo-B-lactamas.
IPR036866. Metallo-hydrolase/OxRdtase.
PfamiView protein in Pfam
PF16123. HAGH_C. 1 hit.
PF00753. Lactamase_B. 1 hit.
PIRSFiPIRSF005457. Glx. 1 hit.
SMARTiView protein in SMART
SM00849. Lactamase_B. 1 hit.
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR03413. GSH_gloB. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: O35952-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVLGRGSLCL RSLSVLGAAC ARRGLGQALL GLSLCHTDFR KNLTVQQDMM
60 70 80 90 100
KIELLPALTD NYMYLIIDED TQEAAVVDPV QPQKVIETVK KHRVKLTTVL
110 120 130 140 150
TTHHHWDHAG GNEKLVKLEP GLKVYGGDDR IGALTHKVTH LSTLEVGSLS
160 170 180 190 200
VKCLSTPCHT SGHICYFVSK PGSSEPSAVF TGDTLFVAGC GKFYEGTADE
210 220 230 240 250
MYKALLEVLG RLPPDTKVIC GHEYTVNNLK FARHVEPGNT AVQEKLAWAK
260 270 280 290 300
EKNAIGEPTV PSTLAEEFTY NPFMRVKEKT VQQHAGETDP VTTMRAIRRE

KDQFKVPRD
Length:309
Mass (Da):34,109
Last modified:September 1, 2009 - v2
Checksum:i625AD975E86E9B72
GO
Isoform 2 (identifier: O35952-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Note: Produced by alternative splicing. Also produced by alternative initiation at Met-50 of isoform 1. Alternative initiation has been proven in human.
Show »
Length:260
Mass (Da):28,896
Checksum:i8384898771085C1C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145E → Q in FM068341 (Ref. 2) Curated1
Sequence conflicti145E → Q in AAH97301 (PubMed:15489334).Curated1
Sequence conflicti173S → N in FM068341 (Ref. 2) Curated1
Sequence conflicti219I → Y in AAH97301 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0379321 – 49Missing in isoform 2. 2 PublicationsAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97667 Genomic DNA. Translation: AAC39944.1.
FM068341 mRNA. No translation available.
BC097301 mRNA. Translation: AAH97301.1.
PIRiJC5826.
RefSeqiNP_203500.2. NM_033349.2.
UniGeneiRn.11048.

Genome annotation databases

GeneIDi24439.
KEGGirno:24439.
UCSCiRGD:2779. rat. [O35952-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiGLO2_RAT
AccessioniPrimary (citable) accession number: O35952
Secondary accession number(s): Q4V8M8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 1, 2009
Last modified: November 22, 2017
This is version 124 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Only one single gene encoding glyoxalase II has been identified in vertebrates. In yeast and higher plants, separate genes encode the cytosolic and mitochondrial forms of glyoxalase II.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families