TYW1_PYRAB
ID TYW1_PYRAB Reviewed; 342 AA.
AC Q9V1F9; G8ZGH2;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase {ECO:0000255|HAMAP-Rule:MF_01921};
DE EC=4.1.3.44 {ECO:0000255|HAMAP-Rule:MF_01921};
DE AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw1 {ECO:0000255|HAMAP-Rule:MF_01921};
GN Name=taw1 {ECO:0000255|HAMAP-Rule:MF_01921}; OrderedLocusNames=PYRAB04680;
GN ORFNames=PAB2039;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=23043105; DOI=10.1074/jbc.m112.405019;
RA Perche-Letuvee P., Kathirvelu V., Berggren G., Clemancey M., Latour J.M.,
RA Maurel V., Douki T., Armengaud J., Mulliez E., Fontecave M.,
RA Garcia-Serres R., Gambarelli S., Atta M.;
RT "4-Demethylwyosine synthase from Pyrococcus abyssi is a radical-S-adenosyl-
RT L-methionine enzyme with an additional [4Fe-4S](+2) cluster that interacts
RT with the pyruvate co-substrate.";
RL J. Biol. Chem. 287:41174-41185(2012).
CC -!- FUNCTION: Component of the wyosine derivatives biosynthesis pathway
CC that catalyzes the condensation of N-methylguanine with 2 carbon atoms
CC from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on
CC guanosine-37 of tRNA(Phe). {ECO:0000255|HAMAP-Rule:MF_01921,
CC ECO:0000269|PubMed:23043105}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01921, ECO:0000269|PubMed:23043105};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:23043105};
CC Note=Binds 2 [4Fe-4S] clusters (PubMed:23043105). Binds 1 4Fe-4S
CC cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC methionine. {ECO:0000305|PubMed:23043105};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01921}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01921}.
CC -!- SIMILARITY: Belongs to the TYW1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01921}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCE69851.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248284; CAB49390.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69851.1; ALT_INIT; Genomic_DNA.
DR PIR; G75163; G75163.
DR AlphaFoldDB; Q9V1F9; -.
DR SMR; Q9V1F9; -.
DR STRING; 272844.PAB2039; -.
DR EnsemblBacteria; CAB49390; CAB49390; PAB2039.
DR KEGG; pab:PAB2039; -.
DR PATRIC; fig|272844.11.peg.495; -.
DR eggNOG; arCOG04174; Archaea.
DR HOGENOM; CLU_007952_3_0_2; -.
DR OMA; HRCLQMT; -.
DR PhylomeDB; Q9V1F9; -.
DR BRENDA; 4.1.3.44; 5242.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01921; TYW1_archaea; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR013917; tRNA_wybutosine-synth.
DR InterPro; IPR034556; tRNA_wybutosine-synthase.
DR InterPro; IPR023993; TYW1_archaea.
DR PANTHER; PTHR13930; PTHR13930; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF08608; Wyosine_form; 1.
DR SFLD; SFLDF00284; tRNA_wybutosine-synthesizing; 1.
DR TIGRFAMs; TIGR03972; rSAM_TYW1; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Lyase; Metal-binding;
KW S-adenosyl-L-methionine; tRNA processing.
FT CHAIN 1..342
FT /note="S-adenosyl-L-methionine-dependent tRNA 4-
FT demethylwyosine synthase"
FT /id="PRO_0000425565"
FT DOMAIN 64..312
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01921"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01921"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01921"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01921"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01921"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01921"
SQ SEQUENCE 342 AA; 39927 MW; D0CD94040E0BEE46 CRC64;
MREMITIKPG KITVQANPNM PEEVANLFRK QHYEIVGRHS GVKLCHWLKK SLTEGRFCYK
QKFYGIHSHR CLQMTPVLAW CTHNCIFCWR PMETFLGTEL PQPWDDPEFI VEESIKAQRK
LLIGYKGNPK VDKKKFEEAW EPKHAAISLS GEPMLYPYMG DLVEEFHKRG FTTFIVTNGT
VPERLEEMIK EDKLPTQLYV SITAPDIETY NSVNIPMIPD GWERIMRFLE LMRDLPTRTV
VRLTLVKGEN MHSPEKYAKL ILKARPMFVE AKAYMFVGYS RNRLTINNMP SHQDIREFAE
ALVKHLPGYH IEDEYEPSRV VLIMRDDVDP QGTGVNGRFI KH
