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Protein

Maleylpyruvate isomerase

Gene

nagL

Organism
Ralstonia sp.
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

3-maleylpyruvate = 3-fumarylpyruvate.1 Publication

Cofactori

glutathione1 Publication

Pathwayi: naphthalene degradation

This protein is involved in the pathway naphthalene degradation, which is part of Aromatic compound metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway naphthalene degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Glutathione1 Publication
Binding sitei52 – 521Glutathione; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei176 – 1761Glutathione1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Pyruvate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14770.
UniPathwayiUPA00082.

Names & Taxonomyi

Protein namesi
Recommended name:
Maleylpyruvate isomerase1 PublicationImported (EC:5.2.1.41 Publication)
Short name:
MPI1 Publication
Alternative name(s):
Naphthalene degradation protein L
Gene namesi
Name:nagLImported
Encoded oniPlasmid pWWU2Imported
OrganismiRalstonia sp.
Taxonomic identifieri54061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Maleylpyruvate isomerasePRO_0000421469Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
212
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi10 – 2213Combined sources
Beta strandi27 – 304Combined sources
Turni33 – 364Combined sources
Helixi37 – 393Combined sources
Helixi41 – 466Combined sources
Beta strandi54 – 563Combined sources
Beta strandi61 – 633Combined sources
Helixi65 – 7511Combined sources
Helixi86 – 10217Combined sources
Helixi104 – 1074Combined sources
Helixi109 – 11911Combined sources
Helixi123 – 14725Combined sources
Beta strandi153 – 1564Combined sources
Helixi162 – 17615Combined sources
Helixi185 – 19410Combined sources
Helixi198 – 2036Combined sources
Helixi205 – 2073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JL4X-ray2.30A/B1-212[»]
2V6KX-ray1.30A/B1-212[»]
ProteinModelPortaliO86043.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO86043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8080GST N-terminalSequence analysisAdd
BLAST
Domaini85 – 212128GST C-terminalSequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 113Glutathione binding1 Publication
Regioni64 – 652Glutathione binding1 Publication
Regioni102 – 1043Glutathione binding1 Publication
Regioni108 – 1103Glutathione binding1 Publication

Sequence similaritiesi

Belongs to the GST superfamily. Zeta family.Sequence analysis
Contains 1 GST C-terminal domain.Sequence analysis
Contains 1 GST N-terminal domain.Sequence analysis

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01262. maiA. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O86043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLYNFWRSG TSHRLRIALN LKGVPYEYLA VHLGKEEHLK DAFKALNPQQ
60 70 80 90 100
LVPALDTGAQ VLIQSPAIIE WLEEQYPTPA LLPADADGRQ RVRALAAIVG
110 120 130 140 150
CDIHPINNRR ILEYLRKTFG ADEAAINAWC GTWISAGFDA YEALLAVDPK
160 170 180 190 200
RGRYSFGDTP TLADCYLVPQ VESARRFQVD LTPYPLIRAV DAACGELDAF
210
RRAAPAAQPD SA
Length:212
Mass (Da):23,505
Last modified:November 1, 1998 - v1
Checksum:i6554F3B95591EAEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036940 Genomic DNA. Translation: AAD12621.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036940 Genomic DNA. Translation: AAD12621.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JL4X-ray2.30A/B1-212[»]
2V6KX-ray1.30A/B1-212[»]
ProteinModelPortaliO86043.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00082.
BioCyciMetaCyc:MONOMER-14770.

Miscellaneous databases

EvolutionaryTraceiO86043.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01262. maiA. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNAGL_RALSP
AccessioniPrimary (citable) accession number: O86043
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.