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Q9WVL0 (MAAI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:Maai
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid By similarity.

Catalytic activity

4-maleylacetoacetate = 4-fumarylacetoacetate.

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

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 Probable. Ref.4

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed in liver, kidney, seminal glands and breast.

Sequence similarities

Belongs to the GST superfamily. Zeta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216Maleylacetoacetate isomerase
PRO_0000186023

Regions

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

Sites

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

Secondary structure

1 .................................... 216
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WVL0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: BDB1E6C07981E855

FASTA21624,275
        10         20         30         40         50         60 
MQAGKPILYS YFRSSCSWRV RIALALKGID YEIVPINLIK DGGQQFTEEF QTLNPMKQVP 

        70         80         90        100        110        120 
ALKIDGITIV QSLAIMEYLE ETRPIPRLLP QDPQKRAIVR MISDLIASGI QPLQNLSVLK 

       130        140        150        160        170        180 
QVGQENQMQW AQKVITSGFN ALEKILQSTA GKYCVGDEVS MADVCLVPQV ANAERFKVDL 

       190        200        210 
SPYPTISHIN KELLALEVFQ VSHPRRQPDT PAELRT

« Hide

References

« Hide 'large scale' references
[1]"Gene structure, chromosomal location, and expression pattern of maleylacetoacetate isomerase."
Fernandez-Canon J.M., Hejna J., Reifsteck C., Olson S., Grompe M.
Genomics 58:263-269(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[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].
Strain: FVB/N.
Tissue: Salivary gland.
[4]"Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate isomerase) from Mus musculus (form-1 crystal)."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF093418 mRNA. Translation: AAD43846.1.
AK002398 mRNA. Translation: BAB22070.1.
AK075927 mRNA. Translation: BAC36059.1.
BC031777 mRNA. Translation: AAH31777.1.
IPIIPI00126120.
RefSeqNP_001239484.1. NM_001252555.1.
NP_001239485.1. NM_001252556.1.
NP_034493.1. NM_010363.4.
UniGeneMm.29652.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZ2X-ray1.40A1-216[»]
2CZ3X-ray2.30A/B1-216[»]
ProteinModelPortalQ9WVL0.
SMRQ9WVL0. Positions 4-214.
ModBaseSearch...

PTM databases

PhosphoSiteQ9WVL0.

Proteomic databases

PaxDbQ9WVL0.
PRIDEQ9WVL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063117; ENSMUSP00000053540; ENSMUSG00000021033.
GeneID14874.
KEGGmmu:14874.
UCSCuc007oil.1. mouse.

Organism-specific databases

CTD2954.
MGIMGI:1341859. Gstz1.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00390000006580.
HOGENOMHOG000125758.
HOVERGENHBG001501.
InParanoidQ9WVL0.
KOK01800.
OMARAQVRMI.
OrthoDBEOG4BG8X2.

Enzyme and pathway databases

UniPathwayUPA00139; UER00340.

Gene expression databases

ArrayExpressQ9WVL0.
BgeeQ9WVL0.
GenevestigatorQ9WVL0.
GermOnlineENSMUSG00000021033. Mus musculus.

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.
IPR004046. GST_C.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
[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

ChiTaRSGSTZ1. mouse.
EvolutionaryTraceQ9WVL0.
NextBio287149.
SOURCESearch...

Entry information

Entry nameMAAI_MOUSE
AccessionPrimary (citable) accession number: Q9WVL0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: April 3, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents