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P0AGL2 (TDCF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative reactive intermediate deaminase TdcF
EC=3.5.4.-
Gene names
Name:tdcF
Synonyms:yhaR
Ordered Locus Names:b3113, JW5521
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Pathway

Amino-acid degradation; L-threonine degradation via propanoate pathway.

Subunit structure

Homotrimer. Ref.4

Sequence similarities

Belongs to the RutC family.

Sequence caution

The sequence AAA57917.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 129129Putative reactive intermediate deaminase TdcF
PRO_0000170316

Regions

Region105 – 1073Substrate binding

Sites

Binding site1201Substrate

Amino acid modifications

Modified residue581N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

1 ........................... 129
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AGL2 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: D5159CB729CDDB7B

FASTA12914,007
        10         20         30         40         50         60 
MKKIIETQRA PGAIGPYVQG VDLGSMVFTS GQIPVCPQTG EIPADVQDQA RLSLENVKAI 

        70         80         90        100        110        120 
VVAAGLSVGD IIKMTVFITD LNDFATINEV YKQFFDEHQA TYPTRSCVQV ARLPKDVKLE 


IEAIAVRSA

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate."
Hesslinger C., Fairhurst S.A., Sawers G.
Mol. Microbiol. 27:477-492(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE NAME.
[4]"The crystal structure of Escherichia coli TdcF, a member of the highly conserved YjgF/YER057c/UK114 family."
Burman J.D., Stevenson C.E., Sawers R.G., Lawson D.M.
BMC Struct. Biol. 7:30-30(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U18997 Genomic DNA. Translation: AAA57917.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76148.2.
AP009048 Genomic DNA. Translation: BAE77161.1.
PIRF65100.
RefSeqNP_417583.4. NC_000913.2.
YP_491302.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0AGL2.
SMRP0AGL2. Positions 2-128.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48213N.
STRING511145.b3113.

Proteomic databases

PaxDbP0AGL2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76148; AAC76148; b3113.
BAE77161; BAE77161; BAE77161.
GeneID12930270.
947624.
KEGGecj:Y75_p3036.
eco:b3113.
PATRIC32121642. VBIEscCol129921_3207.

Organism-specific databases

EchoBASEEB2611.
EcoGeneEG12757. tdcF.

Phylogenomic databases

eggNOGCOG0251.
HOGENOMHOG000267215.
KOK07567.
OMAPYNQAVV.
ProtClustDBPRK11401.

Enzyme and pathway databases

BioCycEcoCyc:G7626-MONOMER.
ECOL316407:JW5521-MONOMER.
UniPathwayUPA00052.

Gene expression databases

GenevestigatorP0AGL2.

Family and domain databases

Gene3D3.30.1330.40. 1 hit.
InterProIPR013813. Endoribo_LPSP/chorism_mut-like.
IPR006056. YjgF-like.
IPR019897. YjgF-like_CS.
IPR006175. YjgF/Yer057p/UK114.
[Graphical view]
PANTHERPTHR11803. PTHR11803. 1 hit.
PfamPF01042. Ribonuc_L-PSP. 1 hit.
[Graphical view]
SUPFAMSSF55298. YjgF/chorismate_mutase-like. 1 hit.
TIGRFAMsTIGR00004. TIGR00004. 1 hit.
PROSITEPS01094. UPF0076. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AGL2.

Entry information

Entry nameTDCF_ECOLI
AccessionPrimary (citable) accession number: P0AGL2
Secondary accession number(s): P42631, Q2M995
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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