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Protein

S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase

Gene

taw1

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe).UniRule annotation

Catalytic activityi

N(1)-methylguanine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + L-methionine + 5'-deoxyadenosine + CO2 + H2O.UniRule annotation

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Iron-sulfur 1 (2Fe-2S)Curated
Metal bindingi58 – 581Iron-sulfur 1 (2Fe-2S)Curated
Metal bindingi71 – 711Iron-sulfur 1 (2Fe-2S)Curated
Metal bindingi81 – 811Iron-sulfur 2 (4Fe-4S-S-AdoMet)Curated
Metal bindingi85 – 851Iron-sulfur 2 (4Fe-4S-S-AdoMet)Curated
Metal bindingi88 – 881Iron-sulfur 2 (4Fe-4S-S-AdoMet)Curated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18047.
PHOR70601:GJWR-1705-MONOMER.
BRENDAi4.1.3.44. 5244.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthaseUniRule annotation (EC:4.1.3.44UniRule annotation)
Alternative name(s):
tRNA wyosine derivatives biosynthesis protein Taw1UniRule annotation
Gene namesi
Name:taw1UniRule annotation
Ordered Locus Names:PH1705
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthasePRO_0000407857Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

IntActiO59412. 1 interaction.
MINTiMINT-1502553.
STRINGi70601.PH1705.

Structurei

Secondary structure

1
342
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 309Combined sources
Beta strandi34 – 374Combined sources
Beta strandi40 – 423Combined sources
Helixi48 – 547Combined sources
Helixi59 – 646Combined sources
Helixi68 – 703Combined sources
Beta strandi71 – 766Combined sources
Beta strandi91 – 944Combined sources
Helixi107 – 12216Combined sources
Helixi133 – 1397Combined sources
Beta strandi144 – 1474Combined sources
Beta strandi149 – 1513Combined sources
Helixi153 – 1553Combined sources
Helixi159 – 16810Combined sources
Beta strandi172 – 1776Combined sources
Helixi182 – 1909Combined sources
Beta strandi196 – 2027Combined sources
Helixi207 – 2148Combined sources
Beta strandi216 – 2194Combined sources
Helixi221 – 23212Combined sources
Beta strandi236 – 24510Combined sources
Turni247 – 2493Combined sources
Helixi254 – 26411Combined sources
Beta strandi267 – 2737Combined sources
Helixi286 – 2883Combined sources
Helixi292 – 30312Combined sources
Beta strandi309 – 3157Combined sources
Helixi316 – 3183Combined sources
Beta strandi320 – 3256Combined sources
Beta strandi328 – 3336Combined sources
Helixi334 – 3363Combined sources
Beta strandi337 – 3393Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YX0X-ray2.21A1-342[»]
ProteinModelPortaliO59412.
SMRiO59412. Positions 11-342.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59412.

Family & Domainsi

Sequence similaritiesi

Belongs to the TYW1 family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04174. Archaea.
COG0731. LUCA.
HOGENOMiHOG000224906.
KOiK15449.
OMAiVKLCHWL.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01921. TYW1_archaea.
InterProiIPR013785. Aldolase_TIM.
IPR007197. rSAM.
IPR013917. tRNA_wybutosine-synth.
IPR023993. TYW1_archaea.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
PF08608. Wyosine_form. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03972. rSAM_TYW1. 1 hit.

Sequencei

Sequence statusi: Complete.

O59412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMEMITIKPG KITVQANPNM PKEVAELFRK QHYEIVGRHS GVKLCHWLKK
60 70 80 90 100
SLTEGRFCYK QKFYGIHSHR CLQMTPVLAW CTHNCIFCWR PMENFLGTEL
110 120 130 140 150
PQPWDDPAFI VEESIKAQRK LLIGYKGNPK VDKKKFEEAW NPTHAAISLS
160 170 180 190 200
GEPMLYPYMG DLVEEFHKRG FTTFIVTNGT IPERLEEMIK EDKLPTQLYV
210 220 230 240 250
SITAPDIETY NSVNIPMIPD GWERILRFLE LMRDLPTRTV VRLTLVKGEN
260 270 280 290 300
MHSPEKYAKL ILKARPMFVE AKAYMFVGYS RNRLTINNMP SHQDIREFAE
310 320 330 340
ALVKHLPGYH IEDEYEPSRV VLIMRDDVDP QGTGVEGRFI KH
Length:342
Mass (Da):39,840
Last modified:August 1, 1998 - v1
Checksum:iF321AF462AA262D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30819.1.
PIRiD71178.

Genome annotation databases

EnsemblBacteriaiBAA30819; BAA30819; BAA30819.
KEGGipho:PH1705.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30819.1.
PIRiD71178.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YX0X-ray2.21A1-342[»]
ProteinModelPortaliO59412.
SMRiO59412. Positions 11-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO59412. 1 interaction.
MINTiMINT-1502553.
STRINGi70601.PH1705.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30819; BAA30819; BAA30819.
KEGGipho:PH1705.

Phylogenomic databases

eggNOGiarCOG04174. Archaea.
COG0731. LUCA.
HOGENOMiHOG000224906.
KOiK15449.
OMAiVKLCHWL.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18047.
PHOR70601:GJWR-1705-MONOMER.
BRENDAi4.1.3.44. 5244.

Miscellaneous databases

EvolutionaryTraceiO59412.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01921. TYW1_archaea.
InterProiIPR013785. Aldolase_TIM.
IPR007197. rSAM.
IPR013917. tRNA_wybutosine-synth.
IPR023993. TYW1_archaea.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
PF08608. Wyosine_form. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03972. rSAM_TYW1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. Cited for: GENE NAME.
  3. "Structure of an archaeal TYW1, the enzyme catalyzing the second step of wye-base biosynthesis."
    Goto-Ito S., Ishii R., Ito T., Shibata R., Fusatomi E., Sekine S.I., Bessho Y., Yokoyama S.
    Acta Crystallogr. D 63:1059-1068(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS), COFACTOR, SUBUNIT.

Entry informationi

Entry nameiTYW1_PYRHO
AccessioniPrimary (citable) accession number: O59412
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.