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Q9SID3 (GLO2N_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxyacylglutathione hydrolase 2, mitochondrial
EC=3.1.2.6
Alternative name(s):
Glyoxalase II
Short name=Glx II
Gene names
Ordered Locus Names:At2g31350
ORF Names:T28P16.16
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 divalent metal cations per subunit. Possible ions are zinc or iron and manganese.

Pathway

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

Subcellular location

Mitochondrion Potential.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandIron
Manganese
Metal-binding
Zinc
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentmitochondrion

Non-traceable author statement Ref.4. Source: TAIR

   Molecular functionhydroxyacylglutathione hydrolase activity

Inferred from direct assay Ref.4. Source: TAIR

iron ion binding

Inferred from direct assay Ref.4. Source: TAIR

zinc ion binding

Inferred from direct assay Ref.4. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9SID3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9SID3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: Missing.
Note: Derived from EST data. May be due to a competing acceptor splice site. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6464Mitochondrion Potential
Chain65 – 324260Hydroxyacylglutathione hydrolase 2, mitochondrial
PRO_0000012287

Sites

Metal binding1241Divalent metal cation 1
Metal binding1261Divalent metal cation 1
Metal binding1281Divalent metal cation 2
Metal binding1291Divalent metal cation 2
Metal binding1821Divalent metal cation 1
Metal binding2011Divalent metal cation 1
Metal binding2011Divalent metal cation 2
Metal binding2391Divalent metal cation 2

Natural variations

Alternative sequence191Missing in isoform 2.
VSP_018092

Secondary structure

1 ................................................... 324
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 91F47F391EFB0AE1

FASTA32435,841
        10         20         30         40         50         60 
MQTISKASSA TSFFRCSRKL SSQPCVRQLN IRKSLVCRVM KLVSSPLRTL RGAGKSIRVS 

        70         80         90        100        110        120 
KFCSVSNVSS LQIELVPCLK DNYAYILHDE DTGTVGVVDP SEAEPIIDSL KRSGRNLTYI 

       130        140        150        160        170        180 
LNTHHHYDHT GGNLELKDRY GAKVIGSAMD KDRIPGIDMA LKDGDKWMFA GHEVHVMDTP 

       190        200        210        220        230        240 
GHTKGHISLY FPGSRAIFTG DTMFSLSCGK LFEGTPKQML ASLQKITSLP DDTSIYCGHE 

       250        260        270        280        290        300 
YTLSNSKFAL SLEPNNEVLQ SYAAHVAELR SKKLPTIPTT VKMEKACNPF LRSSNTDIRR 

       310        320 
ALRIPEAADE AEALGIIRKA KDDF

« Hide

Isoform 2 [UniParc].

Checksum: C32FD27BAC63BCC0
Show »

FASTA32335,713

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[4]"Structural studies on a mitochondrial glyoxalase II."
Marasinghe G.P., Sander I.M., Bennett B., Periyannan G., Yang K.W., Makaroff C.A., Crowder M.W.
J. Biol. Chem. 280:40668-40675(2005) [PubMed: 16227621] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 72-324 IN COMPLEX WITH ZINC AND IRON.
[5]"Ensemble refinement of protein crystal structures: validation and application."
Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.
Structure 15:1040-1052(2007) [PubMed: 17850744] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 72-324 IN COMPLEX WITH ZINC AND IRON.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC007169 Genomic DNA. Translation: AAD26483.1.
CP002685 Genomic DNA. Translation: AEC08531.1.
CP002685 Genomic DNA. Translation: AEC08532.1.
AY072200 mRNA. Translation: AAL60021.1.
AY096672 mRNA. Translation: AAM20306.1.
IPIIPI00528470.
IPI00531832.
PIRF84719.
RefSeqNP_180693.1. NM_128692.4.
NP_850166.1. NM_179835.1.
UniGeneAt.27616.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XM8X-ray1.74A/B72-324[»]
2Q42X-ray1.74A/B72-324[»]
ProteinModelPortalQ9SID3.
SMRQ9SID3. Positions 71-324.
ModBaseSearch...

Proteomic databases

PRIDEQ9SID3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G31350.1; AT2G31350.1; AT2G31350.
GeneID817693.
GenomeReviewsGene locus AT2G31350 in contig CT485783_GR.
KEGGath:AT2G31350.
NMPDRfig|3702.1.peg.10194.

Organism-specific databases

TAIRAt2g31350.

Phylogenomic databases

eggNOGKOG0813.
GeneTreeEPGT00070000030319.
HOGENOMHBG753931.
InParanoidQ9SID3.
OMAFLCRTDN.
PhylomeDBQ9SID3.
ProtClustDBPLN02398.

Gene expression databases

ArrayExpressQ9SID3.
GenevestigatorQ9SID3.
GermOnlineAT2G31350. Arabidopsis thaliana.

Family and domain databases

InterProIPR001279. Beta-lactamas-like.
IPR017782. Hydroxyacylglutathione_Hdrlase.
[Graphical view]
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 nameGLO2N_ARATH
AccessionPrimary (citable) accession number: Q9SID3
Secondary accession number(s): Q3EBQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 2000
Last modified: October 19, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents