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SWNH1_ARTBC
ID   SWNH1_ARTBC             Reviewed;         307 AA.
AC   D4AU26;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Dioxygenase swnH1 {ECO:0000303|PubMed:28381497};
DE            EC=1.14.11.- {ECO:0000305|PubMed:28381497};
DE   AltName: Full=Swainsonine biosynthesis gene cluster protein H1 {ECO:0000303|PubMed:28381497};
GN   Name=swnH1 {ECO:0000303|PubMed:28381497}; ORFNames=ARB_07839;
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: Dioxygenase; 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; EFE33479.1; -; Genomic_DNA.
DR   RefSeq; XP_003014119.1; XM_003014073.1.
DR   AlphaFoldDB; D4AU26; -.
DR   SMR; D4AU26; -.
DR   EnsemblFungi; EFE33479; EFE33479; ARB_07839.
DR   GeneID; 9521536; -.
DR   KEGG; abe:ARB_07839; -.
DR   eggNOG; ENOG502SIE1; Eukaryota.
DR   HOGENOM; CLU_047725_0_0_1; -.
DR   OMA; IGYGAPR; -.
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..307
FT                   /note="Dioxygenase swnH1"
FT                   /id="PRO_0000441183"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         151
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
FT   BINDING         227
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O14832"
SQ   SEQUENCE   307 AA;  34026 MW;  733715CE54869345 CRC64;
     MPEFPPPIDP SYVPSVSLTR IPANAPIEDI LAVLERDGGL ILTDIISSQD VAAINDELDP
     YVQKARAESH AAYDLIPKQT IMVPGIVGKS PTMAKIAEYE VIDKLRTMVL QKKCTATWED
     RTEEFTIGPL LNSSLTYNVS YGGPRQRLHR DDMIHGIYHH DGEYSLSNET MLGFMFAGCK
     TTRENGATMA IPGSHKWNHT RVPRTDEVCF AEMEPGSAFV FLGTVYHGAG HNSVPDQVRK
     VYGLFFISGT LRPEENQFLA IPRSKVLGMS DKMLSLLGYK KPETWLGIVN NGDPAENLKE
     VLDMANS
 
 
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