AMT1_SERL9
ID AMT1_SERL9 Reviewed; 520 AA.
AC F8P1W6; F8P1W5;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=L-tyrosine:2-oxoglutarate aminotransferase amt1;
DE EC=2.6.1.5 {ECO:0000250|UniProtKB:B7STY2};
DE AltName: Full=Atromentin biosynthesis protein amt1;
GN Name=amt1; ORFNames=SERLADRAFT_356993;
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7.9;
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
RN [2]
RP INDUCTION.
RX PubMed=27699944; DOI=10.1111/1462-2920.13558;
RA Tauber J.P., Schroeckh V., Shelest E., Brakhage A.A., Hoffmeister D.;
RT "Bacteria induce pigment formation in the basidiomycete Serpula
RT lacrymans.";
RL Environ. Microbiol. 18:5218-5227(2016).
CC -!- FUNCTION: An L-tyrosine:2-oxoglutarate aminotransferase (probably amt1)
CC and atromentin synthetase nps3 catalyze consecutive steps to turn over
CC L-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 (Probable). The first step catalyzed by amt1
CC converts L-tyrosine in to 4-hydroxyphenylpyruvate (4-HPP). Adenylation
CC of two 4-HPP monomers by the nps3 adenylation (A) domain, covalent
CC tethering of the monomers as a thioester and oxoester onto the nps3
CC thiolation (T) and thioesterase (TE) domains, respectively, and
CC symmetric C-C-bond formation between two monomers catalyzed by the nps3
CC TE domain leads to atromentin. Follow-up products of atromentin in
CC S.lacrymans include atromentic acid, xerocomic acid, isoxerocomic acid
CC and variegatic acid (By similarity). {ECO:0000250|UniProtKB:B7STY2,
CC ECO:0000305|PubMed:27699944}.
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:0000250|UniProtKB:B7STY2};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P00509};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000250|UniProtKB:B7STY2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F8P1W6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F8P1W6-2; Sequence=VSP_059261;
CC -!- INDUCTION: Up-regulated upon coincubation of the fungus with the
CC terrestrial bacteria Streptomyces iranensis, Bacillus subtilis or
CC Pseudomonas putida. {ECO:0000269|PubMed:27699944}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; GL945436; EGO23144.1; -; Genomic_DNA.
DR EMBL; GL945436; EGO23143.1; -; Genomic_DNA.
DR RefSeq; XP_007320383.1; XM_007320321.1. [F8P1W6-2]
DR RefSeq; XP_007320384.1; XM_007320322.1. [F8P1W6-1]
DR AlphaFoldDB; F8P1W6; -.
DR SMR; F8P1W6; -.
DR EnsemblFungi; EGO23143; EGO23143; SERLADRAFT_356993. [F8P1W6-2]
DR EnsemblFungi; EGO23144; EGO23144; SERLADRAFT_356993. [F8P1W6-1]
DR GeneID; 18809549; -.
DR KEGG; sla:SERLADRAFT_356993; -.
DR InParanoid; F8P1W6; -.
DR Proteomes; UP000008064; Unassembled WGS sequence.
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 2: Evidence at transcript level;
KW Alternative splicing; Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..520
FT /note="L-tyrosine:2-oxoglutarate aminotransferase amt1"
FT /id="PRO_0000442628"
FT VAR_SEQ 468..487
FT /note="Missing (in isoform 2)"
FT /id="VSP_059261"
SQ SEQUENCE 520 AA; 58111 MW; 45476A6BE805A59F CRC64;
MVYFATSAEN SKTSYKVDLS HHLSRETRAR QPNPIKTIWK IAQTKVGTIN MGNGDPHNTL
YPISKIDFVV PSLDQPNPVQ AWKEGNSKTD IISSYKDESC ALSLKTAFAY GTGAGLQQVR
GVLADLNNRI HSPPNHTVSL SLGNADSLTK CFRLFGDPGD SFLCEEFTFS PMTNAALPLG
IKWEPIKMDK GGLIPADMDK ILTNWDERTQ GRRPHVLYTV PCSQNPTGST LPFERRKSIY
EIARKWDIII LEDDPYYFLQ YGLNVDQFIV EQHGFTRALA SVLPRSFLSM DYDGRVVRLD
SFSKIVAPGM RLGWVTANNF FAEKLDSLTD SSSQHPHGFG QAFIAELLGD GGWGLDGFMK
WTKSLCDEYQ RRRDLFMDVF RREVGINGFA TAEVPKSGMF VWIKINLEHH ARYRVVKESN
GDPRTNTAAL MDELFRTLLD SGLVLIPAST FAITGSLSPP SGDCILDVSI CIDGVGAIAE
LPLSIFQRVN YFRATFVGTD ETICDGLKIF GRTIEQFFCF
