Reviewed, UniProtKB/Swiss-Prot Q9CPU0 (LGUL_MOUSE)

Names and origin

Protein names

Recommended name:
    Lactoylglutathione lyase
    EC=4.4.1.5
Alternative name(s):
    Methylglyoxalase
    Aldoketomutase
    Glyoxalase I
      Short name=Glx I
    Ketone-aldehyde mutase
    S-D-lactoylglutathione methylglyoxal lyase

Gene names

Name:

Glo1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione By similarity.
Catalytic activity	(R)-S-lactoylglutathione = glutathione + methylglyoxal.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Subunit structure	Homodimer By similarity.
Miscellaneous	Expressed at higher levels in CD-1 mice which have been bred for low-anxiety-related behavior than in those which have been bred for high-anxiety-related behavior.
Sequence similarities	Belongs to the glyoxalase I family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	lactoylglutathione lyase activity Inferred from sequence or structural similarity. Source: UniProtKB 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

Initiator methionine

1

1

Removed By similarity

Chain

2 – 184

183

Lactoylglutathione lyase

PRO_0000168078

Sites

Metal binding

34

1

Zinc By similarity

Metal binding

100

1

Zinc By similarity

Metal binding

127

1

Zinc By similarity

Metal binding

173

1

Zinc By similarity

Amino acid modifications

Modified residue

148

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

92

1

T → M in AAH24663. Ref.2

Secondary structure

1

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184

Helix Strand Turn

Details...

Helix

13 – 18

6

Helix

25 – 27

3

Beta strand

34 – 38

5

Helix

43 – 51

9

Beta strand

56 – 63

8

Helix

64 – 66

3

Beta strand

68 – 75

8

Helix

78 – 80

3

Helix

85 – 92

8

Beta strand

95 – 104

10

Helix

135 – 144

10

Beta strand

149 – 151

3

Beta strand

162 – 165

4

Beta strand

171 – 175

5

Turn

177 – 179

3

Helix

180 – 182

3

Sequences

	Sequence		Length	Mass (Da)
	Q9CPU0-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F6B5667A65454D18	FASTA	184	20,810
	10 20 30 40 50 60 MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK 70 80 90 100 110 120 LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE LTHNWGTEDD ETQSYHNGNS 130 140 150 160 170 180 DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo, Kidney, Liver, Medulla oblongata and Spinal cord.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and Czech II. Tissue: Brain and Mammary gland.
[3]	"Identification of glyoxalase-I as a protein marker in a mouse model of extremes in trait anxiety." Kroemer S.A., Kessler M.S., Milfay D., Birg I.N., Bunck M., Czibere L., Panhuysen M., Puetz B., Deussing J.M., Holsboer F., Landgraf R., Turck C.W. J. Neurosci. 25:4375-4384(2005) [PubMed: 15858064] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, EXPRESSION IN CD-1 STRAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AK002386 mRNA. Translation: BAB22060.1.
AK003567 mRNA. Translation: BAB22863.1.
AK005055 mRNA. Translation: BAB23781.1.
AK031832 mRNA. Translation: BAC27570.1.
AK049703 mRNA. Translation: BAC33882.1.
BC024663 mRNA. Translation: AAH24663.1.
BC081432 mRNA. Translation: AAH81432.1.

IPI

IPI00321734.

RefSeq

NP_001107032.1.
NP_079650.3.

UniGene

Mm.261984

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZA0	X-ray	1.70	A/B	1-184	[»]

SMR

Q9CPU0. Positions 2-184.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9CPU0.

PTM databases

PhosphoSite

Q9CPU0.

2-D gel databases

REPRODUCTION-2DPAGE

Q9CPU0.

Proteomic databases

PRIDE

Q9CPU0.

Genome annotation databases

Ensembl

ENSMUST00000024823; ENSMUSP00000024823; ENSMUSG00000024026; Mus musculus. [Genome view]

GeneID

109801.

KEGG

mmu:109801.

UCSC

uc008btx.1. mouse.

Organism-specific databases

CTD

109801.

MGI

MGI:95742. Glo1.

Phylogenomic databases

HOGENOM

Q9CPU0.

HOVERGEN

Q9CPU0.

OMA

FAYHNGN.

Enzyme and pathway databases

BRENDA

4.4.1.5. 244.

Gene expression databases

ArrayExpress

Q9CPU0.

Bgee

Q9CPU0.

CleanEx

MM_GLO1.

Genevestigator

Q9CPU0.

GermOnline

ENSMUSG00000024026. Mus musculus.
ENSMUSG00000075391. Mus musculus.

Family and domain databases

InterPro

IPR004360. Glyas_bleo-R_dOase.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]

Pfam

PF00903. Glyoxalase. 1 hit.
[Graphical view]

ProDom

PD002334. Gly_diox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00068. glyox_I. 1 hit.

PROSITE

PS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

362781.

SOURCE

Search...

Entry information

Entry name

LGUL_MOUSE

Accession

Primary (citable) accession number: Q9CPU0
Secondary accession number(s): Q543L3, Q8R3T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)