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Protein

tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase

Gene

taw2

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

Functioni

S-adenosyl-L-methionine-dependent transferase that acts as a component of the wyosine derivatives biosynthesis pathway. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of tRNA(Phe).UniRule annotation1 Publication

Catalytic activityi

S-adenosyl-L-methionine + 4-demethylwyosine(37) in tRNA(Phe) = S-methyl-5'-thioadenosine + 7-((3S)-3-amino-3-carboxypropyl)-4-demethylwyosine(37) in tRNA(Phe).UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091S-adenosyl-L-methionine
Binding sitei116 – 1161S-adenosyl-L-methionine
Binding sitei155 – 1551S-adenosyl-L-methionine

GO - Molecular functioni

GO - Biological processi

  • tRNA modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18048.
PHOR70601:GJWR-789-MONOMER.
BRENDAi2.5.1.114. 5244.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferaseUniRule annotation (EC:2.5.1.114UniRule annotation)
Alternative name(s):
PhTYW2
tRNA wyosine derivatives biosynthesis protein Taw2UniRule annotation
Gene namesi
Name:taw2UniRule annotation
Ordered Locus Names:PH0793
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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761R → A: Loss of activity. 1 Publication
Mutagenesisi107 – 1071M → A: Decrease in activity. 1 Publication
Mutagenesisi112 – 1121N → A: Loss of activity. 1 Publication
Mutagenesisi116 – 1161R → A: Loss of activity. 1 Publication
Mutagenesisi138 – 1381H → A: Decrease in activity. 1 Publication
Mutagenesisi142 – 1421P → A: Decrease in activity. 1 Publication
Mutagenesisi155 – 1551E → A: Loss of activity. 1 Publication
Mutagenesisi183 – 1831D → A: Decrease in activity. 1 Publication
Mutagenesisi199 – 1991G → N: Decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 278278tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferasePRO_0000407849Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi70601.PH0793.

Structurei

Secondary structure

1
278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 148Combined sources
Turni15 – 173Combined sources
Helixi20 – 256Combined sources
Beta strandi31 – 333Combined sources
Beta strandi36 – 394Combined sources
Helixi46 – 483Combined sources
Helixi49 – 6012Combined sources
Beta strandi63 – 675Combined sources
Beta strandi81 – 844Combined sources
Beta strandi89 – 946Combined sources
Beta strandi97 – 1026Combined sources
Turni103 – 1053Combined sources
Helixi110 – 1123Combined sources
Helixi113 – 12210Combined sources
Beta strandi128 – 1314Combined sources
Turni135 – 1395Combined sources
Helixi140 – 1456Combined sources
Beta strandi150 – 1545Combined sources
Helixi158 – 17013Combined sources
Turni174 – 1763Combined sources
Beta strandi177 – 1804Combined sources
Turni184 – 1863Combined sources
Beta strandi193 – 1986Combined sources
Helixi204 – 2074Combined sources
Helixi208 – 2147Combined sources
Beta strandi215 – 22814Combined sources
Helixi229 – 2313Combined sources
Turni232 – 2365Combined sources
Helixi237 – 24610Combined sources
Beta strandi250 – 26213Combined sources
Turni263 – 2653Combined sources
Beta strandi266 – 27611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A25X-ray2.30A1-278[»]
3A26X-ray2.50A1-278[»]
3K6RX-ray2.10A1-278[»]
ProteinModelPortaliO58523.
SMRiO58523. Positions 19-278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58523.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 1842S-adenosyl-L-methionine binding

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG10124. Archaea.
COG2520. LUCA.
HOGENOMiHOG000222903.
KOiK07055.
OMAiGGILHYH.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01922. TYW2_archaea.
InterProiIPR030382. MeTrfase_TRM5/TYW2.
IPR029063. SAM-dependent_MTases.
IPR030867. TYW2_archaea.
[Graphical view]
PfamiPF02475. Met_10. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51684. SAM_MT_TRM5_TYW2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O58523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTQGIKPRI REILSKELPE ELVKLLPKRW VRIGDVLLLP LRPELEPYKH
60 70 80 90 100
RIAEVYAEVL GVKTVLRKGH IHGETRKPDY ELLYGSDTVT VHVENGIKYK
110 120 130 140 150
LDVAKIMFSP ANVKERVRMA KVAKPDELVV DMFAGIGHLS LPIAVYGKAK
160 170 180 190 200
VIAIEKDPYT FKFLVENIHL NKVEDRMSAY NMDNRDFPGE NIADRILMGY
210 220 230 240 250
VVRTHEFIPK ALSIAKDGAI IHYHNTVPEK LMPREPFETF KRITKEYGYD
260 270
VEKLNELKIK RYAPGVWHVV LDLRVFKS
Length:278
Mass (Da):32,151
Last modified:August 1, 1998 - v1
Checksum:i392887387506C3F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29886.1.
PIRiD71128.
RefSeqiWP_010884887.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA29886; BAA29886; BAA29886.
GeneIDi1443122.
KEGGipho:PH0793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29886.1.
PIRiD71128.
RefSeqiWP_010884887.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A25X-ray2.30A1-278[»]
3A26X-ray2.50A1-278[»]
3K6RX-ray2.10A1-278[»]
ProteinModelPortaliO58523.
SMRiO58523. Positions 19-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA29886; BAA29886; BAA29886.
GeneIDi1443122.
KEGGipho:PH0793.

Phylogenomic databases

eggNOGiarCOG10124. Archaea.
COG2520. LUCA.
HOGENOMiHOG000222903.
KOiK07055.
OMAiGGILHYH.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18048.
PHOR70601:GJWR-789-MONOMER.
BRENDAi2.5.1.114. 5244.

Miscellaneous databases

EvolutionaryTraceiO58523.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01922. TYW2_archaea.
InterProiIPR030382. MeTrfase_TRM5/TYW2.
IPR029063. SAM-dependent_MTases.
IPR030867. TYW2_archaea.
[Graphical view]
PfamiPF02475. Met_10. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51684. SAM_MT_TRM5_TYW2. 1 hit.
[Graphical view]
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. "Structural basis of AdoMet-dependent aminocarboxypropyl transfer reaction catalyzed by tRNA-wybutosine synthesizing enzyme, TYW2."
    Umitsu M., Nishimasu H., Noma A., Suzuki T., Ishitani R., Nureki O.
    Proc. Natl. Acad. Sci. U.S.A. 106:15616-15621(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH S-ADENOSYL-L-METHIONINE AND 5'-DEOXY-5'-METHYLTHIOADENOSINE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF ARG-76; MET-107; ASN-112; ARG-116; HIS-138; PRO-142; GLU-155; ASP-183 AND GLY-199.
  4. "Crystal structure of protein PH0793 from Pyrococcus horikoshii."
    Midwest center for structural genomics (MCSG)
    Submitted (OCT-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).

Entry informationi

Entry nameiTYW2_PYRHO
AccessioniPrimary (citable) accession number: O58523
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 94 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.