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Q9VHD2 (MAAI2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable maleylacetoacetate isomerase 2

Short name=MAAI 2
EC=5.2.1.2
Alternative name(s):
Glutathione S-transferase zeta 2
EC=2.5.1.18
Gene names
Name:GstZ2
ORF Names:CG9363
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length227 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. Has no glutathione thioltransferase activity with 4-hydroxynonenal (4-HNE), 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.

Sequence caution

The sequence AAL28280.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AEV23904.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processPhenylalanine catabolism
Tyrosine catabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionIsomerase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-phenylalanine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

glutathione metabolic process

Inferred from direct assay Ref.1. Source: FlyBase

tyrosine catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from direct assay Ref.1. Source: FlyBase

maleylacetoacetate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9VHD2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q9VHD2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSTNLCPNASSSDIQ → MSLSAIAK
Isoform C (identifier: Q9VHD2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSTNLCPNASSSDIQ → MNH

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Probable maleylacetoacetate isomerase 2
PRO_0000186027

Regions

Domain14 – 9784GST N-terminal
Domain102 – 222121GST C-terminal
Region24 – 296Glutathione binding By similarity
Region81 – 822Glutathione binding By similarity
Region125 – 1273Glutathione binding By similarity

Sites

Binding site551Glutathione By similarity
Binding site691Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Binding site1211Glutathione By similarity

Natural variations

Alternative sequence1 – 1515MSTNL…SSDIQ → MSLSAIAK in isoform B.
VSP_010291
Alternative sequence1 – 1515MSTNL…SSDIQ → MNH in isoform C.
VSP_010292

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C708DD764F48C754

FASTA22725,975
        10         20         30         40         50         60 
MSTNLCPNAS SSDIQPILYS YWRSSCSWRV RIAMNLKEIP YDIKPISLIK SGGEQHCNEY 

        70         80         90        100        110        120 
REVNPMEQVP ALQIDGHTLI ESVAIMHYLE ETRPQRPLLP QDVHKRAKVR EIVEIICSGI 

       130        140        150        160        170        180 
QPLQNLIVLI HVGEEKKKEW AQHWITRGFR AVEKALSTSA GKYCVGDEIS MADCCLVPQV 

       190        200        210        220 
FNARRFHVDL RPYPIILRID RELESNPAFR AAHPSNQPDC PPELPNK 

« Hide

Isoform B [UniParc].

Checksum: DABCE0A9315EA989
Show »

FASTA22025,227
Isoform C [UniParc].

Checksum: 86D4F06DCD77B834
Show »

FASTA21524,808

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, ALTERNATIVE SPLICING.
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] (ISOFORM A).
Strain: Berkeley.
Tissue: Ovary.
[5]Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014297 Genomic DNA. Translation: AAF54382.1.
AE014297 Genomic DNA. Translation: AAN13429.1.
AE014297 Genomic DNA. Translation: AAS65133.1.
AY060732 mRNA. Translation: AAL28280.2. Different initiation.
BT132880 mRNA. Translation: AEV23904.1. Different initiation.
BT133289 mRNA. Translation: AFC88878.1.
RefSeqNP_649895.1. NM_141638.3.
NP_731358.1. NM_169286.2.
NP_996190.1. NM_206468.2.
UniGeneDm.1121.

3D structure databases

ProteinModelPortalQ9VHD2.
SMRQ9VHD2. Positions 15-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66294. 1 interaction.
DIPDIP-24005N.
IntActQ9VHD2. 1 interaction.
MINTMINT-1563429.

Proteomic databases

PaxDbQ9VHD2.
PRIDEQ9VHD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082041; FBpp0081519; FBgn0037697. [Q9VHD2-2]
FBtr0082042; FBpp0081520; FBgn0037697. [Q9VHD2-1]
GeneID41133.
KEGGdme:Dmel_CG9363.
UCSCCG9363-RA. d. melanogaster. [Q9VHD2-1]

Organism-specific databases

CTD41133.
FlyBaseFBgn0037697. GstZ2.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00390000006580.
InParanoidQ9VHD2.
KOK01800.
OMAKKRASVR.
OrthoDBEOG7TF79P.
PhylomeDBQ9VHD2.

Enzyme and pathway databases

UniPathwayUPA00139; UER00340.

Gene expression databases

BgeeQ9VHD2.

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

GenomeRNAi41133.
NextBio822335.

Entry information

Entry nameMAAI2_DROME
AccessionPrimary (citable) accession number: Q9VHD2
Secondary accession number(s): H0RNF8, H8F4P9, Q8INN9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 120 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