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O86043 (NAGL_RALSP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Maleylpyruvate isomerase
Short name=MPI
EC=5.2.1.4
Alternative name(s):
Naphthalene degradation protein L
Gene names
Name:nagL
Encoded onPlasmid pWWU2
OrganismRalstonia sp.
Taxonomic identifier54061 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Ralstonia

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the GSH-dependent isomerization of maleylpyruvate to fumarylpyruvate which is subsequently processed by NagK to form pyruvate and fumarate. Ref.1

Catalytic activity

3-maleylpyruvate = 3-fumarylpyruvate. Ref.1

Cofactor

Glutathione. Ref.2

Pathway

Aromatic compound metabolism; naphthalene degradation. Ref.1

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the GST superfamily. Zeta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandPyruvate
   Molecular functionIsomerase
   Technical term3D-structure
Plasmid
Gene Ontology (GO)
   Biological_processaromatic amino acid family metabolic process

Inferred from electronic annotation. Source: InterPro

aromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmaleylpyruvate isomerase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Maleylpyruvate isomerase
PRO_0000421469

Regions

Domain1 – 8080GST N-terminal
Domain85 – 212128GST C-terminal
Region9 – 113Glutathione binding
Region64 – 652Glutathione binding
Region102 – 1043Glutathione binding
Region108 – 1103Glutathione binding

Sites

Binding site381Glutathione
Binding site521Glutathione; via amide nitrogen and carbonyl oxygen
Binding site1761Glutathione

Secondary structure

1 .................................... 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O86043 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 6554F3B95591EAEE

FASTA21223,505
        10         20         30         40         50         60 
MKLYNFWRSG TSHRLRIALN LKGVPYEYLA VHLGKEEHLK DAFKALNPQQ LVPALDTGAQ 

        70         80         90        100        110        120 
VLIQSPAIIE WLEEQYPTPA LLPADADGRQ RVRALAAIVG CDIHPINNRR ILEYLRKTFG 

       130        140        150        160        170        180 
ADEAAINAWC GTWISAGFDA YEALLAVDPK RGRYSFGDTP TLADCYLVPQ VESARRFQVD 

       190        200        210 
LTPYPLIRAV DAACGELDAF RRAAPAAQPD SA

« Hide

References

[1]"nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism."
Zhou N.Y., Fuenmayor S.L., Williams P.A.
J. Bacteriol. 183:700-708(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
Strain: U2.
[2]"Structure of bacterial glutathione-S-transferase maleyl pyruvate isomerase and implications for mechanism of isomerisation."
Marsh M., Shoemark D.K., Jacob A., Robinson C., Cahill B., Zhou N.Y., Williams P.A., Hadfield A.T.
J. Mol. Biol. 384:165-177(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, COFACTOR, SUBUNIT.
Strain: U2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF036940 Genomic DNA. Translation: AAD12621.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JL4X-ray2.30A/B1-212[»]
2V6KX-ray1.30A/B1-212[»]
ProteinModelPortalO86043.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14770.
UniPathwayUPA00082.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMSSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMsTIGR01262. maiA. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO86043.

Entry information

Entry nameNAGL_RALSP
AccessionPrimary (citable) accession number: O86043
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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