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P57113 (MAAI_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Maleylacetoacetate isomerase

Short name=MAAI
EC=5.2.1.2
Alternative name(s):
GSTZ1-1
Glutathione S-transferase zeta 1
EC=2.5.1.18
Gene names
Name:Gstz1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1, 3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with t-butyl and cumene hydroperoxides By similarity. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. Ref.4

Catalytic activity

4-maleylacetoacetate = 4-fumarylacetoacetate. Ref.4

RX + glutathione = HX + R-S-glutathione. Ref.4

Cofactor

Glutathione. Required for the MAAI activity By similarity.

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Ref.4.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the GST superfamily. Zeta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=71.4 µM for dichloroacetic acid Ref.4

KM=59.0 µM for glutathione

Vmax=1334 nmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216Maleylacetoacetate isomerase
PRO_0000186024

Regions

Domain4 – 8784GST N-terminal
Domain92 – 212121GST C-terminal
Region14 – 196Glutathione binding By similarity
Region71 – 722Glutathione binding By similarity
Region115 – 1173Glutathione binding By similarity

Sites

Binding site451Glutathione By similarity
Binding site591Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Binding site1111Glutathione By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue571N6-succinyllysine By similarity
Modified residue1361Phosphothreonine By similarity
Modified residue1771N6-succinyllysine By similarity
Modified residue1811Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P57113 [UniParc].

Last modified October 19, 2011. Version 2.
Checksum: 3E02041A8E3749A3

FASTA21623,961
        10         20         30         40         50         60 
MQAGKPVLYS YFRSSCSWRV RIALALKGID YEIVPINLIK DGGQQFSEEF QTLNPMKQVP 

        70         80         90        100        110        120 
ALKIDGITIG QSLAILEYLE ETRPIPRLLP QDPQKRAIVR MISDLIASGI QPLQNLSVLK 

       130        140        150        160        170        180 
QVGQENQMPW AQKAITSGFN ALEKILQSTA GKYCVGDEVS MADVCLAPQV ANAERFKVDL 

       190        200        210 
SPYPTISHIN KALLALEAFQ VSHPCRQPDT PAELRT 

« Hide

References

« Hide 'large scale' references
[1]"Microcystin-induced variations in transcription of GSTs in Wistar rat."
Li G., Xie P.
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[4]"Glutathione transferase zeta catalyses the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid."
Tong Z., Board P.G., Anders M.W.
Biochem. J. 331:371-374(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 131-158, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, BLOCKAGE OF N-TERMINUS.
Strain: Fischer 344.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ179410 mRNA. Translation: ACI32127.1.
CH473982 Genomic DNA. Translation: EDL81627.1.
BC158833 mRNA. Translation: AAI58834.1.
RefSeqNP_001102915.1. NM_001109445.1.
UniGeneRn.216913.

3D structure databases

ProteinModelPortalP57113.
SMRP57113. Positions 4-214.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP57113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000072215; ENSRNOP00000065390; ENSRNOG00000047708.
GeneID681913.
KEGGrno:681913.

Organism-specific databases

CTD2954.
RGD1589363. Gstz1.

Phylogenomic databases

GeneTreeENSGT00390000006580.
HOVERGENHBG001501.
KOK01800.
OMAKKRASVR.
OrthoDBEOG7TF79P.
PhylomeDBP57113.

Enzyme and pathway databases

UniPathwayUPA00139; UER00340.

Gene expression databases

GenevestigatorP57113.

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.
IPR004046. GST_C.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR01262. maiA. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio721886.

Entry information

Entry nameMAAI_RAT
AccessionPrimary (citable) accession number: P57113
Secondary accession number(s): B0BNI1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 19, 2011
Last modified: April 16, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways