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
//