Reviewed, UniProtKB/Swiss-Prot O24496 (GLO2C_ARATH)

Names and origin

Protein names

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

Gene names

Name:	GLX2-2
Synonyms:	GLY2
Ordered Locus Names:	At3g10850
ORF Names:	T7M13.7

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	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 cation ions per subunit. Possible ions are zinc or iron and manganese. The average metal content is 0.8 +/-0.2 iron, 0.4 +/- 0.2 zinc, and 0.3 +/- 0.05 manganese per protein. Ref.6
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Subunit structure	Homodimer Probable.
Subcellular location	Cytoplasm.
Tissue specificity	Mainly expressed in flowers and flower buds. Also detected in roots and leaves. Ref.1
Sequence similarities	Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Biophysicochemical properties	Kinetic parameters: KM=220 µM for S-D-lactoylglutathion

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Iron Manganese Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 258	258	Hydroxyacylglutathione hydrolase cytoplasmic		PRO_0000192347
Sites
	Metal binding	54	1	Divalent metal cation 1 By similarity
	Metal binding	56	1	Divalent metal cation 1 By similarity
	Metal binding	58	1	Divalent metal cation 2 By similarity
	Metal binding	59	1	Divalent metal cation 2 By similarity
	Metal binding	112	1	Divalent metal cation 1 By similarity
	Metal binding	135	1	Divalent metal cation 1 By similarity
	Metal binding	135	1	Divalent metal cation 2 By similarity
	Metal binding	174	1	Divalent metal cation 2 By similarity
Experimental info
	Mutagenesis	54	1	H → N: Binds normal amount of metal, but reduced enzyme activity. Ref.5
	Mutagenesis	58	1	D → C: Binds normal amount of metal, but reduced enzyme activity. Ref.5
	Mutagenesis	142	1	C → A: Increases the metal content and the enzyme activity. Ref.5
	Mutagenesis	144	1	K → A: Binds normal amount of metal, but reduced enzyme activity. Ref.5
	Mutagenesis	180	1	N → A: 70% reduction in enzyme activity. Ref.5
	Mutagenesis	227	1	R → A: Decreases metal binding and enzyme stability. Ref.5
	Mutagenesis	250	1	R → W: Decreases the substrate affinity. Ref.5
	Sequence conflict	14	1	S → T in AAC49867. Ref.1
	Sequence conflict	85 – 93	9	GCTDAVDNG → VALMRLIC in AAC49867. Ref.1
	Sequence conflict	98 – 102	5	LGQDI → WSGY in AAC49867. Ref.1
	Sequence conflict	122	1	N → T in AAC49867. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O24496-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 6703B98A8F902B5A	FASTA	258	28,792
	10 20 30 40 50 60 MKIFHVPCLQ DNYSYLIIDE STGDAAVVDP VDPEKVIASA EKHQAKIKFV LTTHHHWDHA 70 80 90 100 110 120 GGNEKIKQLV PDIKVYGGSL DKVKGCTDAV DNGDKLTLGQ DINILALHTP CHTKGHISYY 130 140 150 160 170 180 VNGKEGENPA VFTGDTLFVA GCGKFFEGTA EQMYQSLCVT LAALPKPTQV YCGHEYTVKN 190 200 210 220 230 240 LEFALTVEPN NGKIQQKLAW ARQQRQADLP TIPSTLEEEL ETNPFMRVDK PEIQEKLGCK 250 SPIDTMREVR NKKDQWRG

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]	"Molecular cloning and characterization of the thiolesterase glyoxalase II from Arabidopsis thaliana." Ridderstroem M., Mannervik B. Biochem. J. 322:449-454(1997) [PubMed: 9065762] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Leaf.
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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.
[5]	"Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis." Zang T.M., Hollman D.A., Crawford P.A., Crowder M.W., Makaroff C.A. J. Biol. Chem. 276:4788-4795(2001) [PubMed: 11085979] [Abstract] Cited for: MUTAGENESIS OF HIS-54; ASP-58; CYS-142; LYS-144; ASN-180; ARG-227 AND ARG-250.
[6]	"Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo." Schilling O., Wenzel N., Naylor M., Vogel A., Crowder M.W., Makaroff C.A., Meyer-Klaucke W. Biochemistry 42:11777-11786(2003) [PubMed: 14529289] [Abstract] Cited for: CHARACTERIZATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U90929 mRNA. Translation: AAC49867.1. Y08357 mRNA. Translation: CAA69644.1. AC011708 Genomic DNA. Translation: AAF19564.1. AY052329 mRNA. Translation: AAK96522.1. BT000849 mRNA. Translation: AAN38686.1.
IPI	IPI00532218.
RefSeq	NP_187696.1.
UniGene	At.47367 At.69008
3D structure databases
SMR	O24496. Positions 1-257.
ModBase	Search...
Proteomic databases
PRIDE	O24496.
Genome annotation databases
GeneID	820255.
GenomeReviews	Gene locus AT3G10850 in contig BA000014_GR.
KEGG	ath:AT3G10850.
Organism-specific databases
TAIR	At3g10850.
Phylogenomic databases
eggNOG	KOG0813.
HOGENOM	HBG753931.
InParanoid	O24496.
OMA	GSLNVKC.
PhylomeDB	O24496.
Enzyme and pathway databases
BRENDA	3.1.2.6. 302.
Gene expression databases
ArrayExpress	O24496.
Genevestigator	O24496.
GermOnline	AT3G10850. Arabidopsis thaliana.
Family and domain databases
InterPro	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

GLO2C_ARATH

Accession

Primary (citable) accession number: O24496
Secondary accession number(s): O04844

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 15, 1998
Last modified:	February 9, 2010
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)