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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)DescriptionActionsGraphical viewLength
Binding sitei38Glutathione1 Publication1
Binding sitei52Glutathione; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei176Glutathione1 Publication1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004214691 – 212Maleylpyruvate isomeraseAdd BLAST212

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1212
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi10 – 22Combined sources13
Beta strandi27 – 30Combined sources4
Turni33 – 36Combined sources4
Helixi37 – 39Combined sources3
Helixi41 – 46Combined sources6
Beta strandi54 – 56Combined sources3
Beta strandi61 – 63Combined sources3
Helixi65 – 75Combined sources11
Helixi86 – 102Combined sources17
Helixi104 – 107Combined sources4
Helixi109 – 119Combined sources11
Helixi123 – 147Combined sources25
Beta strandi153 – 156Combined sources4
Helixi162 – 176Combined sources15
Helixi185 – 194Combined sources10
Helixi198 – 203Combined sources6
Helixi205 – 207Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JL4X-ray2.30A/B1-212[»]
2V6KX-ray1.30A/B1-212[»]
ProteinModelPortaliO86043.
SMRiO86043.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO86043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 80GST N-terminalSequence analysisAdd BLAST80
Domaini85 – 212GST C-terminalSequence analysisAdd BLAST128

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 11Glutathione binding1 Publication3
Regioni64 – 65Glutathione binding1 Publication2
Regioni102 – 104Glutathione binding1 Publication3
Regioni108 – 110Glutathione binding1 Publication3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JL4X-ray2.30A/B1-212[»]
2V6KX-ray1.30A/B1-212[»]
ProteinModelPortaliO86043.
SMRiO86043.
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 2, 2016
This is version 72 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.