A0A2W6PXV1 · A0A2W6PXV1_ECOLX

  • Protein
    Protein/nucleic acid deglycase HchA
  • Gene
    hchA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • H2O + N2-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H+
  • H2O + N2-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H+
  • H2O + N2-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H+
  • H2O + N2-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H+
  • H2O + N2-(1-hydroxy-2-oxopropyl)-GDP = GDP + H+ + lactate
  • H2O + N2-(1-hydroxy-2-oxopropyl)-GMP = GMP + H+ + lactate
  • H2O + N2-(1-hydroxy-2-oxopropyl)-GTP = GTP + H+ + lactate
  • H2O + N2-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H+ + lactate
  • H2O + N6-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H+ + L-lysyl-[protein]
  • H2O + N6-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H+ + L-lysyl-[protein] + lactate
    EC:3.5.1.124 (UniProtKB | ENZYME | Rhea)
  • H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H+ + L-arginyl-[protein]
  • H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H+ + L-arginyl-[protein] + lactate
    EC:3.5.1.124 (UniProtKB | ENZYME | Rhea)
  • H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H+ + L-cysteinyl-[protein]
  • H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H+ + L-cysteinyl-[protein] + lactate
    EC:3.5.1.124 (UniProtKB | ENZYME | Rhea)
  • H2O + methylglyoxal = (R)-lactate + H+
    EC:4.2.1.130 (UniProtKB | ENZYME | Rhea)
  • an N2-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H+
  • an N2-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H+
  • an N2-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H+ + lactate
  • an N2-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H+ + lactate

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site86Zn2+ (UniProtKB | ChEBI)
Binding site91Zn2+ (UniProtKB | ChEBI)
Binding site123Zn2+ (UniProtKB | ChEBI)
Active site185Nucleophile

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglyoxalase III activity
Molecular Functionprotein deglycase activity
Molecular Functionthiolester hydrolase activity
Molecular Functionzinc ion binding
Biological ProcessDNA repair
Biological Processprotein repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein/nucleic acid deglycase HchA
  • EC number
  • Alternative names
    • Maillard deglycase

Gene names

    • Name
      hchA
    • ORF names
      DNQ45_22235

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • EcMLT
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A2W6PXV1

Proteomes

Subcellular Location

Keywords

Expression

Induction

By heat shock.

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the peptidase C56 family. HSP31-like subfamily.
Belongs to the peptidase C56 family. HchA subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    283
  • Mass (Da)
    31,194
  • Last updated
    2018-09-12 v1
  • Checksum
    206A880A904FBA54
MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLSTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLAEVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QKWZ01000683
EMBL· GenBank· DDBJ
PZT64500.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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