Q92MF8 (GLO2_RHIME) 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

Gene names

Name:	gloB
Ordered Locus Names:	R02664
ORF Names:	SMc00708

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	256 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: EC 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 – 256	256	Hydroxyacylglutathione hydrolase HAMAP MF_01374		PRO_0000309688
Sites
	Metal binding	57	1	Zinc 1 By similarity
	Metal binding	59	1	Zinc 1 By similarity
	Metal binding	61	1	Zinc 2 By similarity
	Metal binding	62	1	Zinc 2 By similarity
	Metal binding	115	1	Zinc 1 By similarity
	Metal binding	134	1	Zinc 1 By similarity
	Metal binding	134	1	Zinc 2 By similarity
	Metal binding	172	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92MF8 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 9BAB5A39C115E40D	FASTA	256	28,144
	10 20 30 40 50 60 MAALELDLFL CRTDNYGVLL HDRLSGATAS IDAPEERPIL DALERRGWQL THILTTHHHG 70 80 90 100 110 120 DHVAANASLK ERFGLTIIGP KNEASKIPGI DRTVGHGDRF DFAGHPVDVI ETPGHTSGHV 130 140 150 160 170 180 CYHLPEDKLL FAADTLFALG CGRLFEGTAD TMWQSLSRLM ALPDDTAIYF GHEYTLANAH 190 200 210 220 230 240 FAITVDPENS ALKERAAEIE ETRSDGGFTA PTTMGLEKRT NPFLRAGDPK IRALLGMEKA 250 SDAAVFAEIR KRKDNF

References

[1]	"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[2]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed: 11474104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591688 Genomic DNA. Translation: CAC47243.1.
RefSeq	NP_386770.1. NC_003047.1.
3D structure databases
HSSP	HSSP built from PDB template 1XM8 based on UniProtKB Q9SID3.
ProteinModelPortal	Q92MF8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1234339.
GenomeReviews	Gene locus R02664 in contig AL591688_GR.
KEGG	sme:SMc00708.
NMPDR	fig|266834.1.peg.3958.
PATRIC	23634865. VBISinMel96828_4164.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG753931.
OMA	FLCRTDN.
ProtClustDB	CLSK800959.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC00708-MONOMER.
Family and domain databases
HAMAP	MF_01374. Glyoxalase_2. [Tree]
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_RHIME

Accession

Primary (citable) accession number: Q92MF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program