MAAI_DICDI
ID MAAI_DICDI Reviewed; 219 AA.
AC Q54YN2;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Maleylacetoacetate isomerase;
DE Short=MAAI;
DE EC=5.2.1.2;
GN Name=mai; ORFNames=DDB_G0278155;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-maleylacetoacetate = 4-fumarylacetoacetate;
CC Xref=Rhea:RHEA:14817, ChEBI:CHEBI:17105, ChEBI:CHEBI:18034;
CC EC=5.2.1.2;
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 5/6.
CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68250.1; -; Genomic_DNA.
DR RefSeq; XP_642170.1; XM_637078.1.
DR AlphaFoldDB; Q54YN2; -.
DR SMR; Q54YN2; -.
DR STRING; 44689.DDB0231608; -.
DR PaxDb; Q54YN2; -.
DR EnsemblProtists; EAL68250; EAL68250; DDB_G0278155.
DR GeneID; 8621377; -.
DR KEGG; ddi:DDB_G0278155; -.
DR dictyBase; DDB_G0278155; mai.
DR eggNOG; KOG0868; Eukaryota.
DR HOGENOM; CLU_011226_20_1_1; -.
DR InParanoid; Q54YN2; -.
DR OMA; VYNAHRF; -.
DR PhylomeDB; Q54YN2; -.
DR Reactome; R-DDI-156590; Glutathione conjugation.
DR Reactome; R-DDI-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-DDI-8963684; Tyrosine catabolism.
DR UniPathway; UPA00139; UER00340.
DR PRO; PR:Q54YN2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:dictyBase.
DR GO; GO:0016034; F:maleylacetoacetate isomerase activity; ISS:dictyBase.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR CDD; cd03191; GST_C_Zeta; 1.
DR CDD; cd03042; GST_N_Zeta; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR005955; GST_Zeta.
DR InterPro; IPR034330; GST_Zeta_C.
DR InterPro; IPR034333; GST_Zeta_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01262; maiA; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Isomerase; Phenylalanine catabolism; Reference proteome; Transferase;
KW Tyrosine catabolism.
FT CHAIN 1..219
FT /note="Maleylacetoacetate isomerase"
FT /id="PRO_0000388776"
FT DOMAIN 4..87
FT /note="GST N-terminal"
FT DOMAIN 92..217
FT /note="GST C-terminal"
FT BINDING 14..19
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 71..72
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 115..117
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 219 AA; 24865 MW; 41B5D24CB8D508B1 CRC64;
MTENKTVLYS YWRSSCSWRV RVALAYKKIK YEYKAIHLLK DGGQQKSDEY SKLNPMKAIP
TLEIDGHIIG QSLAILEYLE ETHPENPLMP KGSYERAIAR QMMQIIGSDI QPLQNLKVLG
LIAQYSGDDS KKSEWARTVI TNGFNGLEKL LEKHSGKFCV GDSVSFADLC LPAQVYNANR
FNVDMTPYPN ITRVNQHLLT IPEFIEALPQ NQPDAEPQC
