ID A0A369GLX5_9HYPO Unreviewed; 407 AA.
AC A0A369GLX5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=Branched-chain amino acid aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CP532_3631 {ECO:0000313|EMBL:RDA83943.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA83943.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA83943.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA83943.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-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 -!- 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:RDA83943.1}.
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DR EMBL; PDHP01000151; RDA83943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369GLX5; -.
DR STRING; 2039875.A0A369GLX5; -.
DR Proteomes; UP000252748; 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 CDD; cd01557; BCAT_beta_family; 1.
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 InterPro; IPR033939; BCAT_family.
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:0000256|ARBA:ARBA00022576};
KW Reference proteome {ECO:0000313|Proteomes:UP000252748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 314..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ SEQUENCE 407 AA; 43940 MW; C140C9237BE3E26E CRC64;
MAAAPFPPPP VNTIDWSNVG FRVREVNGHV EATYSRATGN WSPLRFVTDP YMRIHGMAPA
LNYGQQAYEG LKAFRGPSDG DIGLFRPHRN AARLQHSADV VSMPHVPSDL FVRACRAAVS
LNAGFVPPHE TGAAMYVRPQ LYGSSAQLGL APPEEYTFAV FVIPTGVYHG SHPVRALILD
EFDRAAPNGT GHAKVGGNYA PVLRWSDAAR RDGFDITLHL DSARHEEVDE FSTSGFIGVL
KRGDDDVTLV VPDSRCAIDS VTSDSVLAIA RSFGWKTERR TVLYTELPSF SEVIAAGTAA
ALVPIRSITR RLPKGLLPPD APRVSSSSSN EEKPSETVTY IPDEQEDAGP ICLRLLTQLK
AIQLGKVPDE FGWRLVVDAA DGEIEGAASV YSTPVDGEAV RAVGQLT
//
