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Database: UniProt
Entry: A0A3B3YXL3_9TELE
LinkDB: A0A3B3YXL3_9TELE
Original site: A0A3B3YXL3_9TELE 
ID   A0A3B3YXL3_9TELE        Unreviewed;       671 AA.
AC   A0A3B3YXL3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=tRNA 4-demethylwyosine synthase (AdoMet-dependent) {ECO:0000256|ARBA:ARBA00012821};
DE            EC=4.1.3.44 {ECO:0000256|ARBA:ARBA00012821};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000031908.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000031908.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Probable component of the wybutosine biosynthesis pathway.
CC       Wybutosine is a hyper modified guanosine with a tricyclic base found at
CC       the 3'-position adjacent to the anticodon of eukaryotic phenylalanine
CC       tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms
CC       from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate
CC       in wybutosine biosynthesis. {ECO:0000256|ARBA:ARBA00025368}.
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}.
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DR   AlphaFoldDB; A0A3B3YXL3; -.
DR   Ensembl; ENSPMET00000025342.1; ENSPMEP00000031908.1; ENSPMEG00000019437.1.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000261480; Unplaced.
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; IPR001094; Flavdoxin-like.
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   PRINTS; PR00369; FLAVODOXIN.
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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          47..205
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          339..583
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          217..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  75864 MW;  E6684834F95FB665 CRC64;
     MWNNRLYVYS AAALLLGFCF LLQVTRRKVS PALVTSDEDA DVHVSGVKIF YGSQTGTAKG
     FASELSQEVQ ALGIPAEVID MKDFDPDDRL ADECVSKSVC VFLVATYTDG RPTQNAEWFC
     KWLEEASTDF RYGNSFLKGL RYAVFGLGNS VYVGHYNTVG TNVDKCLWML SARRVLSRGE
     GDGNVVKSRH GSVQADFRAW KVRFLSRLRA LARGEKKSCS GNCKSGASCK NRKKHGAPEE
     EEHGSELIES SSEEEESGWP DEKTSRSVVD VEDLGNIMNS VKKAKLILCS AVFSEIFTHQ
     HVFPPSGYKL IGSHSGVKLC RWTKSMLRGR GGCYKHTFYG IESHRCMETT PSLACANKCV
     FCWRHHTNPV GTEWRWKMDP AEKILQDSLE KHQNMIRQFR GVPGVKPERY EEGLAAKHCA
     LSLVGEPIMY PEINTFLRLL HSHRISSFLV TNAQFPEEIR NLVPVTQLYV SVDASTKDSL
     KKIDRPLFKD FWPRFLDCLR ALGEKKQRTV YRLTLVKAWN VEELQAYAEL IALGQPDFIE
     VKGVTYCGES SASSLTMANV PWHQEVVAFV QQLADMLPHY QIACEHEHSN CLLIAHRKFK
     VNGEWRTWID YDRFQDLVQA HEDSGGQQTF SALDYTAKTP SWALFGSNEQ GFDPADTRFQ
     RRNKTKDISG C
//
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