Reviewed, UniProtKB/Swiss-Prot Q2N9P7 (GLO2_ERYLH)

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:	gloB
Ordered Locus Names:	ELI_07510

Organism

Erythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]

Taxonomic identifier

314225 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Erythrobacteraceae › Erythrobacter

Protein attributes

Sequence length	251 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. HAMAP MF_01374
Catalytic activity	S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate. HAMAP MF_01374
Cofactor	Binds 2 zinc ions per subunit By similarity. HAMAP MF_01374
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. HAMAP MF_01374
Subunit structure	Monomer By similarity. HAMAP MF_01374
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
Gene Ontology (GO)
Molecular function	hydroxyacylglutathione hydrolase activity Inferred from electronic annotation. Source: HAMAP 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 – 251	251	Hydroxyacylglutathione hydrolase HAMAP MF_01374		PRO_1000068216
Sites
	Metal binding	55	1	Zinc 1 By similarity
	Metal binding	57	1	Zinc 1 By similarity
	Metal binding	59	1	Zinc 2 By similarity
	Metal binding	60	1	Zinc 2 By similarity
	Metal binding	112	1	Zinc 1 By similarity
	Metal binding	131	1	Zinc 1 By similarity
	Metal binding	131	1	Zinc 2 By similarity
	Metal binding	169	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2N9P7-1 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: FE9D1B7ECA11C9CD	FASTA	251	27,482
	10 20 30 40 50 60 MLEIHQFPCL SDNYGFLLHD PDSGETAAID TPDGKEYLKQ AKAKGWTITH IWNTHWHPDH 70 80 90 100 110 120 AGGNKDIVEA TGAKVIAPQE VEKLSGIDRV VGHGDTVDIG DFTADVIDVS GHTNGHIAYH 130 140 150 160 170 180 LPEAGIAFVG DSVFALGCGR MFEGEPKQFW DSLSRIKALP PETMLYCAHE YTAANARFAV 190 200 210 220 230 240 HADPENDALV AYVEEITAKR ERDEPTVPTQ LKRELATNPF LRADDPALVA KWGGDAPHET 250 FAALRAGKDN F

References

[1]	Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravits S., Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000157 Genomic DNA. Translation: ABC63594.1.
RefSeq	YP_458391.1.
3D structure databases
SMR	Q2N9P7. Positions 2-251.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2N9P7.
Genome annotation databases
GeneID	3869572.
GenomeReviews	Gene locus ELI_07510 in contig CP000157_GR.
KEGG	eli:ELI_07510.
NMPDR	fig|314225.3.peg.1541.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0491.
HOGENOM	HBG753931.
OMA	WCAHEYT.
PhylomeDB	Q2N9P7.
Enzyme and pathway databases
BioCyc	ELIT314225:ELI_07510-MONOMER.
Family and domain databases
HAMAP	MF_01374. Glyoxalase_2. [Tree]
InterPro	IPR001279. Blactmase-like. IPR017782. Hydroxyacylglutathione_Hdrlase. [Graphical view]
SMART	SM00849. Lactamase_B. 1 hit. [Graphical view]
TIGRFAMs	TIGR03413. GSH_gloB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GLO2_ERYLH

Accession

Primary (citable) accession number: Q2N9P7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 7, 2006
Last modified:	February 9, 2010
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)