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Protein

PFL-like enzyme TdcE

Gene

tdcE

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

Functioni

Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate.1 Publication

Catalytic activityi

Propionyl-CoA + formate = CoA + 2-oxobutanoate.
Acetyl-CoA + formate = CoA + pyruvate.

Enzyme regulationi

Dependent on PFL-activase.1 Publication

Pathwayi: L-threonine degradation via propanoate pathway

This protein is involved in step 2 of the subpathway that synthesizes propanoate from L-threonine.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. L-threonine dehydratase catabolic TdcB (tdcB)
  2. PFL-like enzyme TdcE (tdcE)
  3. no protein annotated in this organism
  4. Propionate kinase (tdcD)
This subpathway is part of the pathway L-threonine degradation via propanoate pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes propanoate from L-threonine, the pathway L-threonine degradation via propanoate pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei423 – 4231S-acetylcysteine intermediateBy similarity
Active sitei424 – 4241Cysteine radical intermediateBy similarity

GO - Molecular functioni

  • 2-ketobutyrate formate-lyase activity Source: EcoliWiki
  • formate C-acetyltransferase activity Source: EcoCyc

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • L-threonine catabolic process to propionate Source: EcoliWiki
  • threonine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:KETOBUTFORMLY-INACT-MONOMER.
ECOL316407:JW5522-MONOMER.
MetaCyc:KETOBUTFORMLY-INACT-MONOMER.
UniPathwayiUPA00052; UER00508.

Names & Taxonomyi

Protein namesi
Recommended name:
PFL-like enzyme TdcE
Alternative name(s):
Keto-acid formate acetyltransferase
Keto-acid formate-lyase
Ketobutyrate formate-lyase (EC:2.3.1.-)
Short name:
KFL
Pyruvate formate-lyase (EC:2.3.1.54)
Short name:
PFL
Gene namesi
Name:tdcE
Synonyms:yhaS
Ordered Locus Names:b3114, JW5522
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12758. tdcE.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: GO_Central
  • membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

No discernible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 764764PFL-like enzyme TdcEPRO_0000166691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei739 – 7391Glycine radicalPROSITE-ProRule annotation

Keywords - PTMi

Organic radical

Proteomic databases

PaxDbiP42632.

Expressioni

Inductioni

Strongly repressed by glucose. Anaerobic growth of the pfl mutant in the presence of cAMP and L-threonine induced synthesis of TdcE.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4262415. 15 interactions.
DIPiDIP-10972N.
IntActiP42632. 2 interactions.
MINTiMINT-1231745.
STRINGi511145.b3114.

Structurei

3D structure databases

ProteinModelPortaliP42632.
SMRiP42632. Positions 13-764.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 629623PFLPROSITE-ProRule annotationAdd
BLAST
Domaini636 – 764129Glycine radicalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 glycine radical domain.PROSITE-ProRule annotation
Contains 1 PFL domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105C6N. Bacteria.
COG1882. LUCA.
HOGENOMiHOG000011346.
InParanoidiP42632.
KOiK00656.
OMAiGIRQENA.
PhylomeDBiP42632.

