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Q9AAS7 (Q9AAS7_CAUCR) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Hydroxyacylglutathione hydrolase HAMAP MF_01374

EC=3.1.2.6 HAMAP MF_01374
Alternative name(s):
Glyoxalase II HAMAP MF_01374
Gene names
Name:gloB HAMAP MF_01374
Ordered Locus Names:CC_0519
OrganismCaulobacter crescentus (Caulobacter vibrioides)
Taxonomic identifier155892 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length249 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 SAAS SAAS017782

Catalytic activity

S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate. HAMAP MF_01374 SAAS SAAS017782

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_01374 SAAS SAAS017782

Pathway

Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. HAMAP MF_01374

Subunit structure

Monomer By similarity. HAMAP MF_01374 SAAS SAAS017782

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family. HAMAP MF_01374

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding561Zinc 1 By similarity HAMAP MF_01374
Metal binding581Zinc 1 By similarity HAMAP MF_01374
Metal binding601Zinc 2 By similarity HAMAP MF_01374
Metal binding611Zinc 2 By similarity HAMAP MF_01374
Metal binding1131Zinc 1 By similarity HAMAP MF_01374
Metal binding1321Zinc 1 By similarity HAMAP MF_01374
Metal binding1321Zinc 2 By similarity HAMAP MF_01374
Metal binding1701Zinc 2 By similarity HAMAP MF_01374

Sequences

Sequence LengthMass (Da)Tools
Q9AAS7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 991305F59AF21E61

FASTA24926,499
        10         20         30         40         50         60 
MALTVHQFRC LSDNYGFLVR DEASGKVATI DTPDAGAILA ELAKLGWSLD LILNTHWHPD 

        70         80         90        100        110        120 
HAGGNETLKT ATGATIVGPA EVTRIAPLDR VVRDGEEVML GDTRLTVIDT GGHTLGHVSY 

       130        140        150        160        170        180 
YDAEDAIAFV GDTLFALGCG RLFEGTAEQM WDSLGRLIAL PDETTVYCAH EYTASNARFA 

       190        200        210        220        230        240 
LSVDSSAALA ARAEAVFAAR ARDEATVPTT IGVEKATNPF LRAPLLRPDA PSPAQAFAEI 


RAAKDSFKG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005673 Genomic DNA. Translation: AAK22506.1.
PIRF87313.
RefSeqNP_419338.1. NC_002696.2.

3D structure databases

HSSPHSSP built from PDB template 1QH5 based on UniProtKB Q16775.
ProteinModelPortalQ9AAS7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID941843.
GenomeReviewsGene locus CC_0519 in contig AE005673_GR.
KEGGccr:CC_0519.
NMPDRfig|190650.1.peg.518.
PATRIC21297984. VBICauCre124313_0529.
TIGRCC_0519.

Phylogenomic databases

HOGENOMHBG753931.
OMAIGCGRVF.
ProtClustDBCLSK889979.

Family and domain databases

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

Entry information

Entry nameQ9AAS7_CAUCR
AccessionPrimary (citable) accession number: Q9AAS7
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: December 14, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)