ID A0A1Y1UEM9_9TREE Unreviewed; 423 AA.
AC A0A1Y1UEM9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Pyridoxal phosphate-dependent transferase {ECO:0000313|EMBL:ORX35525.1};
GN ORFNames=BD324DRAFT_630474 {ECO:0000313|EMBL:ORX35525.1};
OS Kockovaella imperatae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cuniculitremaceae; Kockovaella.
OX NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX35525.1, ECO:0000313|Proteomes:UP000193218};
RN [1] {ECO:0000313|EMBL:ORX35525.1, ECO:0000313|Proteomes:UP000193218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX35525.1,
RC ECO:0000313|Proteomes:UP000193218};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRNR:PIRNR000517, ECO:0000256|PIRSR:PIRSR000517-1};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|PIRNR:PIRNR000517}.
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:ORX35525.1}.
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DR EMBL; NBSH01000010; ORX35525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1UEM9; -.
DR STRING; 4999.A0A1Y1UEM9; -.
DR InParanoid; A0A1Y1UEM9; -.
DR OrthoDB; 5474881at2759; -.
DR Proteomes; UP000193218; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
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 InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR005958; TyrNic_aminoTrfase.
DR NCBIfam; TIGR01265; tyr_nico_aTase; 1.
DR PANTHER; PTHR45744; TYROSINE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR45744:SF2; TYROSINE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR000517};
KW Reference proteome {ECO:0000313|Proteomes:UP000193218};
KW Transferase {ECO:0000313|EMBL:ORX35525.1}.
FT DOMAIN 50..412
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 263
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000517-1"
SQ SEQUENCE 423 AA; 45940 MW; 1DD2E8D953C87656 CRC64;
MPYIEDIIMP PAMASARDQW DIRASSLLSK NPIRATLAAV TGTPPDSDQP VINLALGDPT
SSNLYPPPPS TISAITRVVQ TSSSNGYLHG SGSLEARQAV CEYHAKWDKV DYSPSAVILT
HGASHALDMI FNVVVPPSTS TYRPNLLIPR PGFALYRTQL QSLGVEIREY ECLPDRDWEI
NLIDLARCCD ENTVGILVTN PSNPCGSNFS RSHLQDIIHV AERAKVPIIA DEIYAHMTWD
SDFVPMARLS SSVPIFTLSG LSKRFLLPGW RFGWVVVHDP AGLATAVTDG LHMLANRILG
PNSLVQAALP EILETPGDWF EGLTSILARN AKITHEGING IYGLVASAPR GAMYLLIGIS
SAFNLDDIEF SRLLYKEQAL FVLPGSCFGA AGYFRISLAS TADALDEAVR RIGVFSSIHC
LPA
//