MAIA_ASPFU
ID MAIA_ASPFU Reviewed; 231 AA.
AC Q4WHT7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Maleylacetoacetate isomerase maiA {ECO:0000303|PubMed:19028908};
DE EC=5.2.1.2 {ECO:0000305|PubMed:19028908};
GN Name=maiA {ECO:0000303|PubMed:19028908}; ORFNames=AFUA_2G04240;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=19028908; DOI=10.1128/aem.02077-08;
RA Schmaler-Ripcke J., Sugareva V., Gebhardt P., Winkler R., Kniemeyer O.,
RA Heinekamp T., Brakhage A.A.;
RT "Production of pyomelanin, a second type of melanin, via the tyrosine
RT degradation pathway in Aspergillus fumigatus.";
RL Appl. Environ. Microbiol. 75:493-503(2009).
RN [3]
RP FUNCTION.
RX PubMed=19715768; DOI=10.1016/j.fgb.2009.08.005;
RA Valiante V., Jain R., Heinekamp T., Brakhage A.A.;
RT "The MpkA MAP kinase module regulates cell wall integrity signaling and
RT pyomelanin formation in Aspergillus fumigatus.";
RL Fungal Genet. Biol. 46:909-918(2009).
RN [4]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=22046314; DOI=10.1371/journal.pone.0026604;
RA Keller S., Macheleidt J., Scherlach K., Schmaler-Ripcke J., Jacobsen I.D.,
RA Heinekamp T., Brakhage A.A.;
RT "Pyomelanin formation in Aspergillus fumigatus requires HmgX and the
RT transcriptional activator HmgR but is dispensable for virulence.";
RL PLoS ONE 6:e26604-e26604(2011).
CC -!- FUNCTION: Maleylacetoacetate isomerase; part of the L-tyrosine
CC degradation gene cluster that mediates the biosynthesis of the brownish
CC pigment pyomelanin as an alternative melanin (PubMed:19028908,
CC PubMed:22046314). The 4-hydroxyphenylpyruvate dioxygenase hppD
CC catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisic
CC acid (HGA) (PubMed:19028908, PubMed:22046314). The protein hmgX is
CC crucial for this conversion and thus, probably functions as an
CC accessory factor to mediate specific activity of hppD
CC (PubMed:22046314). The homogentisate 1,2-dioxygenase hmgA is then
CC involved in the cleavage of the aromatic ring of HGA and its conversion
CC to 4-maleylacetoacetate (PubMed:19028908, PubMed:19715768). When hmgA
CC activity is lowered by the cell wall integrity (CWI) signaling pathway,
CC HGA accumulates and leads to the production of pyomelanin through
CC benzoquinone acetic acid after oxidation and polymerization
CC (PubMed:19715768). On the opposite, in non-stress conditions, both hppD
CC and hmgA activities are balanced and HGA is degraded into 4-
CC maleylacetoacetate (PubMed:19715768). 4-maleylacetoacetate is further
CC converted to 4-fumarylacetoacetate by the maleylacetoacetate isomerase
CC maiA, which is degraded into fumarate and acetoacetate by the
CC fumarylacetoacetase fahA (Probable). {ECO:0000269|PubMed:19028908,
CC ECO:0000269|PubMed:19715768, ECO:0000269|PubMed:22046314,
CC ECO:0000305|PubMed:19028908}.
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; Evidence={ECO:0000305|PubMed:19028908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14818;
CC Evidence={ECO:0000305|PubMed:19028908};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 5/6.
CC {ECO:0000305|PubMed:19028908}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor hmgR. {ECO:0000269|PubMed:22046314}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR EMBL; AAHF01000008; EAL87518.1; -; Genomic_DNA.
DR RefSeq; XP_749556.1; XM_744463.1.
DR SMR; Q4WHT7; -.
DR STRING; 746128.CADAFUBP00002080; -.
DR EnsemblFungi; EAL87518; EAL87518; AFUA_2G04240.
DR GeneID; 3507124; -.
DR KEGG; afm:AFUA_2G04240; -.
DR VEuPathDB; FungiDB:Afu2g04240; -.
DR eggNOG; KOG0868; Eukaryota.
DR HOGENOM; CLU_011226_20_0_1; -.
DR InParanoid; Q4WHT7; -.
DR OMA; VYNAHRF; -.
DR OrthoDB; 1283865at2759; -.
DR UniPathway; UPA00139; UER00340.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0016034; F:maleylacetoacetate isomerase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
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; PF00043; GST_C; 1.
DR Pfam; PF13409; GST_N_2; 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 2: Evidence at transcript level;
KW Isomerase; Reference proteome.
FT CHAIN 1..231
FT /note="Maleylacetoacetate isomerase maiA"
FT /id="PRO_0000453190"
FT DOMAIN 7..93
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 102..224
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ SEQUENCE 231 AA; 25311 MW; 59D803EFB60EA236 CRC64;
MEDSTSPKVT LYTYFRSSCS ARLRIALNLK SIPYTPIAVN LLKGEQSSPE NIALNPSGTV
PTLIVEHDSK EPVTITQSLA ALEYLEEITP ASSHALLPPA SNPEARAVVR TLVDIMSCDV
QPVTNLRILK RVAPFGVDRA AWSKDLIEDG FRAYEAIAAK SAGLFSVGDS ITMADVCLLP
AVWGAERAGV KVEKFPTIYR VAQRLEEEDA VKRAHWRTQP DTPEEFRVSS S
