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Protein

Maleylacetoacetate isomerase

Gene

Gstz1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

4-maleylacetoacetate = 4-fumarylacetoacetate.
RX + glutathione = HX + R-S-glutathione.

Cofactori

glutathioneBy similarityNote: Glutathione is required for the MAAI activity.By similarity

Pathway:iL-phenylalanine degradation

This protein is involved in step 5 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Phenylalanine-4-hydroxylase (Pah)
  2. Tyrosine aminotransferase (Tat)
  3. 4-hydroxyphenylpyruvate dioxygenase (Hpd)
  4. Homogentisate 1,2-dioxygenase (Hgd)
  5. Maleylacetoacetate isomerase (Gstz1)
  6. Fumarylacetoacetase (Fah)
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451Glutathione1 Publication
Binding sitei59 – 591Glutathione; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei111 – 1111Glutathione1 Publication

GO - Molecular functioni

GO - Biological processi

  • glutathione metabolic process Source: MGI
  • L-phenylalanine catabolic process Source: MGI
  • tyrosine catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Transferase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Enzyme and pathway databases

ReactomeiREACT_317599. Glutathione conjugation.
REACT_336040. Phenylalanine and tyrosine catabolism.
UniPathwayiUPA00139; UER00340.

Names & Taxonomyi

Protein namesi
Recommended name:
Maleylacetoacetate isomerase (EC:5.2.1.2)
Short name:
MAAI
Alternative name(s):
GSTZ1-1
Glutathione S-transferase zeta 1 (EC:2.5.1.18)
Gene namesi
Name:Gstz1
Synonyms:Maai
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1341859. Gstz1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 216216Maleylacetoacetate isomerasePRO_0000186023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei57 – 571N6-succinyllysine1 Publication
Modified residuei136 – 1361Phosphothreonine1 Publication
Modified residuei177 – 1771N6-succinyllysine1 Publication
Modified residuei181 – 1811Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9WVL0.
PaxDbiQ9WVL0.
PRIDEiQ9WVL0.

PTM databases

PhosphoSiteiQ9WVL0.

Expressioni

Tissue specificityi

Expressed in liver, kidney, seminal glands and breast.

Gene expression databases

BgeeiQ9WVL0.
ExpressionAtlasiQ9WVL0. baseline and differential.
GenevisibleiQ9WVL0. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiQ9WVL0. 5 interactions.
MINTiMINT-1859246.
STRINGi10090.ENSMUSP00000053540.

Structurei

Secondary structure

1
216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Helixi15 – 2612Combined sources
Beta strandi32 – 354Combined sources
Helixi40 – 423Combined sources
Helixi44 – 463Combined sources
Helixi48 – 536Combined sources
Beta strandi61 – 644Combined sources
Beta strandi67 – 715Combined sources
Helixi72 – 8211Combined sources
Helixi93 – 10917Combined sources
Helixi111 – 1144Combined sources
Helixi116 – 1227Combined sources
Turni124 – 1263Combined sources
Helixi127 – 14923Combined sources
Beta strandi150 – 1567Combined sources
Helixi161 – 17515Combined sources
Helixi184 – 19411Combined sources
Helixi197 – 2004Combined sources
Helixi204 – 2063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZ2X-ray1.40A1-216[»]
2CZ3X-ray2.30A/B1-216[»]
ProteinModelPortaliQ9WVL0.
SMRiQ9WVL0. Positions 4-214.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WVL0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8784GST N-terminalAdd
BLAST
Domaini92 – 212121GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 196Glutathione binding
Regioni71 – 722Glutathione binding
Regioni115 – 1173Glutathione binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00390000006580.
HOGENOMiHOG000125758.
HOVERGENiHBG001501.
InParanoidiQ9WVL0.
KOiK01800.
OMAiRAQVRMI.
OrthoDBiEOG7TF79P.
PhylomeDBiQ9WVL0.
TreeFamiTF105324.

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.
IPR004046. GST_C.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. 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.

Q9WVL0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAGKPILYS YFRSSCSWRV RIALALKGID YEIVPINLIK DGGQQFTEEF
60 70 80 90 100
QTLNPMKQVP ALKIDGITIV QSLAIMEYLE ETRPIPRLLP QDPQKRAIVR
110 120 130 140 150
MISDLIASGI QPLQNLSVLK QVGQENQMQW AQKVITSGFN ALEKILQSTA
160 170 180 190 200
GKYCVGDEVS MADVCLVPQV ANAERFKVDL SPYPTISHIN KELLALEVFQ
210
VSHPRRQPDT PAELRT
Length:216
Mass (Da):24,275
Last modified:November 1, 1999 - v1
Checksum:iBDB1E6C07981E855
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093418 mRNA. Translation: AAD43846.1.
AK002398 mRNA. Translation: BAB22070.1.
AK075927 mRNA. Translation: BAC36059.1.
BC031777 mRNA. Translation: AAH31777.1.
CCDSiCCDS26071.1.
RefSeqiNP_001239484.1. NM_001252555.1.
NP_001239485.1. NM_001252556.1.
NP_034493.1. NM_010363.4.
UniGeneiMm.29652.

Genome annotation databases

EnsembliENSMUST00000063117; ENSMUSP00000053540; ENSMUSG00000021033.
GeneIDi14874.
KEGGimmu:14874.
UCSCiuc007oil.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093418 mRNA. Translation: AAD43846.1.
AK002398 mRNA. Translation: BAB22070.1.
AK075927 mRNA. Translation: BAC36059.1.
BC031777 mRNA. Translation: AAH31777.1.
CCDSiCCDS26071.1.
RefSeqiNP_001239484.1. NM_001252555.1.
NP_001239485.1. NM_001252556.1.
NP_034493.1. NM_010363.4.
UniGeneiMm.29652.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZ2X-ray1.40A1-216[»]
2CZ3X-ray2.30A/B1-216[»]
ProteinModelPortaliQ9WVL0.
SMRiQ9WVL0. Positions 4-214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVL0. 5 interactions.
MINTiMINT-1859246.
STRINGi10090.ENSMUSP00000053540.

PTM databases

PhosphoSiteiQ9WVL0.

Proteomic databases

MaxQBiQ9WVL0.
PaxDbiQ9WVL0.
PRIDEiQ9WVL0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000063117; ENSMUSP00000053540; ENSMUSG00000021033.
GeneIDi14874.
KEGGimmu:14874.
UCSCiuc007oil.1. mouse.

Organism-specific databases

CTDi2954.
MGIiMGI:1341859. Gstz1.

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00390000006580.
HOGENOMiHOG000125758.
HOVERGENiHBG001501.
InParanoidiQ9WVL0.
KOiK01800.
OMAiRAQVRMI.
OrthoDBiEOG7TF79P.
PhylomeDBiQ9WVL0.
TreeFamiTF105324.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00340.
ReactomeiREACT_317599. Glutathione conjugation.
REACT_336040. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

ChiTaRSiGstz1. mouse.
EvolutionaryTraceiQ9WVL0.
NextBioi287149.
PROiQ9WVL0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVL0.
ExpressionAtlasiQ9WVL0. baseline and differential.
GenevisibleiQ9WVL0. MM.

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.
IPR004046. GST_C.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. 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...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-136 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-57 AND LYS-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "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.

Entry informationi

Entry nameiMAAI_MOUSE
AccessioniPrimary (citable) accession number: Q9WVL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.