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Q7V6G8 (GLO2_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:PMT_1194
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length260 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 – 260260Hydroxyacylglutathione hydrolase HAMAP MF_01374
PRO_0000309680

Sites

Metal binding661Zinc 1 By similarity
Metal binding681Zinc 1 By similarity
Metal binding701Zinc 2 By similarity
Metal binding711Zinc 2 By similarity
Metal binding1251Zinc 1 By similarity
Metal binding1501Zinc 1 By similarity
Metal binding1501Zinc 2 By similarity
Metal binding1881Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V6G8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: A384BD33702814B5

FASTA26028,990
        10         20         30         40         50         60 
MEATSTAATS DKQRSSIHAL PVLQDNIIWI WIKGNQAVVV DPAIAEPVKT WLRTRKLSLA 

        70         80         90        100        110        120 
AVLQTHHHAD HIGGTLELLR DWPNAAVVAA AEDRDRIPFQ TISVRDRDKV SLLNSSVEVL 

       130        140        150        160        170        180 
AVAGHTRAHI AYYLPTNKED LEDPAVFCGD TLFGAGCGRL FEGTAEDMFK ALQRLSCLPA 

       190        200        210        220        230        240 
KTRVYCAHEY TEANLRWASA LHPEDVAISE RLADVSSRRQ RGALSLPSSI SEEQRTNLFV 

       250        260 
RAQSSKELAE LRHHKDQWRN 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE21369.1.
RefSeqNP_895024.1. NC_005071.1.

3D structure databases

HSSPHSSP built from PDB template 1QH5 based on UniProtKB Q16775.
ProteinModelPortalQ7V6G8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7V6G8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1729141.
GenomeReviewsGene locus PMT_1194 in contig BX548175_GR.
KEGGpmt:PMT1194.
NMPDRfig|74547.1.peg.1191.
PATRIC23010793. VBIProMar135351_1545.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0491.
HOGENOMHBG753931.
OMAITHHHRD.
PhylomeDBQ7V6G8.
ProtClustDBCLSK647185.

Enzyme and pathway databases

BioCycPMAR74547:PMT1194-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_PROMM
AccessionPrimary (citable) accession number: Q7V6G8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 47 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