Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q4R5F2

- LGUL_MACFA

UniProt

Q4R5F2 - LGUL_MACFA

Protein

Lactoylglutathione lyase

Gene

GLO1

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B By similarity.By similarity

    Catalytic activityi

    (R)-S-lactoylglutathione = glutathione + methylglyoxal.

    Cofactori

    Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi34 – 341Zinc; shared with dimeric partnerBy similarity
    Binding sitei34 – 341Substrate; shared with dimeric partnerBy similarity
    Binding sitei38 – 381Substrate; shared with dimeric partnerBy similarity
    Metal bindingi100 – 1001Zinc; shared with dimeric partnerBy similarity
    Binding sitei104 – 1041Substrate; shared with dimeric partnerBy similarity
    Binding sitei123 – 1231SubstrateBy similarity
    Metal bindingi127 – 1271Zinc; via tele nitrogenBy similarity
    Binding sitei127 – 1271SubstrateBy similarity
    Active sitei173 – 1731Proton donor/acceptorBy similarity
    Metal bindingi173 – 1731ZincBy similarity

    GO - Molecular functioni

    1. lactoylglutathione lyase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. metabolic process Source: GOC
    2. negative regulation of apoptotic process Source: UniProtKB

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00619; UER00675.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lactoylglutathione lyase (EC:4.4.1.5)
    Alternative name(s):
    Aldoketomutase
    Glyoxalase I
    Short name:
    Glx I
    Ketone-aldehyde mutase
    Methylglyoxalase
    S-D-lactoylglutathione methylglyoxal lyase
    Gene namesi
    Name:GLO1
    ORF Names:QnpA-15219
    OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
    Taxonomic identifieri9541 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 184183Lactoylglutathione lyasePRO_0000168077Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Disulfide bondi19 ↔ 20By similarity
    Disulfide bondi61 ↔ 139AlternateBy similarity
    Modified residuei88 – 881N6-succinyllysineBy similarity
    Modified residuei107 – 1071PhosphothreonineBy similarity
    Modified residuei139 – 1391S-glutathionyl cysteine; alternateBy similarity
    Modified residuei148 – 1481N6-acetyllysine; alternateBy similarity
    Modified residuei148 – 1481N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    Glutathionylation at Cys-139 inhibits enzyme activity.By similarity
    Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B By similarity.By similarity
    Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B By similarity.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Glutathionylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ4R5F2.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ4R5F2.
    SMRiQ4R5F2. Positions 2-184.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni157 – 1582Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glyoxalase I family.Curated

    Phylogenomic databases

    HOVERGENiHBG025852.
    KOiK01759.

    Family and domain databases

    Gene3Di3.10.180.10. 1 hit.
    InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR004360. Glyas_Fos-R_dOase_dom.
    IPR004361. Glyoxalase_1.
    IPR018146. Glyoxalase_1_CS.
    [Graphical view]
    PfamiPF00903. Glyoxalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF54593. SSF54593. 1 hit.
    TIGRFAMsiTIGR00068. glyox_I. 1 hit.
    PROSITEiPS00934. GLYOXALASE_I_1. 1 hit.
    PS00935. GLYOXALASE_I_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q4R5F2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT    50
    RVLGMTLIQK CDFPAMKFSL YFLAYEDKND IPKDKEEKIA WALSRKATLE 100
    LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVHSACK RFEELGVKFV 150
    KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM 184
    Length:184
    Mass (Da):20,710
    Last modified:January 23, 2007 - v3
    Checksum:i8E8B276CB80EAB34
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB169591 mRNA. Translation: BAE01673.1.
    RefSeqiNP_001271981.1. NM_001285052.1.
    UniGeneiMfa.8289.

    Genome annotation databases

    GeneIDi101926610.
    KEGGimcf:101926610.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB169591 mRNA. Translation: BAE01673.1 .
    RefSeqi NP_001271981.1. NM_001285052.1.
    UniGenei Mfa.8289.

    3D structure databases

    ProteinModelPortali Q4R5F2.
    SMRi Q4R5F2. Positions 2-184.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q4R5F2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 101926610.
    KEGGi mcf:101926610.

    Organism-specific databases

    CTDi 2739.

    Phylogenomic databases

    HOVERGENi HBG025852.
    KOi K01759.

    Enzyme and pathway databases

    UniPathwayi UPA00619 ; UER00675 .

    Family and domain databases

    Gene3Di 3.10.180.10. 1 hit.
    InterProi IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR004360. Glyas_Fos-R_dOase_dom.
    IPR004361. Glyoxalase_1.
    IPR018146. Glyoxalase_1_CS.
    [Graphical view ]
    Pfami PF00903. Glyoxalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54593. SSF54593. 1 hit.
    TIGRFAMsi TIGR00068. glyox_I. 1 hit.
    PROSITEi PS00934. GLYOXALASE_I_1. 1 hit.
    PS00935. GLYOXALASE_I_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."
      International consortium for macaque cDNA sequencing and analysis
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Parietal cortex.

    Entry informationi

    Entry nameiLGUL_MACFA
    AccessioniPrimary (citable) accession number: Q4R5F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 54 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3