ID A8PUK0_MALGO Unreviewed; 232 AA.
AC A8PUK0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 08-NOV-2023, entry version 66.
DE RecName: Full=Aminotransferase class V domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MGL_0703 {ECO:0000313|EMBL:EDP44896.1};
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:EDP44896.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44896.1, 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|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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:EDP44896.1}.
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DR EMBL; AAYY01000002; EDP44896.1; -; Genomic_DNA.
DR RefSeq; XP_001732110.1; XM_001732058.1.
DR AlphaFoldDB; A8PUK0; -.
DR STRING; 425265.A8PUK0; -.
DR GeneID; 5856416; -.
DR KEGG; mgl:MGL_0703; -.
DR VEuPathDB; FungiDB:MGL_0703; -.
DR InParanoid; A8PUK0; -.
DR OMA; HEVIHKY; -.
DR OrthoDB; 5482552at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR11808:SF35; CYSTATHIONINE GAMMA-SYNTHASE (AFU_ORTHOLOGUE AFUA_7G01590); 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837}.
SQ SEQUENCE 232 AA; 25453 MW; D05792A40CA93E0E CRC64;
MTKPTFPDPP KLDTLVLHAD QPDETKDEAF PVAPSISMST TFRQPHPDST LARNADNLES
APDVAPYHVY SRYTQDTRTR AERVISGILG AHSLLYSSGL SASDSLLDFC LPSVIAIREG
YFGVHEVIHK YCRGRNVKVI DLDDEYPVLA GVPAENESNI SQGKLLVWLE TPLNPTGEAR
DIEHYANRAR AANGYLVVDA TLAPPPLMDP FLHGADFVVH SGTKYLADIP IC
//