ID A0A2H3IYU2_9EURO Unreviewed; 362 AA.
AC A0A2H3IYU2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 08-NOV-2023, entry version 13.
DE SubName: Full=Aminotransferase, class IV {ECO:0000313|EMBL:PCH07332.1};
GN ORFNames=PENO1_012320 {ECO:0000313|EMBL:PCH07332.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH07332.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH07332.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH07332.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(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:PCH07332.1}.
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DR EMBL; NPFK01000018; PCH07332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IYU2; -.
DR STRING; 290292.A0A2H3IYU2; -.
DR OrthoDB; 1304at2759; -.
DR Proteomes; UP000218381; 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 ECO:0000313|EMBL:PCH07332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PCH07332.1}.
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ SEQUENCE 362 AA; 39119 MW; 66E45F21B5B3FA52 CRC64;
MAFPPEPTDS VDWKSLGFSI SDVNGHIEAK WSSKTGTWGP PTFVTDPYIR LHGLAPALNY
GQQAYEGLKA LRTADNQILI FRPQKNAARF AHSASFISIP AVPEELFVEC VHAAVALNAE
YVPPHETGAA MYIRPLIFGS GPELRSQPPA EFTLCVYVNP VGTYHGAHPV KALVMEEYHR
AAPKGTGSAK IGGNYAPVMR WQKQAAEQGY GITLHLDAKT ESEIDEFSSS GFIGVKTDKE
NNITLVLTNS KNIIDSITVD SCLGIGKSLG WNVEVRPIKY EEVGSFSEVL AAGTAAALLP
IRSITRPSTS ETVSYIDDSS EEPGPVCSIL LSTLKGIQSG KMKDTFGWTY PVHGVDATQY
AS
//
