Q9PBI4 (GLO2_XYLFA) 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:	XF_2160

Organism

Xylella fastidiosa [Complete proteome] [HAMAP]

Taxonomic identifier

2371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length	258 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 – 258	258	Hydroxyacylglutathione hydrolase HAMAP MF_01374		PRO_1000068234
Sites
	Metal binding	52	1	Zinc 1 By similarity
	Metal binding	54	1	Zinc 1 By similarity
	Metal binding	56	1	Zinc 2 By similarity
	Metal binding	57	1	Zinc 2 By similarity
	Metal binding	109	1	Zinc 1 By similarity
	Metal binding	126	1	Zinc 1 By similarity
	Metal binding	126	1	Zinc 2 By similarity
	Metal binding	164	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PBI4 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 7FBE2FF769B24B58	FASTA	258	28,548
	10 20 30 40 50 60 MRLTPLPAFD NNYIWTLIAP DGRAIIVDPG QALPILEAHS KGLIPTAILL THHHADHIGG 70 80 90 100 110 120 VPELLERWPT LPIYAPHDTR IALNYHRIGE GDSLNILGLR FQVIHTPGHT HSHLTFIGND 130 140 150 160 170 180 LLFCGDTLFS LGCGQIFEGT PTQMLASLQR LAALPIQTRV CCGHEYTLSN AAFALHVDPT 190 200 210 220 230 240 NTALQKRRQQ ANAMRLANLP TLPISLESEL NTNPFLRTAA PTIHAATATH LQRTPIDEVE 250 VFATLRHWKN NFPIKNIP

References

[1]

"The genome sequence of the plant pathogen Xylella fastidiosa." Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C. Nature 406:151-159(2000) [PubMed: 10910347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9a5c.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003849 Genomic DNA. Translation: AAF84959.1.
PIR	H82591.
RefSeq	NP_299439.1. NC_002488.3.
3D structure databases
HSSP	HSSP built from PDB template 1XM8 based on UniProtKB Q9SID3.
ProteinModelPortal	Q9PBI4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1127713.
GenomeReviews	Gene locus XF_2160 in contig AE003849_GR.
KEGG	xfa:XF2160.
NMPDR	fig|160492.1.peg.2146.
PATRIC	24134562. VBIXylFas578_2301.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG753931.
OMA	FLCRTDN.
ProtClustDB	CLSK497122.
Enzyme and pathway databases
BioCyc	XFAS160492:XF2160-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_XYLFA

Accession

Primary (citable) accession number: Q9PBI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 1, 2000
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