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B0BZI8 (GLO2_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxyacylglutathione hydrolase

EC=3.1.2.6
Alternative name(s):
Glyoxalase II
Short name=Glx II
Gene names
Name:gloB
Ordered Locus Names:AM1_5788
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesAcaryochloris

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceInferred 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
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionhydroxyacylglutathione hydrolase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257Hydroxyacylglutathione hydrolase HAMAP MF_01374
PRO_1000087274

Sites

Metal binding541Zinc 1 By similarity
Metal binding561Zinc 1 By similarity
Metal binding581Zinc 2 By similarity
Metal binding591Zinc 2 By similarity
Metal binding1131Zinc 1 By similarity
Metal binding1371Zinc 1 By similarity
Metal binding1371Zinc 2 By similarity
Metal binding1751Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
B0BZI8 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 17620DDCCE37E58E

FASTA25729,006
        10         20         30         40         50         60 
MQIHRLPAFS DNYIFVLHDP GQNIAAVVDP ADPQPVLKKL AELGAELVAI FNTHHHSDHV 

        70         80         90        100        110        120 
GGNRTLLQAF PNTVVYGGEQ DRGRIPGQQH FLKEGDQVSF AHRRAEVYFV PGHTRAHIAY 

       130        140        150        160        170        180 
YFPPTTGEEW GELFCGDTLF AGGCGRLFEG TPAQMVDSLS KLRNLPETTR VWCAHEYTLK 

       190        200        210        220        230        240 
NLQFALTVDS DNSHLKNRFK QVQNARNLSQ PTVPSDIGLE KQTNPFLRWD QPHLIIHTKS 

       250 
NTPVQCFARL RGMKDQF 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW30733.1.
RefSeqYP_001520052.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0BZI8.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0BZI8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5684575.
GenomeReviewsGene locus AM1_5788 in contig CP000828_GR.
KEGGamr:AM1_5788.
PATRIC20625538. VBIAcaMar40141_5374.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG753931.
OMAIGCGRVF.
PhylomeDBB0BZI8.

Enzyme and pathway databases

BioCycAMAR329726:AM1_5788-MONOMER.

Family and domain databases

HAMAPMF_01374. Glyoxalase_2.
[Tree]
InterProIPR001279. Beta-lactamas-like.
IPR017782. Hydroxyacylglutathione_Hdrlase.
[Graphical view]
KOK01069.
PANTHERPTHR11935:SF7. PTHR11935:SF7. 1 hit.
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
TIGRFAMsTIGR03413. GSH_gloB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLO2_ACAM1
AccessionPrimary (citable) accession number: B0BZI8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families