HMGX_ASPFU
ID HMGX_ASPFU Reviewed; 256 AA.
AC Q4WHU0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 23-FEB-2022, entry version 68.
DE RecName: Full=L-tyrosine degradation gene cluster protein hmgX {ECO:0000303|PubMed:22046314};
DE AltName: Full=Pyomelanin biosynthesis cluster protein hmgX {ECO:0000303|PubMed:22046314};
GN Name=hmgX {ECO:0000303|PubMed:22046314}; ORFNames=AFUA_2G04210;
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.
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, DISRUPTION PHENOTYPE, INDUCTION, AND SUBCELLULAR LOCATION.
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: Part of the L-tyrosine degradation gene cluster that mediates
CC the biosynthesis of the brownish pigment pyomelanin as an alternative
CC melanin (PubMed:19028908, PubMed:22046314). The 4-hydroxyphenylpyruvate
CC dioxygenase hppD catalyzes the conversion of 4-hydroxyphenylpyruvate to
CC homogentisic acid (HGA) (PubMed:19028908, PubMed:22046314). The protein
CC hmgX is 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22046314}.
CC -!- INDUCTION: Expression is induced by L-tyrosine (PubMed:22046314).
CC Expression is positively regulated by the cluster-specific
CC transcription factor hmgR (PubMed:22046314).
CC {ECO:0000269|PubMed:22046314}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth on L-tyrosine as the sole carbon
CC source and affects homogentisic acid and pyomelanin formation.
CC {ECO:0000269|PubMed:19028908}.
CC -!- SIMILARITY: Belongs to the TTC36 family. {ECO:0000305}.
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DR EMBL; AAHF01000008; EAL87515.1; -; Genomic_DNA.
DR RefSeq; XP_749553.1; XM_744460.1.
DR STRING; 746128.CADAFUBP00002077; -.
DR EnsemblFungi; EAL87515; EAL87515; AFUA_2G04210.
DR GeneID; 3507121; -.
DR KEGG; afm:AFUA_2G04210; -.
DR VEuPathDB; FungiDB:Afu2g04210; -.
DR eggNOG; KOG4555; Eukaryota.
DR HOGENOM; CLU_074601_0_0_1; -.
DR InParanoid; Q4WHU0; -.
DR OMA; AHTHRAY; -.
DR OrthoDB; 1597848at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IDA:AspGD.
DR GO; GO:0006583; P:melanin biosynthetic process from tyrosine; IMP:AspGD.
DR GO; GO:0006572; P:tyrosine catabolic process; IMP:AspGD.
DR InterPro; IPR038906; TTC36.
DR PANTHER; PTHR21405; PTHR21405; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..256
FT /note="L-tyrosine degradation gene cluster protein hmgX"
FT /id="PRO_0000453193"
SQ SEQUENCE 256 AA; 27644 MW; 1F11CC0EB2944A23 CRC64;
MASGTTIQPS RPSLTSNDSA VLQALFDAES SPSSAVAIDP SLSPFPEYLH ISASDHESLK
ARELSIIRSL QSDDVSMDTI TSAIRDLDAL ITEHPTYPSA YVNRAQALRL HIEKTAEAST
DPEEAIFTPG NTESASRLFS DLGQAISLCT PRSPADPVST VQARILADSH THRGYLLLKA
ARLKKNANGN EMVGGPDKLR DMGPDQLEEM ASRDFFFGGR YGNKVAQQLA VQTNPYAKMC
GAIVKEALRK EVEGVI
