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Database: UniProt
Entry: A8PRI6_MALGO
LinkDB: A8PRI6_MALGO
Original site: A8PRI6_MALGO 
ID   A8PRI6_MALGO            Unreviewed;       409 AA.
AC   A8PRI6;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE            EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
GN   ORFNames=MGL_0061 {ECO:0000313|EMBL:EDP45072.1};
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:EDP45072.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP45072.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC         L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00001871};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006904}.
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:EDP45072.1}.
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DR   EMBL; AAYY01000001; EDP45072.1; -; Genomic_DNA.
DR   RefSeq; XP_001732286.1; XM_001732234.1.
DR   AlphaFoldDB; A8PRI6; -.
DR   STRING; 425265.A8PRI6; -.
DR   GeneID; 5856592; -.
DR   KEGG; mgl:MGL_0061; -.
DR   VEuPathDB; FungiDB:MGL_0061; -.
DR   InParanoid; A8PRI6; -.
DR   OMA; AFVYFCD; -.
DR   OrthoDB; 1404347at2759; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT   DOMAIN          12..398
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   409 AA;  44872 MW;  3C9397CA1E90CF48 CRC64;
     MSTTPERERT VNLGAGPSKL STDVVLEASK AFIDYQGLGI GVAELSHRSD TFKTILANAE
     NDLRKLLDIP DNYAVLFMQG GGTEQFSSTL LNMLAAHAAK HGNNSNAGAS APPVDYVVSG
     AWSKKAVQEA RRLTSRVNVA SDMISMIGDP NAEIPSPDKW QLSPVDEYPA MLYYCENETI
     HGFEFPEHWI QRLPQAYRER VPIVADCSSN ILSRPIDVRA HGVIFFGAQK NVGPSGVTMV
     IVRRDLIVDP DALQASYVPP IPATLVYKNM ADNGSLYNTP PTFSIYVSGI GFRKLLLDGG
     VPAAQERARI KSELVYKTLD VFPHVYRPTV AHPAFRSKMN LTFRVLDRAS GEPSPDAEKR
     LVAFCREHHV VSIQGHRSVG GIRASLYNSV TIEEANKLAS LLKHFAEVN
//
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