Reviewed, UniProtKB/Swiss-Prot Q9UT36 (GLO21_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable hydroxyacylglutathione hydrolase C824.07
    EC=3.1.2.6
Alternative name(s):
    Glyoxalase II
      Short name=Glx II

Gene names

ORF Names:

SPAC824.07

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
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 By similarity.
Catalytic activity	S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Subcellular location	Cytoplasm. Nucleus Ref.2.
Sequence similarities	Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to stress Inferred from expression pattern. Source: GeneDB_SPombe response to methylglyoxal Non-traceable author statement. Source: GeneDB_SPombe
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe nucleus Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	hydroxyacylglutathione hydrolase activity Inferred from electronic annotation. Source: EC 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 – 256	256	Probable hydroxyacylglutathione hydrolase C824.07		PRO_0000337689
Regions
	Region	178 – 180	3	Substrate By similarity
	Region	250 – 253	4	Substrate By similarity
Sites
	Metal binding	63	1	Zinc 1 By similarity
	Metal binding	65	1	Zinc 1 By similarity
	Metal binding	67	1	Zinc 2 By similarity
	Metal binding	68	1	Zinc 2 By similarity
	Metal binding	118	1	Zinc 1 By similarity
	Metal binding	139	1	Zinc 1 By similarity
	Metal binding	139	1	Zinc 2 By similarity
	Metal binding	178	1	Zinc 2 By similarity
	Binding site	148	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9UT36-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 1DA6B3A0F8BBF0FE	FASTA	256	28,483
	10 20 30 40 50 60 MSFHITPIWM WKGTGNNYAY LLTCDKTKIT AIVDPAEPES VIPVIKEKTA KKEIDLQYIL 70 80 90 100 110 120 TTHHHYDHAG GNEDILSYFP SLKVYGGKNA SGVTYTPKDK EIFKVGEVQV EALHTPCHTQ 130 140 150 160 170 180 DSICYYVSSP SKRAVFTGDT LFTSGCGRFF EGDAKQMDYA LNHVLAALPD DTVTYPGHEY 190 200 210 220 230 240 TKSNAKFSST IFSTPELTKL VDFCKNHEST TGHFTIGDEK KFNPFMCLGL ESVQKAVGSS 250 DPITVMKKLR DMKNAA

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB57337.1.
PIR	T39108.
RefSeq	NP_593446.1.
3D structure databases
HSSP	HSSP built from PDB template 1QH5 based on UniProtKB Q16775.
SMR	Q9UT36. Positions 14-255.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UT36.
Genome annotation databases
GeneID	2542447.
KEGG	spo:SPAC824.07.
NMPDR	fig|4896.1.peg.3416.
Organism-specific databases
GeneDB_Spombe	SPAC824.07.
Phylogenomic databases
eggNOG	fuNOG07131.
HOGENOM	HBG753931.
OMA	GSLNVKC.
OrthoDB	EOG9C2JTC.
PhylomeDB	Q9UT36.
Gene expression databases
ArrayExpress	Q9UT36.
Family and domain databases
InterPro	IPR001279. Blactmase-like. [Graphical view]
SMART	SM00849. Lactamase_B. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLO21_SCHPO

Accession

Primary (citable) accession number: Q9UT36

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 1, 2000
Last modified:	January 19, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)