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Protein

Probable maleylacetoacetate isomerase 1

Gene

GstZ1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid in vitro. Possesses low glutathione thioltransferase activity toward 4-hydroxynonenal (4-HNE). Has no glutathione thioltransferase activity with adrenochrome, phenethyl isothiocyanate (PEITC), 5-hydroperoxyeicosatetraenoic acid ((5S)-HpETE), prostaglandin A2 (PGA2) or 2-hydroxyethyldisulfide (HED).1 Publication

Catalytic activityi

4-maleylacetoacetate = 4-fumarylacetoacetate.1 Publication
RX + glutathione = HX + R-S-glutathione.1 Publication

Cofactori

glutathione1 PublicationNote: Glutathione is required for the MAAI activity.1 Publication

Pathway: L-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. Protein henna (Hn)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Homogentisate 1,2-dioxygenase (hgo)
  5. Probable maleylacetoacetate isomerase 1 (GstZ1), Probable maleylacetoacetate isomerase 2 (GstZ2)
  6. no protein annotated in this organism
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 sitei88 – 881Glutathione; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei140 – 1401GlutathioneBy similarity

GO - Molecular functioni

  • glutathione transferase activity Source: FlyBase
  • maleylacetoacetate isomerase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Transferase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Enzyme and pathway databases

ReactomeiREACT_277980. Glutathione conjugation.
REACT_327548. Phenylalanine and tyrosine catabolism.
UniPathwayiUPA00139; UER00340.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable maleylacetoacetate isomerase 1 (EC:5.2.1.2)
Short name:
MAAI 1
Alternative name(s):
Glutathione S-transferase zeta 1 (EC:2.5.1.18)
Gene namesi
Name:GstZ1
ORF Names:CG9362
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0037696. GstZ1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246Probable maleylacetoacetate isomerase 1PRO_0000186026Add
BLAST

Proteomic databases

PaxDbiQ9VHD3.
PRIDEiQ9VHD3.

Expressioni

Developmental stagei

Expressed during embryogenesis.1 Publication

Gene expression databases

BgeeiQ9VHD3.
GenevisibleiQ9VHD3. DM.

Interactioni

Protein-protein interaction databases

BioGridi66293. 2 interactions.
STRINGi7227.FBpp0081522.

Structurei

3D structure databases

ProteinModelPortaliQ9VHD3.
SMRiQ9VHD3. Positions 33-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 11685GST N-terminalAdd
BLAST
Domaini121 – 241121GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 476Glutathione bindingBy similarity
Regioni100 – 1012Glutathione bindingBy similarity
Regioni144 – 1463Glutathione bindingBy similarity

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.
InParanoidiQ9VHD3.
KOiK01800.
OMAiEYRAVTR.
OrthoDBiEOG7TF79P.
PhylomeDBiQ9VHD3.

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.

Q9VHD3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASATQLTHR GIHLAGLYRS SWSKPLFRHL ATKPILYSYW PSSCSWRVRV
60 70 80 90 100
ALAIKKIDYD IKPTSLLKTV SGHAYTDEYR EVNPMQKVPS LKIDGHTLCD
110 120 130 140 150
SVAIIHYLEE TRPQPALLPQ DPVKRAKIRE IVELICSGIQ PLQNVSVLDH
160 170 180 190 200
IGKDQSLQWA QHWISRGFQG LEKVLSHSAG KFCVGDELSM ADICLVPQVR
210 220 230 240
NARRYKADLT PYPTIVRLNQ ELQELDVFKA THPSTQPDCP PEFAKK
Length:246
Mass (Da):27,890
Last modified:May 1, 2000 - v1
Checksum:i9DEBC10717E380E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54381.1.
AY061527 mRNA. Translation: AAL29075.1.
RefSeqiNP_649894.1. NM_141637.3.
UniGeneiDm.3568.

Genome annotation databases

EnsemblMetazoaiFBtr0082044; FBpp0081522; FBgn0037696.
GeneIDi41132.
KEGGidme:Dmel_CG9362.
UCSCiCG9362-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54381.1.
AY061527 mRNA. Translation: AAL29075.1.
RefSeqiNP_649894.1. NM_141637.3.
UniGeneiDm.3568.

3D structure databases

ProteinModelPortaliQ9VHD3.
SMRiQ9VHD3. Positions 33-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66293. 2 interactions.
STRINGi7227.FBpp0081522.

Proteomic databases

PaxDbiQ9VHD3.
PRIDEiQ9VHD3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082044; FBpp0081522; FBgn0037696.
GeneIDi41132.
KEGGidme:Dmel_CG9362.
UCSCiCG9362-RA. d. melanogaster.

Organism-specific databases

CTDi2954.
FlyBaseiFBgn0037696. GstZ1.

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00390000006580.
InParanoidiQ9VHD3.
KOiK01800.
OMAiEYRAVTR.
OrthoDBiEOG7TF79P.
PhylomeDBiQ9VHD3.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00340.
ReactomeiREACT_277980. Glutathione conjugation.
REACT_327548. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

GenomeRNAii41132.
NextBioi822330.
PROiQ9VHD3.

Gene expression databases

BgeeiQ9VHD3.
GenevisibleiQ9VHD3. DM.

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. "A preliminary characterization of the cytosolic glutathione transferase proteome from Drosophila melanogaster."
    Saisawang C., Wongsantichon J., Ketterman A.J.
    Biochem. J. 442:181-190(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DEVELOPMENTAL STAGE.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiMAAI1_DROME
AccessioniPrimary (citable) accession number: Q9VHD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.