Reviewed, UniProtKB/Swiss-Prot Q16775 (GLO2_HUMAN)

Names and origin

Protein names

Recommended name:
    Hydroxyacylglutathione hydrolase
    EC=3.1.2.6
Alternative name(s):
    Glyoxalase II
      Short name=Glx II

Gene names

Name:	HAGH
Synonyms:	GLO2, HAGH1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic activity	S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate.
Cofactor	Binds 2 zinc ions per subunit.
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; D-lactate from methylglyoxal: step 2/2.
Subunit structure	Monomer.
Sequence similarities	Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Molecular function	hydroxyacylglutathione hydrolase activity Ref.1 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 260

260

Hydroxyacylglutathione hydrolase

PRO_0000192342

Regions

Region

143 – 145

3

Substrate

Region

173 – 175

3

Substrate

Region

249 – 252

4

Substrate

Sites

Metal binding

54

1

Zinc 1

Metal binding

56

1

Zinc 1

Metal binding

58

1

Zinc 2

Metal binding

59

1

Zinc 2

Metal binding

110

1

Zinc 1

Metal binding

134

1

Zinc 1

Metal binding

134

1

Zinc 2

Metal binding

173

1

Zinc 2

Secondary structure

1

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260

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Turn

9 – 11

3

Beta strand

12 – 19

8

Turn

20 – 23

4

Beta strand

24 – 29

6

Helix

33 – 43

11

Beta strand

46 – 51

6

Helix

57 – 60

4

Helix

63 – 69

7

Beta strand

74 – 78

5

Beta strand

86 – 88

3

Beta strand

94 – 97

4

Beta strand

100 – 106

7

Beta strand

109 – 111

3

Beta strand

115 – 120

6

Beta strand

122 – 126

5

Beta strand

129 – 133

5

Helix

149 – 157

9

Turn

158 – 162

5

Beta strand

168 – 173

6

Helix

176 – 186

11

Helix

191 – 206

16

Helix

215 – 221

7

Turn

223 – 228

6

Helix

230 – 236

7

Helix

241 – 254

14

Sequences

	Sequence		Length	Mass (Da)
	Q16775-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4C3DEC87FB27A1D2	FASTA	260	28,860
	10 20 30 40 50 60 MKVEVLPALT DNYMYLVIDD ETKEAAIVDP VQPQKVVDAA RKHGVKLTTV LTTHHHWDHA 70 80 90 100 110 120 GGNEKLVKLE SGLKVYGGDD RIGALTHKIT HLSTLQVGSL NVKCLATPCH TSGHICYFVS 130 140 150 160 170 180 KPGGSEPPAV FTGDTLFVAG CGKFYEGTAD EMCKALLEVL GRLPPDTRVY CGHEYTINNL 190 200 210 220 230 240 KFARHVEPGN AAIREKLAWA KEKYSIGEPT VPSTLAEEFT YNPFMRVREK TVQQHAGETD 250 260 PVTTMRAVRR EKDQFKMPRD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, heterologous expression, and characterization of human glyoxalase II." Ridderstroem M., Saccucci F., Hellman U., Bergman T., Principato G., Mannervik B. J. Biol. Chem. 271:319-323(1996) [PubMed: 8550579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16." Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R. Hum. Mol. Genet. 10:339-352(2001) [PubMed: 11157797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix and Uterus.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue." Cameron A.D., Ridderstroem M., Olin B., Mannervik B. Structure 7:1067-1077(1999) [PubMed: 10508780] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND ZINC IONS. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X90999 mRNA. Translation: CAA62483.1.
AE006639 Genomic DNA. Translation: AAK61294.1.
AL031722 Genomic DNA. No translation available.
BC000840 mRNA. Translation: AAH00840.1.
BC002627 mRNA. Translation: AAH02627.2. Different initiation.

IPI

IPI00745553.

RefSeq

NP_001035517.1.
NP_005317.2.

UniGene

Hs.157394
Hs.513265

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QH3	X-ray	1.90	A/B	1-260	[»]
1QH5	X-ray	1.45	A/B	1-260	[»]
2F50	model	-	A	15-177	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q16775.

Proteomic databases

PRIDE

Q16775.

Genome annotation databases

Ensembl

ENSG00000063854. Homo sapiens. [Contig view]

GeneID

3029.

KEGG

hsa:3029.

NMPDR

fig|9606.3.peg.11513.

Organism-specific databases

GeneCards

GC16M001799.

H-InvDB

HIX0012697.

HGNC

HGNC:4805. HAGH.

MIM

138760. gene+phenotype.

PharmGKB

PA29179.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q16775.

HOVERGEN

Q16775.

Enzyme and pathway databases

BRENDA

3.1.2.6. 247.

Gene expression databases

ArrayExpress

Q16775.

Bgee

Q16775.

CleanEx

HS_HAGH.

GermOnline

ENSG00000063854. Homo sapiens.

Family and domain databases

InterPro

IPR001279. Blactmase-like.
IPR017782. Hydroxyacylglutathione_Hdrlase.
[Graphical view]

Pfam

PF00753. Lactamase_B. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03413. GSH_gloB. 1 hit.

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

11990.

SOURCE

Search...

Entry information

Entry name

GLO2_HUMAN

Accession

Primary (citable) accession number: Q16775

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)