B8D941 (B8D941_BUCA5) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Hydroxyacylglutathione hydrolase HAMAP-Rule MF_01374
EC=3.1.2.6 HAMAP-Rule MF_01374

Alternative name(s):
Glyoxalase II HAMAP-Rule MF_01374

Gene names

Name:	gloB HAMAP-Rule MF_01374 EMBL ACL30612.1
Ordered Locus Names:	BUAP5A_242

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A) [Complete proteome] [HAMAP]

Taxonomic identifier

563178 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Acyrthosiphon pisum) › Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)

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-Rule MF_01374 SAAS SAAS017782
Catalytic activity	S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate. HAMAP-Rule MF_01374 SAAS SAAS017782
Cofactor	Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_01374 SAAS SAAS017782
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. HAMAP-Rule MF_01374
Subunit structure	Monomer By similarity. HAMAP-Rule MF_01374 SAAS SAAS017782
Sequence similarities	Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family. HAMAP-Rule MF_01374

Ontologies

Keywords
Ligand	Metal-binding HAMAP-Rule MF_01374 SAAS SAAS017782 Zinc HAMAP-Rule MF_01374 SAAS SAAS017782
Molecular function	Hydrolase HAMAP-Rule MF_01374 SAAS SAAS017782 EMBL ACL30612.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glutathione biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	hydroxyacylglutathione hydrolase activity Inferred from electronic annotation. Source: HAMAP 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
Sites
	Metal binding	53	1	Zinc 1 By similarity HAMAP-Rule MF_01374
	Metal binding	55	1	Zinc 1 By similarity HAMAP-Rule MF_01374
	Metal binding	57	1	Zinc 2 By similarity HAMAP-Rule MF_01374
	Metal binding	58	1	Zinc 2 By similarity HAMAP-Rule MF_01374
	Metal binding	110	1	Zinc 1 By similarity HAMAP-Rule MF_01374
	Metal binding	127	1	Zinc 1 By similarity HAMAP-Rule MF_01374
	Metal binding	127	1	Zinc 2 By similarity HAMAP-Rule MF_01374
	Metal binding	165	1	Zinc 2 By similarity HAMAP-Rule MF_01374

Sequences

	Sequence		Length	Mass (Da)
	B8D941 [UniParc]. Last modified March 3, 2009. Version 1. Checksum: D023179CAFF715CF	FASTA	251	29,156
	10 20 30 40 50 60 MILKKISILS DNYVWVLLNT SGSCIIIDPG LSEPIIQEIE RKKWRLRAIL LTHNHIDHTG 70 80 90 100 110 120 GTRKIIEYFP KISVFGPKET RQHGVNKIVS HGDRIILLDK IFYVFFTPGH TSGHVSYYSQ 130 140 150 160 170 180 PYIFCGDTLF SAGCGRVFKN KHLEMYRSIK IISSLPDSTL LCCSHEYTLS NLQFSMFILP 190 200 210 220 230 240 NDNFIKLYLK KIEIKLKLGQ SSLPSYIFFE KKINLFLRTN DNYVKKSIGL KSTCTDFEVF 250 KRLRLKKDFW S

References

[1]	"The dynamics and time scale of ongoing genomic erosion in symbiotic bacteria." Moran N.A., McLaughlin H.J., Sorek R. Science 323:379-382(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 5A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001161 Genomic DNA. Translation: ACL30612.1.
RefSeq	YP_002468000.1. NC_011833.1.
3D structure databases
ProteinModelPortal	B8D941.
ModBase	Search...
Protein-protein interaction databases
STRING	107806.BU246.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACL30612; ACL30612; BUAP5A_242.
GeneID	7262507.
KEGG	bap:BUAP5A_242.
PATRIC	21242729. VBIBucAph51993_0243.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0491.
HOGENOM	HOG000058041.
KO	K01069.
OMA	LTHHHQD.
ProtClustDB	CLSK315822.
Enzyme and pathway databases
BioCyc	BAPH563178:GHDF-241-MONOMER.
UniPathway	UPA00619; UER00676.
Family and domain databases
HAMAP	MF_01374. Glyoxalase_2.
InterPro	IPR001279. Beta-lactamas-like. IPR017782. Hydroxyacylglutathione_Hdrlase. [Graphical view]
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

B8D941_BUCA5

Accession

Primary (citable) accession number: B8D941

Entry history

Integrated into UniProtKB/TrEMBL:	March 3, 2009
Last sequence update:	March 3, 2009
Last modified:	May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)