ID   HTYB_ASPRU              Reviewed;         379 AA.
AC   K0E3V3;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Transaminase htyB {ECO:0000303|PubMed:22998630};
DE            EC=2.6.1.- {ECO:0000305|PubMed:22998630};
DE   AltName: Full=L-homotyrosine biosynthetic cluster protein B {ECO:0000303|PubMed:22998630};
GN   Name=htyB {ECO:0000303|PubMed:22998630};
OS   Aspergillus rugulosus (Emericella rugulosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND BIOTECHNOLOGY.
RC   STRAIN=ATCC 58397 / NRRL 11440;
RX   PubMed=22998630; DOI=10.1021/ja307220z;
RA   Cacho R.A., Jiang W., Chooi Y.H., Walsh C.T., Tang Y.;
RT   "Identification and characterization of the echinocandin B biosynthetic
RT   gene cluster from Emericella rugulosa NRRL 11440.";
RL   J. Am. Chem. Soc. 134:16781-16790(2012).
CC   -!- FUNCTION: Transaminase; part of the gene cluster that mediates the de
CC       novo generation of L-homotyrosine from acetyl-CoA and 4-hydroxyphenyl-
CC       pyruvate (PubMed:22998630). L-homotyrosine is a building block of
CC       echinocandin B, a fungal lipidated cyclic hexapeptide that acts as an
CC       antifungal agent (PubMed:22998630). L-homotyrosine 4-hydroxyphenyl-
CC       pyruvate first undergoes an aldol-type condensation by htyA with the C-
CC       2 of acetyl-CoA followed by the release of CoA to form 2-(4-
CC       hydroxybenzyl)-malate (PubMed:22998630). This is followed by
CC       isomerization of 2-(4-hydroxy-benzyl)-malate to 3-(4-hydroxybenzyl)-
CC       malate by htyD (PubMed:22998630). Thereafter, 3-(4-hydroxybenzyl)-
CC       malate undergoes decarboxylation and oxidation to form 2-oxo-4-(4-
CC       hydroxybenzyl)butanoic acid, coupled to reduction of NAD(+) to NADH by
CC       htyC (PubMed:22998630). The product then undergoes transamination
CC       catalyzed by htyB to form L-homotyrosine (PubMed:22998630).
CC       {ECO:0000269|PubMed:22998630}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P19938};
CC   -!- PATHWAY: Antifungal biosynthesis. {ECO:0000305|PubMed:22998630}.
CC   -!- BIOTECHNOLOGY: Due to their effectiveness as antifungal agents,
CC       echinocandin derivatives can be used for the treatment of human
CC       invasive candidiasis (PubMed:22998630). {ECO:0000269|PubMed:22998630}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; JX421685; AFT91392.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0E3V3; -.
DR   SMR; K0E3V3; -.
DR   BioCyc; MetaCyc:MON-19237; -.
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; 3.20.10.10; -; 1.
DR   Gene3D; 3.30.470.10; -; 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; PTHR42825; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..379
FT                   /note="Transaminase htyB"
FT                   /id="PRO_0000443852"
FT   BINDING         92
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         239
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   MOD_RES         203
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
SQ   SEQUENCE   379 AA;  41386 MW;  437B9144EB8CBE59 CRC64;
     MIATEYPRPP LAGIDWNHLG FEPVEVNGHI ESRFSPSTKT WSTPTFIPDP YIRIHGLTPA
     LNYGQQIFEG LKAFRTPSGS ITVFRPDQNA HRFARSARAV SIPPIPTDIF LEAVHLAVGM
     NSEFVPPVGT GAALYIRPLA FASSATVGLA LASEFLFCVY VLPVAPLHKH SGENDKDRKK
     RGVRALVVED FDRAAPRGTG DVKVGGNYGP ALGRIDAARQ EGYGLTLHLD SQSRSLVDEF
     STSGFIGVRK ENDDELKLVV SDSQQIVASV TIDSICEIAR GFGWAVEKRS IAFTEVSEFV
     EVYAAGTAAM LVPVQSVERR STGEFIQYSV DYAEPTSVFA QLYKALSGVQ QGLVPDQWGW
     TQEVLRPKQL ASQDTEADT