GenomeNet

Database: UniProt
Entry: K1WQX3_MARBU
LinkDB: K1WQX3_MARBU
Original site: K1WQX3_MARBU 
ID   K1WQX3_MARBU            Unreviewed;       774 AA.
AC   K1WQX3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=tRNA 4-demethylwyosine synthase (AdoMet-dependent) {ECO:0000256|ARBA:ARBA00012821};
DE            EC=4.1.3.44 {ECO:0000256|ARBA:ARBA00012821};
GN   ORFNames=MBM_01987 {ECO:0000313|EMBL:EKD20035.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20035.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD20035.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20035.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-
CC         L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine
CC         + CO2 + H2O + L-methionine; Xref=Rhea:RHEA:36347, Rhea:RHEA-
CC         COMP:10164, Rhea:RHEA-COMP:10165, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC         ChEBI:CHEBI:73542; EC=4.1.3.44;
CC         Evidence={ECO:0000256|ARBA:ARBA00000664};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004797}.
CC   -!- SIMILARITY: Belongs to the TYW1 family.
CC       {ECO:0000256|ARBA:ARBA00010115}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH921430; EKD20035.1; -; Genomic_DNA.
DR   RefSeq; XP_007289876.1; XM_007289814.1.
DR   AlphaFoldDB; K1WQX3; -.
DR   STRING; 1072389.K1WQX3; -.
DR   GeneID; 18757922; -.
DR   KEGG; mbe:MBM_01987; -.
DR   eggNOG; KOG1160; Eukaryota.
DR   HOGENOM; CLU_007952_1_2_1; -.
DR   InParanoid; K1WQX3; -.
DR   OMA; FHVNGKW; -.
DR   OrthoDB; 275822at2759; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102521; F:tRNA-4-demethylwyosine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR013917; tRNA_wybutosine-synth.
DR   InterPro; IPR034556; tRNA_wybutosine-synthase.
DR   PANTHER; PTHR13930; S-ADENOSYL-L-METHIONINE-DEPENDENT TRNA 4-DEMETHYLWYOSINE SYNTHASE; 1.
DR   PANTHER; PTHR13930:SF0; S-ADENOSYL-L-METHIONINE-DEPENDENT TRNA 4-DEMETHYLWYOSINE SYNTHASE TYW1-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF08608; Wyosine_form; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDF00284; tRNA_wybutosine-synthesizing; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          111..281
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          432..680
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   774 AA;  87062 MW;  552E4ED58C0183C3 CRC64;
     MPLDKFFRPL LPFEVADLIA LWHIHRIPII LSTVTVLIVA RTYLHIRCPR YKIPDTPPIS
     PALPALNGKS TPPEKKAVAA VEKAPRRIVG GLKRRKSSQE DIKPRKQKIR VLVFFSSLTG
     TTEKIAKAFT EEIAQSTRKI AETTSTTFLE PVILDLSYID YDEYFINPPK NDSGAQYFYL
     LLLPTYNIDT VLDNFLEHLQ ETHNDFRIDT APLSTILGYS VFGFGDRDGW PTEEEGFCSQ
     ARDVDKWMAK LTGKKRAFPL GMGDSKSDAT ERLAEWKEGV EDVLGHIAAT GSLGEGVVGS
     GDAVESDMED VDDEDDVLFD DQKIAQRKTK AQKKDALNDL EDIGSAMNKQ ASIPGADLDD
     EPLEVDFTTY GKNPQSKPTP VIKEMVPKNS PTYTALTKQG YSIVGSHSGV KICRWTKSAL
     RGRGSCYKYS FYGIASHQCM ETTPSLSCSN KCVFCWRHGT NPVGTTWRWK VDAPDLIFDG
     VKAGHYQKIK MMRGVPGVRA ERFAEAMRIR HCALSLVGEP IFYPHINEFT AMLHKEHISS
     FLVCNAQHPD QLAALKPVTQ LYVSIDASNR ESLRKIDRPL HRDFWERFQR CLDILKERRF
     EQRTVFRLTL VKGFNIEDEA EGYADLVEKG LPCFVEVKGV TYCGTSSSAG AGLTMQNVPF
     YEEVCAFVEA LNAALARRGL GYGIAAEHAH SCCILLASER FRVGGKWHTR IDYVKFFQCL
     ESKEPFRPED YMGPETPDWA TWGKGGFDPR DERVYRKGKN KVALTEKQGV VMEI
//
DBGET integrated database retrieval system