ID I2GZ16_TETBL Unreviewed; 834 AA.
AC I2GZ16;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=tRNA 4-demethylwyosine synthase (AdoMet-dependent) {ECO:0000256|ARBA:ARBA00012821};
DE EC=4.1.3.44 {ECO:0000256|ARBA:ARBA00012821};
GN Name=TBLA0B05360 {ECO:0000313|EMBL:CCH59368.1};
GN ORFNames=TBLA_0B05360 {ECO:0000313|EMBL:CCH59368.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH59368.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH59368.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE806317; CCH59368.1; -; Genomic_DNA.
DR RefSeq; XP_004178887.1; XM_004178839.1.
DR AlphaFoldDB; I2GZ16; -.
DR STRING; 1071380.I2GZ16; -.
DR GeneID; 14494020; -.
DR KEGG; tbl:TBLA_0B05360; -.
DR eggNOG; KOG1160; Eukaryota.
DR HOGENOM; CLU_007952_1_2_1; -.
DR InParanoid; I2GZ16; -.
DR OMA; FHVNGKW; -.
DR OrthoDB; 275822at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000002866; Chromosome 2.
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; 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:UP000002866};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 207..368
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 469..717
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 149..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 94027 MW; 1BB6810924903476 CRC64;
MDAIGKHNVS VAVGASAIAY CYFGGRTSFA LVGVVLYDMF YSNYVFKSSS PTSANFVVEP
EPVEKKKHKC CGGKGGSGCC SNKKDANDKA KKSCKCGHKK NTKESKTVPL STGFTNKITL
EKSIGDITNS TKDNSFPIAV DFTQSFKPKK TKGKKKDTSK KVIISKLPSK NSSEEDVSAS
QPIAVIDPST VKSAMTVSTD KLINSQIYIF YSSLQGASLR VANRVKDNLS NKVQDLKYTP
IVIHLDEIDD LDDFFVNLPS SENNQINSLY ILVIPSYDTD CPLDYFLQTL QENFYDWRIN
KFPLTKLSGY TVLGLGDKES WPEKFCYQAK KVDHWLSKLG GRRIYPVGEI CMKTEGDSKV
DEWSDLLSEC LKDDNPIVYQ YEQSDDEDSD EENSEAEDED LQDVEDIVKN GKVINDTDIK
QMVSKNSPTF KQLKKQGYHI VGSHSGVKIC RWTKSDLRGT GSCYKQSLFN ITSSRCMELT
PSLACSSKCV FCWRHGTNPV SKTWRWEVDE PEYILENALK GHYAMIKQMR GVPGVVAERF
QKAFKVGHCA LSLVGEPIMY PYINRFVELL HEKEITSFLV CNAQHPEPLE NLGKVTQLYV
SIDAPTKDEL RKVDRPLFKD FWERMLQCLD ILNTKQHHQR TVFRLTLVKG FNMGDISAYA
DLVQRGSPCF IEVKGATFSG TSKSGSNPLT MQNIPFYEEC TNFVKEFAKE LQRRGLDYDL
AAEHAHSNCI LLAHKKFQIN GEWYTHIDFA KFFELLNSGK DFTHMDYMAK TPEWALFGNG
GFAPGNTRVY RKGKNKQKKQ DDSSQVDTNM ETTIKPGNDI TDKMITTNEV KAAV
//
