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Q9VHD3 (MAAI1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Probable maleylacetoacetate isomerase 1

Short name=MAAI 1
EC=5.2.1.2
Alternative name(s):
Glutathione S-transferase zeta 1
EC=2.5.1.18
Gene names
Name:GstZ1
ORF Names:CG9362
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1

Catalytic activity

4-maleylacetoacetate = 4-fumarylacetoacetate. Ref.1

RX + glutathione = HX + R-S-glutathione. Ref.1

Cofactor

Glutathione. Required for the MAAI activity. Ref.1

Pathway

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

Subcellular location

Cytoplasm By similarity.

Developmental stage

Expressed during embryogenesis. Ref.1

Sequence similarities

Belongs to the GST superfamily. Zeta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Probable maleylacetoacetate isomerase 1
PRO_0000186026

Regions

Domain32 – 11685GST N-terminal
Domain121 – 241121GST C-terminal
Region42 – 476Glutathione binding By similarity
Region100 – 1012Glutathione binding By similarity
Region144 – 1463Glutathione binding By similarity

Sites

Binding site881Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Binding site1401Glutathione By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9VHD3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 9DEBC10717E380E4

FASTA24627,890
        10         20         30         40         50         60 
MASATQLTHR GIHLAGLYRS SWSKPLFRHL ATKPILYSYW PSSCSWRVRV ALAIKKIDYD 

        70         80         90        100        110        120 
IKPTSLLKTV SGHAYTDEYR EVNPMQKVPS LKIDGHTLCD SVAIIHYLEE TRPQPALLPQ 

       130        140        150        160        170        180 
DPVKRAKIRE IVELICSGIQ PLQNVSVLDH IGKDQSLQWA QHWISRGFQG LEKVLSHSAG 

       190        200        210        220        230        240 
KFCVGDELSM ADICLVPQVR NARRYKADLT PYPTIVRLNQ ELQELDVFKA THPSTQPDCP 


PEFAKK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014297 Genomic DNA. Translation: AAF54381.1.
AY061527 mRNA. Translation: AAL29075.1.
RefSeqNP_649894.1. NM_141637.3.
UniGeneDm.3568.

3D structure databases

ProteinModelPortalQ9VHD3.
SMRQ9VHD3. Positions 33-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66293. 2 interactions.
STRING7227.FBpp0081522.

Proteomic databases

PaxDbQ9VHD3.
PRIDEQ9VHD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082044; FBpp0081522; FBgn0037696.
GeneID41132.
KEGGdme:Dmel_CG9362.
UCSCCG9362-RA. d. melanogaster.

Organism-specific databases

CTD2954.
FlyBaseFBgn0037696. GstZ1.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00390000006580.
InParanoidQ9VHD3.
KOK01800.
OMARVRTFLM.
OrthoDBEOG7TF79P.
PhylomeDBQ9VHD3.

Enzyme and pathway databases

UniPathwayUPA00139; UER00340.

Gene expression databases

BgeeQ9VHD3.

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

GenomeRNAi41132.
NextBio822330.

Entry information

Entry nameMAAI1_DROME
AccessionPrimary (citable) accession number: Q9VHD3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase