SWNH2_ARTBC
ID SWNH2_ARTBC Reviewed; 313 AA.
AC D4AU30;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Dioxygenase swnH2 {ECO:0000303|PubMed:28381497};
DE EC=1.14.11.- {ECO:0000305|PubMed:28381497};
DE AltName: Full=Swainsonine biosynthesis gene cluster protein H2 {ECO:0000303|PubMed:28381497};
GN Name=swnH2 {ECO:0000303|PubMed:28381497}; ORFNames=ARB_07843;
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=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q4WAW9};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:28381497}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WAW9}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; ABSU01000010; EFE33483.1; -; Genomic_DNA.
DR RefSeq; XP_003014123.1; XM_003014077.1.
DR AlphaFoldDB; D4AU30; -.
DR SMR; D4AU30; -.
DR EnsemblFungi; EFE33483; EFE33483; ARB_07843.
DR GeneID; 9521540; -.
DR KEGG; abe:ARB_07843; -.
DR eggNOG; ENOG502SHTY; Eukaryota.
DR HOGENOM; CLU_047725_0_0_1; -.
DR OMA; MKINEVD; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..313
FT /note="Dioxygenase swnH2"
FT /id="PRO_0000441185"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
SQ SEQUENCE 313 AA; 35076 MW; 2C29FEE3191A5545 CRC64;
MDKKYAAARL LPPIDASYQP ARSVTKIPAT SSLEEILEVL ERDGGVILTD FVPKETMDKI
DEELEPYTKT IPDSDSYDDF IGKKTLVIAG LISKSDTLAN ILDTNETIDK LLKIILEERY
PAVFEGHTEE LVIDPLLSIS MAFHVGQGSP RQALHRDDMV FSSKHHPNMK INEVDGFSCF
IAGSNVTREN GGTMVILGSH KWEHDRRGRP DEVSFLEMER GSAFIFLSTM AHGAGYNTIP
GEIRKIMNLV FCRGTLRQEE NQFLCNPRSK VLKMSPKMQT LLGFKKPAGT WLGMVDNDDP
AKDLPAIYEK IMQ
