ID A0A3F3Q2F7_9EURO Unreviewed; 777 AA.
AC A0A3F3Q2F7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BDQ94DRAFT_34453 {ECO:0000313|EMBL:RDH33285.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH33285.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH33285.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH33285.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KZ852047; RDH33285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3Q2F7; -.
DR STRING; 1341132.A0A3F3Q2F7; -.
DR OrthoDB; 275822at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; SFLDF00284; tRNA_wybutosine-synthesizing; 1.
DR SFLD; SFLDG01071; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 122..297
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 432..681
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 42..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 86992 MW; E41B5EF04CCC1FCD CRC64;
MEGSGNEGLL AFWHSYRLPL LLALATLLVL VRAYRKLQPK SKIATASSIP SSPRSHSPEK
REKTISNSTE KDVGTDLKPS VVEKDASQKQ AGPKRVTGKK PLKVAGRRRG SDQEPAVSFI
QPIIFFASLT ANTERYAQVL LEELRAAARD RADPDNRERG LLPPQIHDLS YVDFDDYFIS
APKPPSTSPG TRYVYCMLIP TYNIDTILNT FLGHLDETHH DFRIDTAPLS GLAGYSVFGF
GDKEGWPTEE EGFCSQAKEL DRWMAKLTGR KRAYPLGFGD VKSDAESALK EWSRGLQDIL
GDIVENGGLG EGVPGSGDPL ESDEEDLDDE GSESDKANGR KRNKNQSVVD LEDIKFSSDA
ASGSPIPVDF TTGGKSPAPA TEKEMVPKTS PTYASLTKQG YTIVGSHSGV KICRWTKSAL
RGRGSCYKFS FYGIRSHLCM EATPSLSCSN KCIFCWRHGT NPVGTTWRWK VDDPELIFNG
VKEGHYKKIK MMRGVPGVRA ERFAEAMRIR HCALSLVGEP IFYPHINRFL DMLHSEHISS
FLVCNAQHPD QLETLHRVTQ LYVSIDASNR ESLRKIDRPL HRDFWERFQR CLDILREKRH
YQRTVFRLTL VKGFNIDDEV IGYANLVEKA LPCFVEIKGV TYCGTSTSAG AGLTMQNVPF
YEEVQQFVTS LNAELERRGL KYGIAAEHAH SCCALIASER FHVNGKWHSR IDYDRFFQLL
EKEKADGTSF TPEDYMRETE DWALWGNGGF DPNDERVYKK GKKKAIQAAA AATEAQG
//
