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Protein

Hydroxyacylglutathione hydrolase

Gene

gloB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.1 Publication

Catalytic activityi

S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate.

Cofactori

Fe2+1 Publication, Zn2+1 Publication, Mn2+1 PublicationNote: Binds 2 metal ions per subunit; upon overexpression in E.coli the enzyme purifies with various amounts of iron, zinc and manganese. The endogenous metal is unknown.1 Publication

Pathwayi: methylglyoxal degradation

This protein is involved in step 2 of the subpathway that synthesizes (R)-lactate from methylglyoxal.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Lactoylglutathione lyase (gloA)
  2. Hydroxyacylglutathione hydrolase (gloB)
This subpathway is part of the pathway methylglyoxal degradation, which is itself part of Secondary metabolite metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-lactate from methylglyoxal, the pathway methylglyoxal degradation and in Secondary metabolite metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi53Divalent metal cation 1; via tele nitrogen1 Publication1
Metal bindingi55Divalent metal cation 1; via pros nitrogen1 Publication1
Metal bindingi57Divalent metal cation 21 Publication1
Metal bindingi58Divalent metal cation 2; via tele nitrogen1 Publication1
Metal bindingi110Divalent metal cation 1; via tele nitrogen1 Publication1
Metal bindingi127Divalent metal cation 11 Publication1
Metal bindingi127Divalent metal cation 21 Publication1
Metal bindingi165Divalent metal cation 2; via tele nitrogen1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.2.6. 5542.
SABIO-RKQ8ZRM2.
UniPathwayiUPA00619; UER00676.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacylglutathione hydrolase (EC:3.1.2.6)
Alternative name(s):
Glyoxalase II
Short name:
Glx II
Gene namesi
Name:gloB
Ordered Locus Names:STM0261
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003097041 – 251Hydroxyacylglutathione hydrolaseAdd BLAST251

Proteomic databases

PaxDbiQ8ZRM2.
PRIDEiQ8ZRM2.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM0261.

Structurei

Secondary structure

1251
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Turni9 – 11Combined sources3
Beta strandi12 – 18Combined sources7
Beta strandi22 – 27Combined sources6
Helixi32 – 42Combined sources11
Beta strandi45 – 50Combined sources6
Helixi56 – 59Combined sources4
Helixi62 – 68Combined sources7
Beta strandi73 – 76Combined sources4
Helixi78 – 83Combined sources6
Beta strandi86 – 88Combined sources3
Beta strandi94 – 97Combined sources4
Beta strandi100 – 106Combined sources7
Beta strandi109 – 111Combined sources3
Beta strandi115 – 119Combined sources5
Beta strandi122 – 126Combined sources5
Beta strandi138 – 140Combined sources3
Helixi142 – 153Combined sources12
Beta strandi160 – 165Combined sources6
Helixi168 – 178Combined sources11
Helixi183 – 197Combined sources15
Helixi207 – 213Combined sources7
Helixi215 – 217Combined sources3
Helixi222 – 229Combined sources8
Helixi237 – 250Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QEDX-ray1.45A1-251[»]
ProteinModelPortaliQ8ZRM2.
SMRiQ8ZRM2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8ZRM2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108RW0. Bacteria.
COG0491. LUCA.
HOGENOMiHOG000058041.
KOiK01069.
OMAiDNYIFLL.
PhylomeDBiQ8ZRM2.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01374. Glyoxalase_2. 1 hit.
InterProiIPR032282. HAGH_C.
IPR017782. Hydroxyacylglutathione_Hdrlase.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF16123. HAGH_C. 1 hit.
PF00753. Lactamase_B. 1 hit.
[Graphical view]
PIRSFiPIRSF005457. Glx. 1 hit.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR03413. GSH_gloB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8ZRM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLNSIPAFQ DNYIWVLTND EGRCVIVDPG EAAPVLKAIA EHKWMPEAIF
60 70 80 90 100
LTHHHHDHVG GVKELLQHFP QMTVYGPAET QDKGATHLVG DGDTIRVLGE
110 120 130 140 150
KFTLFATPGH TLGHVCYFSR PYLFCGDTLF SGGCGRLFEG TPSQMYQSLM
160 170 180 190 200
KINSLPDDTL ICCAHEYTLA NIKFALSILP HDSFINEYYR KVKELRVKKQ
210 220 230 240 250
MTLPVILKNE RKINLFLRTE DIDLINEINK ETILQQPEAR FAWLRSKKDT

F
Length:251
Mass (Da):28,633
Last modified:March 1, 2002 - v1
Checksum:i5A8194A0C921C0E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19218.1.
RefSeqiNP_459259.1. NC_003197.1.
WP_001052775.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19218; AAL19218; STM0261.
GeneIDi1251779.
KEGGistm:STM0261.
PATRICi32378813. VBISalEnt20916_0270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19218.1.
RefSeqiNP_459259.1. NC_003197.1.
WP_001052775.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QEDX-ray1.45A1-251[»]
ProteinModelPortaliQ8ZRM2.
SMRiQ8ZRM2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM0261.

Proteomic databases

PaxDbiQ8ZRM2.
PRIDEiQ8ZRM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19218; AAL19218; STM0261.
GeneIDi1251779.
KEGGistm:STM0261.
PATRICi32378813. VBISalEnt20916_0270.

Phylogenomic databases

eggNOGiENOG4108RW0. Bacteria.
COG0491. LUCA.
HOGENOMiHOG000058041.
KOiK01069.
OMAiDNYIFLL.
PhylomeDBiQ8ZRM2.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00676.
BRENDAi3.1.2.6. 5542.
SABIO-RKQ8ZRM2.

Miscellaneous databases

EvolutionaryTraceiQ8ZRM2.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01374. Glyoxalase_2. 1 hit.
InterProiIPR032282. HAGH_C.
IPR017782. Hydroxyacylglutathione_Hdrlase.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF16123. HAGH_C. 1 hit.
PF00753. Lactamase_B. 1 hit.
[Graphical view]
PIRSFiPIRSF005457. Glx. 1 hit.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR03413. GSH_gloB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLO2_SALTY
AccessioniPrimary (citable) accession number: Q8ZRM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2002
Last modified: November 2, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.