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Database: UniProt/TrEMBL
Entry: A8Q6D9_MALGO
LinkDB: A8Q6D9_MALGO
Original site: A8Q6D9_MALGO 
ID   A8Q6D9_MALGO            Unreviewed;       521 AA.
AC   A8Q6D9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDP42735.1};
GN   ORFNames=MGL_2935 {ECO:0000313|EMBL:EDP42735.1};
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP42735.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP42735.1, ECO:0000313|Proteomes:UP000008837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP42735.1}.
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DR   EMBL; AAYY01000010; EDP42735.1; -; Genomic_DNA.
DR   RefSeq; XP_001729949.1; XM_001729897.1.
DR   AlphaFoldDB; A8Q6D9; -.
DR   STRING; 425265.A8Q6D9; -.
DR   GeneID; 5854256; -.
DR   KEGG; mgl:MGL_2935; -.
DR   VEuPathDB; FungiDB:MGL_2935; -.
DR   InParanoid; A8Q6D9; -.
DR   OMA; ENPECTN; -.
DR   OrthoDB; 51460at2759; -.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008837}.
FT   REGION          365..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         328
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   521 AA;  56004 MW;  BF2C7036F7072964 CRC64;
     MTSSTPLRAE HAATELDRLG TKCLALVTEW VSQGQDSRTL AAPWPDASSF RSSIDVCVPE
     EGVSENTLFA KIRAILHNSV NPWTHRFLEK LYSAPAVISI MGDLLLGVMN ASVHVFSASP
     ILTMIEEQCA AALCERVGYT AADADGLCMP GGAASNTFAV QTALSQLFGG VYRHGGVCAL
     VDAYTQHKGR IGRGARPAIL VSADAHFSLS RAALAAGLGT DAVVPIAVDK HGKMDTSELV
     RVCLEMEQEP AHTRGVPMMI CATSGTTVLG AFDDLCTIAH ICRRFACWMH VDASWGGAMV
     FLPSDAPARA CRLDGLQEAN SITINPHKLL GVTHQCSFLL VKNKLVLQVA SLTEDAGYLF
     HDASTSSSVS SSSPSSSSSQ PPRPLVNDMA AKTLGCGRRG DALKLYLVWL RYGTHGLSEH
     IQHGLYMAQL ILARIEQTPT LELGPLAKPL FLQICFRPRF GGPDATRRMH AKLKASGQYV
     VDYAPVHEMG DFMRLVVHPT TPLHVYEALI DTLGDMVDST L
//
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