ID A0A1V6YPX4_PENNA Unreviewed; 374 AA.
AC A0A1V6YPX4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Branched-chain amino acid aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENNAL_c0014G09022 {ECO:0000313|EMBL:OQE89480.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE89480.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE89480.1}.
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DR EMBL; MOOB01000014; OQE89480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6YPX4; -.
DR STRING; 60175.A0A1V6YPX4; -.
DR OMA; VGMNAAY; -.
DR OrthoDB; 1304at2759; -.
DR Proteomes; UP000191691; 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 NCBIfam; TIGR01123; ilvE_II; 1.
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:UP000191691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ SEQUENCE 374 AA; 40744 MW; F37B4D2F3F0CCEF6 CRC64;
MFPPPPIALD WNNLGFKVRD GNGHVEIHFS HSGENKWSAP QFVASPFLPV HGMAPGLNYG
QQVYEGLKAF RHPANDKITI FRPDRNAKRM QYSAEVVSMP PVPEDLFIEC VRLAVGANAE
YVPPHDSGAA MYVRPILFGS SAQLGLSPPD GYTLAVFAMP TGVYHGASAV EALILEDFDR
CAPHGTGAAK VGGNYAPVLR HSDRARREGF GITLHLDSAT RSEVDEFSTS AFIGVKRDGD
QVTVVQPDSR NAIDSVTASS VLEIARTLGY RVEKRRVTYE ELREFDEVIA AGTAAALVPV
GSITTRSRGD RFEYRSGAQK EGGEVCVKLL QTLRGIQSGT VEDTFGWNYE VQAPPKGWAQ
QEQEEIELSG ANVP
//
