ATRD_TAPPA
ID ATRD_TAPPA Reviewed; 524 AA.
AC B7STY2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=L-tyrosine:2-oxoglutarate aminotransferase atrD {ECO:0000303|PubMed:18805498};
DE EC=2.6.1.5 {ECO:0000269|PubMed:18805498};
DE AltName: Full=Atromentin biosynthesis protein D {ECO:0000305};
GN Name=atrD {ECO:0000303|PubMed:18805498};
OS Tapinella panuoides (Oyster rollrim mushroom) (Paxillus panuoides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Tapinellineae; Tapinellaceae; Tapinella.
OX NCBI_TaxID=80604;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND CATALYTIC ACTIVITY.
RX PubMed=18805498; DOI=10.1016/j.fgb.2008.08.009;
RA Schneider P., Bouhired S., Hoffmeister D.;
RT "Characterization of the atromentin biosynthesis genes and enzymes in the
RT homobasidiomycete Tapinella panuoides.";
RL Fungal Genet. Biol. 45:1487-1496(2008).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=5862512; DOI=10.1002/jps.2600540714;
RA Khanna J.M., Malone M.H., Euler K.L., Brady L.R.;
RT "Atromentin, anticoagulant from Hydnellum diabolus.";
RL J. Pharm. Sci. 54:1016-1020(1965).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=6541963; DOI=10.1139/m84-166;
RA Brewer D., Jen W.C., Jones G.A., Taylor A.;
RT "The antibacterial activity of some naturally occurring 2,5-dihydroxy-1,4-
RT benzoquinones.";
RL Can. J. Microbiol. 30:1068-1072(1984).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=17323650; DOI=10.1038/ja.2006.108;
RA Zheng C.J., Sohn M.J., Kim W.G.;
RT "Atromentin and leucomelone, the first inhibitors specific to enoyl-ACP
RT reductase (FabK) of Streptococcus pneumoniae.";
RL J. Antibiot. 59:808-812(2006).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=19809251; DOI=10.4014/jmb.0811.617;
RA Kim J.H., Lee C.H.;
RT "Atromentin-induced apoptosis in human leukemia U937 cells.";
RL J. Microbiol. Biotechnol. 19:946-950(2009).
CC -!- FUNCTION: The L-tyrosine:2-oxoglutarate aminotransferase atrD and the
CC atromentin synthetase atrA catalyze consecutive steps to turn over L-
CC tyrosine into atromentin, which represents the generic precursor
CC molecule for the entire terphenylquinone and pulvinic acid family of
CC pigments, which are widely distributed secondary metabolites in
CC homobasidiomycetes (PubMed:18805498). The first step is catalyzed by
CC atrD which converts L-tyrosine in to 4-hydroxyphenylpyruvate (4-HPP)
CC (PubMed:18805498). Adenylation of two 4-HPP monomers by the atrA
CC adenylation (A) domain, ester bond formation between monomers and atrA,
CC and symmetric C-C-bond formation between two monomers by atrA leads to
CC atromentin (PubMed:18805498). {ECO:0000269|PubMed:18805498}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5;
CC Evidence={ECO:0000269|PubMed:18805498};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P00509};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=291 uM for L-tyrosine {ECO:0000269|PubMed:18805498};
CC KM=590 uM for 2-oxoglutarate {ECO:0000269|PubMed:18805498};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:18805498};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:18805498};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:18805498}.
CC -!- BIOTECHNOLOGY: Atromentin has been shown to induce caspase-3 and poly
CC (ADP-ribose) polymerase (PARP) in human leukemia U937 cells
CC (PubMed:19809251). It has also anticoagulant activity (PubMed:5862512).
CC Moreover, atromentin has antimicrobial activity (PubMed:6541963). It
CC acts especially as an inhibitor of FabK, the enoyl-acyl carrier protein
CC (ACP) reductase of S.pneumoniae (PubMed:17323650).
CC {ECO:0000269|PubMed:17323650, ECO:0000269|PubMed:19809251,
CC ECO:0000269|PubMed:5862512, ECO:0000269|PubMed:6541963}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255}.
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DR EMBL; EU711406; ACH90387.1; -; Genomic_DNA.
DR AlphaFoldDB; B7STY2; -.
DR SMR; B7STY2; -.
DR BioCyc; MetaCyc:MON-18721; -.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..524
FT /note="L-tyrosine:2-oxoglutarate aminotransferase atrD"
FT /id="PRO_0000437679"
SQ SEQUENCE 524 AA; 57619 MW; C6369F787182E948 CRC64;
MPVAVESAIP YPTPRKVDLA HHLSTEARIR QPNPIKSVWK AAQVRPGIIN MGNGDPHHTL
YPISSMNFIV PSLEGDHPVE AWRTGTSKTL VLSSHKDAPS TLSLRTAFAY GAGAGLPAVR
EALADLGARI HAPPNHTVCL SLGNADALTK CFRLFGDPDD SFLCEEFTFS AMTNAALALG
IRWVPVRVDG GGLLPEDLER VMRCWDEKKQ GKRPHVLYTV PCSQNPTGST ISLERRRRIY
EVAHIYDIII IEDDPYYFLQ YDLQINQNTL KEHGYTRAMS EVLPRSFLSM DIDGRVVRLD
SFSKVLAPGI RLGWITSSPF FADKLDMLTD SSTQHPHGLG QAYLAELLGP TGWGADGLMK
WVHSLAREYE RRRDLFVSVF DAKVAPTGCA SAEVPQSGMF VWIQVHLETH PRFVVRTPDS
GSDDEGDVLG AVMAAPGVLG EVARGGPITN TEQLMSELLR KLVESGVIMI PASTFAIVDR
SGSTLSPIGD RANYLRATFV GTDETIRDGL TIFAQALEEF FNLK
