ID   A0A061HH08_9BASI        Unreviewed;       493 AA.
AC   A0A061HH08;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN   ORFNames=PFL1_02593 {ECO:0000313|EMBL:EPQ29921.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ29921.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ29921.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ29921.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; KE361629; EPQ29921.1; -; Genomic_DNA.
DR   RefSeq; XP_007878300.1; XM_007880109.1.
DR   AlphaFoldDB; A0A061HH08; -.
DR   GeneID; 19316712; -.
DR   KEGG; pfp:PFL1_02593; -.
DR   eggNOG; KOG0634; Eukaryota.
DR   HOGENOM; CLU_017584_0_6_1; -.
DR   OrthoDB; 5486605at2759; -.
DR   Proteomes; UP000053664; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProt.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42790:SF3; KYNURENINE_ALPHA-AMINOADIPATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT   DOMAIN          129..396
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   493 AA;  53456 MW;  25ECF618BE873DD3 CRC64;
     MTAPTSASAK PIDYRSLLSQ TARNRMPSAI RSLYPAELIP DMISLLSGKP NAETFPFHRI
     LLELKPRGPD GIIETIPIEG ADLDVALQYG PTAGIPKLVD WVEEFQSRLH HRPRVTKAAP
     GVHGEAWRCS FGTGSQDLLT KTFEALTDPG DSVIVESPAY SGILPSLVSL KARIFEAHTD
     AEGVDPIYLE QLLSDWASAE ATRTSPFPKF IYTAPTGANP SGTTASEGRK RAVLSVARKH
     GLIILEDDPY YFLSFPGLGE DPVTRTRSKS YFALEQEEED QWGKGRVLRF DSFSKILSAG
     LRLGFCTGPT ELVDAIDADT SIRNLQPSGA SQGIALALLS RWGIDGFLRH ADSVAHFYKA
     RLDQFEAKAR HHLCASPSVA EWVTPSAGMF LWIKLKLPPT RPSDSGDGDV DEGDTLDLIG
     QKAKAAGVLA LPGVAFMPPP SATGAGLASG TKRTSPYVRT SFSIVPMERV DAAFERLRTV
     VVQAWQEAGL EMI
//