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Protein

tRNA N6-adenosine threonylcarbamoyltransferase

Gene

tsaD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. May also be involved in the metabolism of glycated proteins, but does not show sialoglycoprotease activity against glycophorin A.3 Publications

Catalytic activityi

L-threonylcarbamoyladenylate + adenine(37) in tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.UniRule annotation1 Publication

Cofactori

Fe2+UniRule annotationNote: Binds 1 Fe2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi111IronUniRule annotation1
Metal bindingi115IronUniRule annotation1
Binding sitei167SubstrateUniRule annotation1
Binding sitei180Substrate; via amide nitrogenUniRule annotation1
Binding sitei272SubstrateUniRule annotation1
Metal bindingi300IronUniRule annotation1

GO - Molecular functioni

  • glycoprotein binding Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • iron ion binding Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • metalloendopeptidase activity Source: InterPro
  • N(6)-L-threonylcarbamoyladenine synthase Source: UniProtKB-EC

GO - Biological processi

  • tRNA threonylcarbamoyladenosine modification Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11171-MONOMER.
ECOL316407:JW3036-MONOMER.
MetaCyc:EG11171-MONOMER.
BRENDAi2.6.99.4. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA N6-adenosine threonylcarbamoyltransferaseUniRule annotation (EC:2.3.1.234UniRule annotation1 Publication)
Alternative name(s):
N6-L-threonylcarbamoyladenine synthaseUniRule annotation
Short name:
t(6)A synthaseUniRule annotation
t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaDUniRule annotation
tRNA threonylcarbamoyladenosine biosynthesis protein TsaDUniRule annotation
Gene namesi
Name:tsaDUniRule annotation
Synonyms:gcp, ygjD
Ordered Locus Names:b3064, JW3036
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11171. tsaD.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • EKC/KEOPS complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Appears essential for growth, since no null mutants can be obtained. Conditional depletion of this gene prevents t6A37 modification, and leads to pleiotropic phenotypes including increased or reduced cell size, unusual distribution of DNA around the cell periphery, nucleoid loss, and membrane/cell envelope defects. These phenotypes could be indirect effects of severe translation defects. The TsaD depletion phenotype is suppressed by overexpressing the response regulator RstA.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000969621 – 337tRNA N6-adenosine threonylcarbamoyltransferaseAdd BLAST337

Post-translational modificationi

Can be proteolytically processed in vitro by TsaB.1 Publication

Proteomic databases

EPDiP05852.
PaxDbiP05852.
PRIDEiP05852.

Interactioni

Subunit structurei

Homodimer. Interacts with TsaB; may form a heterodimer with TsaB. Also interacts with TsaC.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
tsaBP762566EBI-561994,EBI-560669

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261402. 64 interactors.
DIPiDIP-9749N.
IntActiP05852. 14 interactors.
STRINGi511145.b3064.

Structurei

Secondary structure

1337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Beta strandi9 – 19Combined sources11
Turni20 – 22Combined sources3
Beta strandi23 – 31Combined sources9
Helixi33 – 36Combined sources4
Helixi37 – 39Combined sources3
Helixi44 – 66Combined sources23
Helixi70 – 72Combined sources3
Beta strandi75 – 83Combined sources9
Helixi85 – 102Combined sources18
Beta strandi106 – 110Combined sources5
Helixi111 – 117Combined sources7
Helixi118 – 121Combined sources4
Beta strandi122 – 124Combined sources3
Beta strandi128 – 135Combined sources8
Beta strandi140 – 147Combined sources8
Beta strandi151 – 159Combined sources9
Helixi162 – 172Combined sources11
Helixi180 – 187Combined sources8
Beta strandi203 – 205Combined sources3
Helixi212 – 223Combined sources12
Helixi229 – 258Combined sources30
Beta strandi262 – 267Combined sources6
Helixi268 – 271Combined sources4
Helixi273 – 285Combined sources13
Beta strandi289 – 291Combined sources3
Helixi295 – 298Combined sources4
Helixi303 – 314Combined sources12
Helixi331 – 333Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WQ4X-ray2.33A/B1-337[»]
4WQ5X-ray2.33A/B1-337[»]
4YDUX-ray2.33A/B1-337[»]
ProteinModelPortaliP05852.
SMRiP05852.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni134 – 138Substrate bindingUniRule annotation5

Sequence similaritiesi

Belongs to the KAE1 / TsaD family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CPM. Bacteria.
COG0533. LUCA.
HOGENOMiHOG000109568.
InParanoidiP05852.
KOiK01409.
OMAiRDHVKRM.
PhylomeDBiP05852.