Family and domain databases

InterProiIPR005949. Form_AcTrfase.
IPR019777. Form_AcTrfase_GR_CS.
IPR001150. Gly_radical.
IPR004184. PFL_dom.
[Graphical view]
PfamiPF01228. Gly_radical. 1 hit.
PF02901. PFL-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000379. For_Ac_trans_1. 1 hit.
TIGRFAMsiTIGR01255. pyr_form_ly_1. 1 hit.
PROSITEiPS00850. GLY_RADICAL_1. 1 hit.
PS51149. GLY_RADICAL_2. 1 hit.
PS51554. PFL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVDIDTSDK LYADAWLGFK GTDWKNEINV RDFIQHNYTP YEGDESFLAE
60 70 80 90 100
ATPATTELWE KVMEGIRIEN ATHAPVDFDT NIATTITAHD AGYINQPLEK
110 120 130 140 150
IVGLQTDAPL KRALHPFGGI NMIKSSFHAY GREMDSEFEY LFTDLRKTHN
160 170 180 190 200
QGVFDVYSPD MLRCRKSGVL TGLPDGYGRG RIIGDYRRVA LYGISYLVRE
210 220 230 240 250
RELQFADLQS RLEKGEDLEA TIRLREELAE HRHALLQIQE MAAKYGFDIS
260 270 280 290 300
RPAQNAQEAV QWLYFAYLAA VKSQNGGAMS LGRTASFLDI YIERDFKAGV
310 320 330 340 350
LNEQQAQELI DHFIMKIRMV RFLRTPEFDS LFSGDPIWAT EVIGGMGLDG
360 370 380 390 400
RTLVTKNSFR YLHTLHTMGP APEPNLTILW SEELPIAFKK YAAQVSIVTS
410 420 430 440 450
SLQYENDDLM RTDFNSDDYA IACCVSPMVI GKQMQFFGAR ANLAKTLLYA
460 470 480 490 500
INGGVDEKLK IQVGPKTAPL MDDVLDYDKV MDSLDHFMDW LAVQYISALN
510 520 530 540 550
IIHYMHDKYS YEASLMALHD RDVYRTMACG IAGLSVATDS LSAIKYARVK
560 570 580 590 600
PIRDENGLAV DFEIDGEYPQ YGNNDERVDS IACDLVERFM KKIKALPTYR
610 620 630 640 650
NAVPTQSILT ITSNVVYGQK TGNTPDGRRA GTPFAPGANP MHGRDRKGAV
660 670 680 690 700
ASLTSVAKLP FTYAKDGISY TFSIVPAALG KEDPVRKTNL VGLLDGYFHH
710 720 730 740 750
EADVEGGQHL NVNVMNREML LDAIEHPEKY PNLTIRVSGY AVRFNALTRE
760
QQQDVISRTF TQAL
Length:764
Mass (Da):85,936
Last modified:October 11, 2004 - v2
Checksum:i2C4F46944118449B
GO

Sequence cautioni

The sequence AAA57918 differs from that shown. Reason: Frameshift at position 742. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA57918.1. Frameshift.
U00096 Genomic DNA. Translation: AAT48170.1.
AP009048 Genomic DNA. Translation: BAE77162.1.
PIRiG65100.
RefSeqiWP_000861734.1. NZ_LN832404.1.
YP_026205.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48170; AAT48170; b3114.
BAE77162; BAE77162; BAE77162.
GeneIDi947623.
KEGGiecj:JW5522.
eco:b3114.
PATRICi32121644. VBIEscCol129921_3208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA57918.1. Frameshift.
U00096 Genomic DNA. Translation: AAT48170.1.
AP009048 Genomic DNA. Translation: BAE77162.1.
PIRiG65100.
RefSeqiWP_000861734.1. NZ_LN832404.1.
YP_026205.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP42632.
SMRiP42632. Positions 13-764.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262415. 15 interactions.
DIPiDIP-10972N.
IntActiP42632. 2 interactions.
MINTiMINT-1231745.
STRINGi511145.b3114.

Proteomic databases

PaxDbiP42632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48170; AAT48170; b3114.
BAE77162; BAE77162; BAE77162.
GeneIDi947623.
KEGGiecj:JW5522.
eco:b3114.
PATRICi32121644. VBIEscCol129921_3208.

Organism-specific databases

EchoBASEiEB2612.
EcoGeneiEG12758. tdcE.

Phylogenomic databases

eggNOGiENOG4105C6N. Bacteria.
COG1882. LUCA.
HOGENOMiHOG000011346.
InParanoidiP42632.
KOiK00656.
OMAiGIRQENA.
PhylomeDBiP42632.

Enzyme and pathway databases

UniPathwayiUPA00052; UER00508.
BioCyciEcoCyc:KETOBUTFORMLY-INACT-MONOMER.
ECOL316407:JW5522-MONOMER.
MetaCyc:KETOBUTFORMLY-INACT-MONOMER.

Miscellaneous databases

PROiP42632.

Family and domain databases

InterProiIPR005949. Form_AcTrfase.
IPR019777. Form_AcTrfase_GR_CS.
IPR001150. Gly_radical.
IPR004184. PFL_dom.
[Graphical view]
PfamiPF01228. Gly_radical. 1 hit.
PF02901. PFL-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000379. For_Ac_trans_1. 1 hit.
TIGRFAMsiTIGR01255. pyr_form_ly_1. 1 hit.
PROSITEiPS00850. GLY_RADICAL_1. 1 hit.
PS51149. GLY_RADICAL_2. 1 hit.
PS51554. PFL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTDCE_ECOLI
AccessioniPrimary (citable) accession number: P42632
Secondary accession number(s): Q2M994, Q6BF44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 11, 2004
Last modified: September 7, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.