Q54MR1 (GLO2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hydroxyacylglutathione hydrolase
EC=3.1.2.6

Alternative name(s):
Glyoxalase II
Short name=Glx II
Glyoxylase B1

Gene names

Name:	hagh
Synonyms:	gloB1
ORF Names:	DDB_G0285717

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	268 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

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

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from sequence or structural similarity. Source: dictyBase
Molecular function	hydroxyacylglutathione hydrolase activity Inferred from sequence or structural similarity. Source: dictyBase zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 268	268	Hydroxyacylglutathione hydrolase		PRO_0000328327
Regions
	Region	146 – 148	3	Substrate By similarity
	Region	176 – 178	3	Substrate By similarity
	Region	262 – 265	4	Substrate By similarity
Sites
	Metal binding	56	1	Zinc 1 By similarity
	Metal binding	58	1	Zinc 1 By similarity
	Metal binding	60	1	Zinc 2 By similarity
	Metal binding	61	1	Zinc 2 By similarity
	Metal binding	112	1	Zinc 1 By similarity
	Metal binding	137	1	Zinc 1 By similarity
	Metal binding	137	1	Zinc 2 By similarity
	Metal binding	176	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54MR1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 3F872B30F713E8CF	FASTA	268	30,406
	10 20 30 40 50 60 MKVQPVLVNK DNYSYLVIDE KNKVAIAIDP CEPNKVISSL SSISSDIKIN SVFTTHHHWD 70 80 90 100 110 120 HAGGNNLIKT IIKDINVYGR DERFEGITKK LENNEVLKIG SLKIKTLDAP AHTSSHVLYL 130 140 150 160 170 180 IEDENEPNQV KSLFTGDTLF IGGCGRLFEG NPEQMYNALY NVIGKLPDNT LVYVGHEYTL 190 200 210 220 230 240 KNLEFAKTLE SENENKELYN FYDQCKEKLA NGEFTVPSSI AQEKLINPFM RCHLPSIYNH 250 260 YLKENPNSIN PPSPIDVLGF IRSLKDKF

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000079 Genomic DNA. Translation: EAL64696.1.
RefSeq	XP_638232.1. XM_633140.1.
3D structure databases
HSSP	HSSP built from PDB template 1QH5 based on UniProtKB Q16775.
ProteinModelPortal	Q54MR1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54MR1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0230988; DDB0230988; DDB_G0285717.
GeneID	8625280.
GenomeReviews	Gene locus hagh in contig CM000153_GR.
KEGG	ddi:DDB_G0285717.
Organism-specific databases
dictyBase	DDB_G0285717. gloB1.
Phylogenomic databases
eggNOG	KOG0813.
GeneTree	EPrGT00060000009549.
HOGENOM	HBG753931.
OMA	GSLNVKC.
PhylomeDB	Q54MR1.
Family and domain databases
InterPro	IPR001279. Beta-lactamas-like. IPR017782. Hydroxyacylglutathione_Hdrlase. [Graphical view]
KO	K01069.
PANTHER	PTHR11935:SF7. PTHR11935:SF7. 1 hit.
Pfam	PF00753. Lactamase_B. 1 hit. [Graphical view]
SMART	SM00849. Lactamase_B. 1 hit. [Graphical view]
TIGRFAMs	TIGR03413. GSH_gloB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GLO2_DICDI

Accession

Primary (citable) accession number: Q54MR1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)