Family and domain databases

HAMAPiMF_01445. TsaD. 1 hit.
InterProiIPR000905. Gcp-like_dom.
IPR017861. KAE1/TsaD.
IPR017860. Peptidase_M22_CS.
IPR022450. TsaD.
[Graphical view]
PfamiPF00814. Peptidase_M22. 1 hit.
[Graphical view]
PRINTSiPR00789. OSIALOPTASE.
TIGRFAMsiTIGR00329. gcp_kae1. 1 hit.
TIGR03723. T6A_TsaD_YgjD. 1 hit.
PROSITEiPS01016. GLYCOPROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05852-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLGIETSC DETGIAIYDD EKGLLANQLY SQVKLHADYG GVVPELASRD
60 70 80 90 100
HVRKTVPLIQ AALKESGLTA KDIDAVAYTA GPGLVGALLV GATVGRSLAF
110 120 130 140 150
AWDVPAIPVH HMEGHLLAPM LEDNPPEFPF VALLVSGGHT QLISVTGIGQ
160 170 180 190 200
YELLGESIDD AAGEAFDKTA KLLGLDYPGG PLLSKMAAQG TAGRFVFPRP
210 220 230 240 250
MTDRPGLDFS FSGLKTFAAN TIRDNGTDDQ TRADIARAFE DAVVDTLMIK
260 270 280 290 300
CKRALDQTGF KRLVMAGGVS ANRTLRAKLA EMMKKRRGEV FYARPEFCTD
310 320 330
NGAMIAYAGM VRFKAGATAD LGVSVRPRWP LAELPAA
Length:337
Mass (Da):36,008
Last modified:August 29, 2003 - v2
Checksum:iAD676E3B635EC637
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti136S → C in AAA72575 (PubMed:3297921).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16194 Genomic DNA. Translation: AAA72575.1.
U28379 Genomic DNA. Translation: AAA89144.1.
U00096 Genomic DNA. Translation: AAC76100.1.
AP009048 Genomic DNA. Translation: BAE77115.1.
PIRiF65094. QQECR6.
RefSeqiNP_417536.1. NC_000913.3.
WP_001264352.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76100; AAC76100; b3064.
BAE77115; BAE77115; BAE77115.
GeneIDi947578.
KEGGiecj:JW3036.
eco:b3064.
PATRICi32121542. VBIEscCol129921_3158.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16194 Genomic DNA. Translation: AAA72575.1.
U28379 Genomic DNA. Translation: AAA89144.1.
U00096 Genomic DNA. Translation: AAC76100.1.
AP009048 Genomic DNA. Translation: BAE77115.1.
PIRiF65094. QQECR6.
RefSeqiNP_417536.1. NC_000913.3.
WP_001264352.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WQ4X-ray2.33A/B1-337[»]
4WQ5X-ray2.33A/B1-337[»]
4YDUX-ray2.33A/B1-337[»]
ProteinModelPortaliP05852.
SMRiP05852.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261402. 64 interactors.
DIPiDIP-9749N.
IntActiP05852. 14 interactors.
STRINGi511145.b3064.

Proteomic databases

EPDiP05852.
PaxDbiP05852.
PRIDEiP05852.

Protocols and materials databases

DNASUi947578.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76100; AAC76100; b3064.
BAE77115; BAE77115; BAE77115.
GeneIDi947578.
KEGGiecj:JW3036.
eco:b3064.
PATRICi32121542. VBIEscCol129921_3158.

Organism-specific databases

EchoBASEiEB1158.
EcoGeneiEG11171. tsaD.

Phylogenomic databases

eggNOGiENOG4105CPM. Bacteria.
COG0533. LUCA.
HOGENOMiHOG000109568.
InParanoidiP05852.
KOiK01409.
OMAiRDHVKRM.
PhylomeDBiP05852.

Enzyme and pathway databases

BioCyciEcoCyc:EG11171-MONOMER.
ECOL316407:JW3036-MONOMER.
MetaCyc:EG11171-MONOMER.
BRENDAi2.6.99.4. 2026.

Miscellaneous databases

PROiP05852.

Family and domain databases

HAMAPiMF_01445. TsaD. 1 hit.
InterProiIPR000905. Gcp-like_dom.
IPR017861. KAE1/TsaD.
IPR017860. Peptidase_M22_CS.
IPR022450. TsaD.
[Graphical view]
PfamiPF00814. Peptidase_M22. 1 hit.
[Graphical view]
PRINTSiPR00789. OSIALOPTASE.
TIGRFAMsiTIGR00329. gcp_kae1. 1 hit.
TIGR03723. T6A_TsaD_YgjD. 1 hit.
PROSITEiPS01016. GLYCOPROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTSAD_ECOLI
AccessioniPrimary (citable) accession number: P05852
Secondary accession number(s): Q2M9E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: August 29, 2003
Last modified: November 2, 2016
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

TsaBCDE are necessary and sufficient for tRNA(NNU) t6A37 threonylcarbamoyladenosine modification in vitro in E.coli.1 Publication

Caution

Was proposed to be a ligase for bicarbonate and threonine (PubMed:21285948): in the first step, TsaD would catalyze transfer of a gamma-phosphate group from ATP to bicarbonate, yielding carboxyphosphate and ADP; carboxyphosphate would then react with the threonine amine, producing N-carbamoylthreonine and phosphate. However, the protein ortholog in B.subtilis was shown to be involved in another step of t6A37 biosynthesis, i.e. the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB (PubMed:23072323). The protein ortholog in yeast (QRI7) was also shown to catalyze this step, and does not require the presence of additional proteins (PubMed:23620299).1 Publication
The well-known t6A modification appears to be a hydrolyzed artifact of natural cyclic t6A (ct6A) that occurs during the preparation and handling of tRNA in E.coli and many other species (PubMed:23242255). In these species, the t6A modification is processed further by dehydration into ct6A, a reaction catalyzed by TcdA.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.