SWNA_ARTBC
ID SWNA_ARTBC Reviewed; 493 AA.
AC D4AU29;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Aminotransferase swnA {ECO:0000303|PubMed:28381497};
DE EC=2.6.1.- {ECO:0000305|PubMed:28381497};
DE AltName: Full=Swainsonine biosynthesis gene cluster protein A {ECO:0000303|PubMed:28381497};
GN Name=swnA {ECO:0000303|PubMed:28381497}; ORFNames=ARB_07842;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION, AND PATHWAY.
RX PubMed=28381497; DOI=10.1534/g3.117.041384;
RA Cook D., Donzelli B.G., Creamer R., Baucom D.L., Gardner D.R., Pan J.,
RA Moore N., Jaromczyk J.W., Schardl C.L.;
RT "Swainsonine biosynthesis genes in diverse symbiotic and pathogenic
RT fungi.";
RL G3 (Bethesda) 7:1791-1797(2017).
CC -!- FUNCTION: Aminotransferase; part of the gene cluster that mediates the
CC biosynthesis of swainsonine (SW), a cytotoxic fungal alkaloid and a
CC potential cancer therapy drug (PubMed:28381497). Swainsonine production
CC occurs via a multibranched pathway and is dispensable for fungal
CC colonization of plants and infection of insect hosts (By similarity).
CC The first step of swainsonine biosynthesis is the production of the
CC precursor pipecolic acid (PA) via conversion of L-lysine (Lys) to 1-
CC piperideine-6-carboxylate (P6C) by the aminotransferase swnA, the
CC latter being further reduced to PA by the reductase swnR (By
CC similarity). The PKS-NRPS hybrid synthetase swnK uptakes and
CC condensates PA and malonyl-CoA with and without skipping of the
CC ketoreductase (KR) domain in order to produce 3 intermediates, 1-
CC oxoindolizidine, (1S)-1-hydroxyindolizin, and (1R)-1-hydroxyindolizine;
CC with the transisomer (1S)-1-hydroxyindolizin being predominant (By
CC similarity). The terminal thioester reductase (TE) domain of swnK is
CC involved in reduction of the thioester bond to release the intermediate
CC aldehydes (By similarity). The oxidoreductase swnN could contribute to
CC the reduction of 1-oxoindolizidine to (1S)-1-hydroxyindolizin and (1R)-
CC 1-hydroxyindolizine, contributing to the major route of SW production
CC (By similarity). The dioxygenase swnH2 would be responsible for the
CC oxidization of (1R)-1-hydroxyindolizine into (1R,2S)-1,2-
CC dihydroxyindolizine and of (1S)-1-hydroxyindolizin to yield both
CC (1R,2S)-1,2-dihydroxyindolizine and (1S,2S)-1,2-dihydroxyindolizine (By
CC similarity). The dioxygenase swnH1 then performs the conversion of the
CC 1,2-dihydroxyindolizine epimers to SW (By similarity).
CC {ECO:0000250|UniProtKB:E9F8L8, ECO:0000250|UniProtKB:E9F8L9,
CC ECO:0000250|UniProtKB:E9F8M1, ECO:0000250|UniProtKB:E9F8M3,
CC ECO:0000250|UniProtKB:E9F8M4, ECO:0000269|PubMed:28381497}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P00509};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:28381497}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255}.
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DR EMBL; ABSU01000010; EFE33482.1; -; Genomic_DNA.
DR RefSeq; XP_003014122.1; XM_003014076.1.
DR AlphaFoldDB; D4AU29; -.
DR SMR; D4AU29; -.
DR STRING; 663331.D4AU29; -.
DR EnsemblFungi; EFE33482; EFE33482; ARB_07842.
DR GeneID; 9521539; -.
DR KEGG; abe:ARB_07842; -.
DR eggNOG; KOG0634; Eukaryota.
DR HOGENOM; CLU_017584_0_5_1; -.
DR OMA; PSQVMLY; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0047536; F:2-aminoadipate transaminase activity; IEA:EnsemblFungi.
DR GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IEA:EnsemblFungi.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..493
FT /note="Aminotransferase swnA"
FT /id="PRO_0000441181"
SQ SEQUENCE 493 AA; 55277 MW; 3BB3700DE060BE84 CRC64;
MHLEFEKAHD VLLEDVRDTV NIRQTHFSSP KRLANRWDHR LSDESLSQGA SPLKNSVKTA
TTSVPIPLGV GRPASLFYPW QSMTMTGTKE SNTRNPMTCN IGEAAFDISS ALNYADPSGS
TELVACFREN TRLIHNPPYQ DWDTTLTCGS TSAIDIVLRM LCNRGDWILA EASTYTGTVM
AAKAHGLNIQ SIEMDEEGLL PVDLDNKLRY WDTSRSRKPF VLYTIPSGHN PTGITQSTAR
KAAIYQIAER HDLLVLEDDP YFFLRLDGSF SSLDINPPYS SFEKLRKSLP SSYLSLDKSG
RVIRVDSTSK ILAPGLRCGW LTASKQIVEI FENFAEVGPA PPSGPSQVML YKLFVESWGQ
EGFANWLNHL SGEYKSRRDI MIAACSQHLP KGLCTWTTPT HGMFLWITID LARHPDYSEK
RENLSLDLED KIYERAASYG VAVAKGSWFN VEACLDKVFF RITFVSTTCL DDLENGVKRL
GAAVRDEFRF TQA
