ID A0A024GUJ4_9STRA Unreviewed; 733 AA.
AC A0A024GUJ4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=BN9_115290 {ECO:0000313|EMBL:CCI50025.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI50025.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI50025.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI50025.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCI50025.1}.
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DR EMBL; CAIX01000379; CCI50025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GUJ4; -.
DR STRING; 65357.A0A024GUJ4; -.
DR InParanoid; A0A024GUJ4; -.
DR OrthoDB; 275822at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000053237; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..733
FT /note="tRNA 4-demethylwyosine synthase (AdoMet-dependent)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001529768"
FT DOMAIN 81..233
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 393..638
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 47..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..66
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 83798 MW; 79BDECE836F3D42E CRC64;
MQSSYSSAWV FAVPIAALLL TAVSLQLTDT WHPSIELLCS KFAQKSRQKP TKANKKKLKK
STISRKSPQK PHSDAPRAIP VRILFGTQTG TAKSMALDLE KRLFACNVSG FHFQPEVINM
NEYDQDHLEH ESVVIFILST WTGGIAPKDA ETFCSWLKDM ALDFRVSKTW LSHIFHAVFG
LGSAEYDEHY CTAAKELSKH LKLLGSSSLV EIGFGDDNID QNQQFEQWSD QLIVKLCSQS
TMSPPATEVQ TVNEEENDDE TKGWLSQNQH RRQKRAEKQQ DALRLDPKAM EWTEEDLMND
RLLTDDTLEI NRDISTTKQS SEGESIVDVE DIGNTMRESQ TANESQEMVT PMQRKALTKE
GYKIIGSHSA VKLCRWTKHQ LRGRGGCYKH TFYGITSYQC METTPSLACA NKCVFCWRHH
KNPVGRVWRW KIDEPEGLIV GSIERHQNMI KELRGLPGLN LERWKEAFTV RHCALSLVGE
PIMYPHINTF CRKLHQRRIS SFLVTNAQFP EKIAALEPIT QLYVSVDAAT KDALQAVDRP
LFKDFWERFL ACLRELRRKG QRTVYRLTLV KSYNMQDIEK YAELIEIGQP DFIEVKAVTY
CGKSDGSDLT MKHVPWHEEV CDFCTALVEK TNGVYGLAAQ HAHSNCVLLA KKTFCIDGQW
HTWIDYEKFH DLMDRYYTDG TMFSSSEYIS PTPSWATFDA PEKGFDPCET RFYRTKNGKI
AETSYQSTES GCG
//
