ID A0A395NWM4_TRIAR Unreviewed; 369 AA.
AC A0A395NWM4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 08-NOV-2023, entry version 15.
DE SubName: Full=Branched-chain amino acid aminotransferase ii {ECO:0000313|EMBL:RFU80499.1};
GN ORFNames=TARUN_1710 {ECO:0000313|EMBL:RFU80499.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU80499.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU80499.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU80499.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
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:RFU80499.1}.
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DR EMBL; PXOA01000106; RFU80499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NWM4; -.
DR STRING; 490622.A0A395NWM4; -.
DR Proteomes; UP000266272; Unassembled WGS sequence.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IEA:InterPro.
DR GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR PANTHER; PTHR42825; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42825:SF2; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE 3, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:RFU80499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000266272};
KW Transferase {ECO:0000313|EMBL:RFU80499.1}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ SEQUENCE 369 AA; 40767 MW; 268DB0310977D365 CRC64;
MTFAPIPRDD LDWKQLSSST PTRGHIESRW NQGAGTWTEP EFVGDPFLRI HGLAPVLHYG
QEAYEGLKAF RAPNGEINIV RPEYHARRLM HSSSLVSIPP VPVDHFLKCV QLAVGMNGDY
VPPNDANGML YIRPVVFGTG CNISLDPTDE YLFCVYVTTA GAFYANDSLD ALILEEFDRA
APRGTGSGKV GGNYSPVMRW SKKAKAEGYD ITLHLDSQTR SEIEEFSTSA FIGVKNDGKN
ITLVVPDTEN VVASVTSDSV QQLAKYLGWQ VDRRSIKYEE LADFSEVIAC GTAVTVISIK
SITRKSTQDK FVYLETGIEA GPCAQRLSAM LHDIYKGKEE DPFGWCAKVR RPAGFKEATI
DHSHVNGTH
//
