Reviewed, UniProtKB/Swiss-Prot O24495 (GLO2M_ARATH)

Names and origin

Protein names

Recommended name:
    Hydroxyacylglutathione hydrolase 1, mitochondrial
    EC=3.1.2.6
Alternative name(s):
    Glyoxalase II
      Short name=Glx II

Gene names

Name:	GLX2-1
Synonyms:	GLY1
Ordered Locus Names:	At2g43430
ORF Names:	T1O24.17

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
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 By similarity.
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Subcellular location	Mitochondrion.
Tissue specificity	Mainly expressed in roots, flowers and flower buds. Also detected in leaves. Ref.1
Sequence similarities	Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Iron Manganese Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	antibiotic catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-lactamase activity Inferred from direct assay. Source: TAIR hydroxyacylglutathione hydrolase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O24495-1)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 76	76	Mitochondrion Potential
	Chain	77 – 331	255	Hydroxyacylglutathione hydrolase 1, mitochondrial		PRO_0000012286
Sites
	Metal binding	131	1	Divalent metal cation 1 By similarity
	Metal binding	133	1	Divalent metal cation 1 By similarity
	Metal binding	135	1	Divalent metal cation 2 By similarity
	Metal binding	136	1	Divalent metal cation 2 By similarity
	Metal binding	189	1	Divalent metal cation 1 By similarity
	Metal binding	208	1	Divalent metal cation 1 By similarity
	Metal binding	208	1	Divalent metal cation 2 By similarity
Experimental info
	Sequence conflict	159	1	D → H in AAC49866. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 27, 2002. Version 2. Checksum: 2EDC21B4902419C5	FASTA	331	36,500
	10 20 30 40 50 60 MPVISKASST TTNSSIPSCS RIGGQLCVWP GLRQLCLRKS LLYGVMWLLS MPLKTLRGAR 70 80 90 100 110 120 KTLKITHFCS ISNMPSSLKI ELVPCSKDNY AYLLHDEDTG TVGVVDPSEA APVIEALSRK 130 140 150 160 170 180 NWNLTYILNT HHHDDHIGGN AELKERYGAK VIGSAVDKDR IPGIDILLKD SDKWMFAGHE 190 200 210 220 230 240 VRILDTPGHT QGHISFYFPG SATIFTGDLI YSLSCGTLSE GTPEQMLSSL QKIVSLPDDT 250 260 270 280 290 300 NIYCGRENTA GNLKFALSVE PKNETLQSYA TRVAHLRSQG LPSIPTTVKV EKACNPFLRI 310 320 330 SSKDIRKSLS IPDSATEAEA LRRIQRARDR F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of glyoxalase II from Arabidopsis thaliana." Maiti M.K., Krishnasamy S., Owen H.A., Makaroff C.A. Plant Mol. Biol. 35:471-481(1997) [PubMed: 9349270] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Wassilewskija.
[2]	"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. , 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.
[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. , 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]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U90927 Genomic DNA. Translation: AAC49865.1. U90928 mRNA. Translation: AAC49866.1. AC002335 Genomic DNA. Translation: AAB64315.2. AY091278 mRNA. Translation: AAM14217.1. AY063806 mRNA. Translation: AAL36162.1.
IPI	IPI00543847.
PIR	A84866.
RefSeq	NP_565999.1.
UniGene	At.10817
3D structure databases
SMR	O24495. Positions 78-331.
ModBase	Search...
Genome annotation databases
GeneID	818944.
GenomeReviews	Gene locus AT2G43430 in contig CT485783_GR.
KEGG	ath:AT2G43430.
NMPDR	fig|3702.1.peg.11499.
Organism-specific databases
TAIR	At2g43430.
Phylogenomic databases
eggNOG	KOG0813.
HOGENOM	HBG753931.
InParanoid	O24495.
OMA	RENTAGN.
PhylomeDB	O24495.
Enzyme and pathway databases
BRENDA	3.1.2.6. 302.
Gene expression databases
ArrayExpress	O24495.
Genevestigator	O24495.
Family and domain databases
InterPro	IPR001018. Beta-lactamase_class-B_CS. IPR001279. Blactmase-like. IPR017782. Hydroxyacylglutathione_Hdrlase. [Graphical view]
SMART	SM00849. Lactamase_B. 1 hit. [Graphical view]
TIGRFAMs	TIGR03413. GSH_gloB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GLO2M_ARATH

Accession

Primary (citable) accession number: O24495
Secondary accession number(s): O22857, O24494

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 27, 2002
Last modified:	February 9, 2010
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)