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Protein

Hydroxyacylglutathione hydrolase, mitochondrial

Gene

Hagh

Organism
Mus musculus (Mouse)
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), 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi103 – 1031Zinc 1; via tele nitrogenBy similarity
Metal bindingi105 – 1051Zinc 1; via pros nitrogenBy similarity
Metal bindingi107 – 1071Zinc 2By similarity
Metal bindingi108 – 1081Zinc 2; via tele nitrogenBy similarity
Metal bindingi159 – 1591Zinc 1; via tele nitrogenBy similarity
Metal bindingi183 – 1831Zinc 1By similarity
Metal bindingi183 – 1831Zinc 2By similarity
Metal bindingi222 – 2221Zinc 2; via tele nitrogenBy similarity

GO - Molecular functioni

  • hydroxyacylglutathione hydrolase activity Source: MGI
  • 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

SABIO-RKQ99KB8.
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
Gene namesi
Name:Hagh
Synonyms:Glo2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95745. Hagh.

Subcellular locationi

Isoform 1 :
  • Mitochondrion matrix By similarity
Isoform 2 :
  • Cytoplasm By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrial matrix Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionSequence analysisAdd
BLAST
Chaini25 – 309285Hydroxyacylglutathione hydrolase, mitochondrialPRO_0000192343Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901N6-acetyllysineCombined sources
Modified residuei117 – 1171N6-acetyllysineCombined sources
Modified residuei230 – 2301N6-acetyllysine; alternateBy similarity
Modified residuei230 – 2301N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99KB8.
MaxQBiQ99KB8.
PaxDbiQ99KB8.
PRIDEiQ99KB8.

2D gel databases

REPRODUCTION-2DPAGEQ99KB8.

PTM databases

iPTMnetiQ99KB8.
PhosphoSiteiQ99KB8.

Expressioni

Gene expression databases

BgeeiQ99KB8.
CleanExiMM_HAGH.

Interactioni

Protein-protein interaction databases

IntActiQ99KB8. 5 interactions.
MINTiMINT-1855726.
STRINGi10090.ENSMUSP00000113051.

Structurei

3D structure databases

ProteinModelPortaliQ99KB8.
SMRiQ99KB8. Positions 50-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 1943Substrate bindingBy similarity
Regioni222 – 2243Substrate bindingBy similarity
Regioni298 – 3014Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0813. Eukaryota.
COG0491. LUCA.
HOGENOMiHOG000058041.
HOVERGENiHBG001152.
InParanoidiQ99KB8.
KOiK01069.
PhylomeDBiQ99KB8.

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]
PIRSFiPIRSF005457. Glx. 1 hit.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
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: Q99KB8-1) [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 RSLSALGATC ARRGLGQALL GLSLCHSDFR KNLTVQQDIM
60 70 80 90 100
KVELLPALTD NYMYLIIDED TQEAAIVDPV QPQKVIEAAK KHHVKLTTVL
110 120 130 140 150
TTHHHWDHAG GNEKLVKLEP GLKVYGGDDR IGALTHKVTH LSTLQVGSLS
160 170 180 190 200
VKCLSTPCHT SGHICYFVSK PGSSEPSAVF TGDTLFVAGC GKFYEGTADE
210 220 230 240 250
MYKALLEVLG RLPPDTKVYC GHEYTVNNLK FARHVEPGNA AIQEKLAWAK
260 270 280 290 300
EKYAIGEPTV PSTLAEEFTY NPFMRVKEKT VQQHAGETDP VTTMRAIRRE

KDQFKVPRD
Length:309
Mass (Da):34,084
Last modified:September 1, 2009 - v2
Checksum:iAC2C17D7AB6E4FBA
GO
Isoform 2 (identifier: Q99KB8-2) [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):28,901
Checksum:i94FD38ACD64684BF
GO

Sequence cautioni

The sequence AAH04749.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH19817.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE27615.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE29657.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE30223.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE31462.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931H → R in BAE27615 (PubMed:16141072).Curated
Sequence conflicti93 – 931H → R in BAE29657 (PubMed:16141072).Curated
Sequence conflicti93 – 931H → R in BAE30223 (PubMed:16141072).Curated
Sequence conflicti93 – 931H → R in BAE31462 (PubMed:16141072).Curated
Sequence conflicti93 – 931H → R in BAE38377 (PubMed:16141072).Curated
Sequence conflicti147 – 1471G → E in BAE38377 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949Missing in isoform 2. 2 PublicationsVSP_037931Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147022 mRNA. Translation: BAE27615.1. Different initiation.
AK150557 mRNA. Translation: BAE29657.1. Different initiation.
AK151231 mRNA. Translation: BAE30223.1. Different initiation.
AK152742 mRNA. Translation: BAE31462.1. Different initiation.
AK165777 mRNA. Translation: BAE38377.1.
BC004749 mRNA. Translation: AAH04749.1. Different initiation.
BC019817 mRNA. Translation: AAH19817.1. Different initiation.
CCDSiCCDS28499.2. [Q99KB8-1]
CCDS50021.1. [Q99KB8-2]
RefSeqiNP_001153098.1. NM_001159626.1.
NP_077246.2. NM_024284.2.
XP_006523723.1. XM_006523660.2.
XP_006523724.1. XM_006523661.1.
UniGeneiMm.43784.

Genome annotation databases

GeneIDi14651.
KEGGimmu:14651.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147022 mRNA. Translation: BAE27615.1. Different initiation.
AK150557 mRNA. Translation: BAE29657.1. Different initiation.
AK151231 mRNA. Translation: BAE30223.1. Different initiation.
AK152742 mRNA. Translation: BAE31462.1. Different initiation.
AK165777 mRNA. Translation: BAE38377.1.
BC004749 mRNA. Translation: AAH04749.1. Different initiation.
BC019817 mRNA. Translation: AAH19817.1. Different initiation.
CCDSiCCDS28499.2. [Q99KB8-1]
CCDS50021.1. [Q99KB8-2]
RefSeqiNP_001153098.1. NM_001159626.1.
NP_077246.2. NM_024284.2.
XP_006523723.1. XM_006523660.2.
XP_006523724.1. XM_006523661.1.
UniGeneiMm.43784.

3D structure databases

ProteinModelPortaliQ99KB8.
SMRiQ99KB8. Positions 50-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99KB8. 5 interactions.
MINTiMINT-1855726.
STRINGi10090.ENSMUSP00000113051.

PTM databases

iPTMnetiQ99KB8.
PhosphoSiteiQ99KB8.

2D gel databases

REPRODUCTION-2DPAGEQ99KB8.

Proteomic databases

EPDiQ99KB8.
MaxQBiQ99KB8.
PaxDbiQ99KB8.
PRIDEiQ99KB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14651.
KEGGimmu:14651.

Organism-specific databases

CTDi3029.
MGIiMGI:95745. Hagh.

Phylogenomic databases

eggNOGiKOG0813. Eukaryota.
COG0491. LUCA.
HOGENOMiHOG000058041.
HOVERGENiHBG001152.
InParanoidiQ99KB8.
KOiK01069.
PhylomeDBiQ99KB8.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00676.
SABIO-RKQ99KB8.

Miscellaneous databases

PROiQ99KB8.
SOURCEiSearch...

Gene expression databases

BgeeiQ99KB8.
CleanExiMM_HAGH.

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]
PIRSFiPIRSF005457. Glx. 1 hit.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR03413. GSH_gloB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Cerebellum and Heart.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: FVB/N.
    Tissue: Liver and Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90 AND LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGLO2_MOUSE
AccessioniPrimary (citable) accession number: Q99KB8
Secondary accession number(s): Q3TMR4, Q3UCF6, Q8WUR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: September 1, 2009
Last modified: June 8, 2016
This is version 121 of the entry and version 2 of the sequence. [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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.