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Protein

Putative reactive intermediate deaminase TdcF

Gene

tdcF

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

Functioni

May be a post-translational regulator that controls the metabolic fate of L-threonine or the potentially toxic intermediate 2-ketobutyrate.

Pathwayi: L-threonine degradation via propanoate pathway

This protein is involved in the pathway L-threonine degradation via propanoate pathway, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway L-threonine degradation via propanoate pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei120Substrate1

GO - Molecular functioni

  • hydrolase activity Source: UniProtKB-KW
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • L-threonine catabolic process to propionate Source: UniProtKB-UniPathway
  • threonine metabolic process Source: UniProtKB

Keywordsi

Molecular functionHydrolase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:G7626-MONOMER
UniPathwayiUPA00052

Names & Taxonomyi

Protein namesi
Recommended name:
Putative reactive intermediate deaminase TdcF (EC:3.5.4.-)
Gene namesi
Name:tdcF
Synonyms:yhaR
Ordered Locus Names:b3113, JW5521
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12757 tdcF

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001703161 – 129Putative reactive intermediate deaminase TdcFAdd BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei58N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PaxDbiP0AGL2
PRIDEiP0AGL2

Interactioni

Subunit structurei

Homotrimer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259264, 16 interactors
DIPiDIP-48213N
STRINGi316385.ECDH10B_3287

Structurei

Secondary structure

1129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi8 – 10Combined sources3
Beta strandi14 – 16Combined sources3
Beta strandi19 – 22Combined sources4
Beta strandi24 – 29Combined sources6
Turni37 – 39Combined sources3
Helixi46 – 63Combined sources18
Helixi68 – 70Combined sources3
Beta strandi71 – 79Combined sources9
Helixi81 – 83Combined sources3
Helixi84 – 97Combined sources14
Beta strandi104 – 109Combined sources6
Helixi114 – 116Combined sources3
Beta strandi118 – 126Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UYJX-ray2.35A/B/C1-129[»]
2UYKX-ray1.60A/B/C1-129[»]
2UYNX-ray1.60A/B/C1-129[»]
2UYPX-ray2.44A/B/C1-129[»]
ProteinModelPortaliP0AGL2
SMRiP0AGL2
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AGL2

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni105 – 107Substrate binding3

Sequence similaritiesi

Belongs to the RutC family.Curated

Phylogenomic databases

eggNOGiENOG4105KME Bacteria
COG0251 LUCA
HOGENOMiHOG000267215
InParanoidiP0AGL2
KOiK09022
OMAiATDKAPQ
PhylomeDBiP0AGL2

Family and domain databases

Gene3Di3.30.1330.40, 1 hit
InterProiView protein in InterPro
IPR006056 RidA
IPR019897 RidA_CS
IPR035959 RutC-like_sf
IPR006175 YjgF/YER057c/UK114
PANTHERiPTHR11803 PTHR11803, 1 hit
PfamiView protein in Pfam
PF01042 Ribonuc_L-PSP, 1 hit
SUPFAMiSSF55298 SSF55298, 1 hit
TIGRFAMsiTIGR00004 TIGR00004, 1 hit
PROSITEiView protein in PROSITE
PS01094 UPF0076, 1 hit

Sequencei

Sequence statusi: Complete.

P0AGL2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIIETQRA PGAIGPYVQG VDLGSMVFTS GQIPVCPQTG EIPADVQDQA
60 70 80 90 100
RLSLENVKAI VVAAGLSVGD IIKMTVFITD LNDFATINEV YKQFFDEHQA
110 120
TYPTRSCVQV ARLPKDVKLE IEAIAVRSA
Length:129
Mass (Da):14,007
Last modified:December 20, 2005 - v1
Checksum:iD5159CB729CDDB7B
GO

Sequence cautioni

The sequence AAA57917 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA Translation: AAA57917.1 Different initiation.
U00096 Genomic DNA Translation: AAC76148.2
AP009048 Genomic DNA Translation: BAE77161.1
PIRiF65100
RefSeqiNP_417583.4, NC_000913.3
WP_000719990.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76148; AAC76148; b3113
BAE77161; BAE77161; BAE77161
GeneIDi947624
KEGGiecj:JW5521
eco:b3113
PATRICifig|511145.12.peg.3207

Similar proteinsi

Entry informationi

Entry nameiTDCF_ECOLI
AccessioniPrimary (citable) accession number: P0AGL2
Secondary accession number(s): P42631, Q2M995
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 28, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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