UniProtKB - P42632 (TDCE_ECOLI)
Protein
PFL-like enzyme TdcE
Gene
tdcE
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate.1 Publication
Catalytic activityi
- EC:2.3.1.54
Activity regulationi
Dependent on PFL-activase.1 Publication
: L-threonine degradation via propanoate pathway Pathwayi
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:
- L-threonine dehydratase catabolic TdcB (tdcB), L-threonine dehydratase catabolic TdcB (tdcB)
- PFL-like enzyme TdcE (tdcE)
- no protein annotated in this organism
- Propionate kinase (tdcD), Propionate kinase (tdcD)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 423 | S-acetylcysteine intermediateBy similarity | 1 | |
Active sitei | 424 | Cysteine radical intermediateBy similarity | 1 |
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
Keywordsi
Molecular function | Acyltransferase, Transferase |
Enzyme and pathway databases
BioCyci | EcoCyc:KETOBUTFORMLY-INACT-MONOMER MetaCyc:KETOBUTFORMLY-INACT-MONOMER |
UniPathwayi | UPA00052;UER00508 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:tdcE Synonyms:yhaS Ordered Locus Names:b3114, JW5522 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
No discernible phenotype.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000166691 | 1 – 764 | PFL-like enzyme TdcEAdd BLAST | 764 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 739 | Glycine radicalPROSITE-ProRule annotation | 1 |
Keywords - PTMi
Organic radicalProteomic databases
jPOSTi | P42632 |
PaxDbi | P42632 |
PRIDEi | P42632 |
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
BioGRIDi | 4262415, 15 interactors |
DIPi | DIP-10972N |
IntActi | P42632, 2 interactors |
STRINGi | 511145.b3114 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 7 – 629 | PFLPROSITE-ProRule annotationAdd BLAST | 623 | |
Domaini | 636 – 764 | Glycine radicalPROSITE-ProRule annotationAdd BLAST | 129 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1882, Bacteria |
HOGENOMi | CLU_023898_0_0_6 |
InParanoidi | P42632 |
PhylomeDBi | P42632 |
Family and domain databases
CDDi | cd01678, PFL1, 1 hit |
InterProi | View protein in InterPro IPR005949, Form_AcTrfase IPR019777, Form_AcTrfase_GR_CS IPR001150, Gly_radical IPR004184, PFL_dom |
Pfami | View protein in Pfam PF01228, Gly_radical, 1 hit PF02901, PFL-like, 1 hit |
TIGRFAMsi | TIGR01255, pyr_form_ly_1, 1 hit |
PROSITEi | View protein in PROSITE PS00850, GLY_RADICAL_1, 1 hit PS51149, GLY_RADICAL_2, 1 hit PS51554, PFL, 1 hit |
i Sequence
Sequence statusi: Complete.
P42632-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence AAA57918 differs from that shown. Reason: Frameshift.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 |
PIRi | G65100 |
RefSeqi | WP_000861734.1, NZ_STEB01000001.1 YP_026205.1, NC_000913.3 |
Genome annotation databases
EnsemblBacteriai | AAT48170; AAT48170; b3114 BAE77162; BAE77162; BAE77162 |
GeneIDi | 57728239 947623 |
KEGGi | ecj:JW5522 eco:b3114 |
PATRICi | fig|1411691.4.peg.3616 |
Similar proteinsi
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 |
PIRi | G65100 |
RefSeqi | WP_000861734.1, NZ_STEB01000001.1 YP_026205.1, NC_000913.3 |
3D structure databases
SMRi | P42632 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4262415, 15 interactors |
DIPi | DIP-10972N |
IntActi | P42632, 2 interactors |
STRINGi | 511145.b3114 |
Proteomic databases
jPOSTi | P42632 |
PaxDbi | P42632 |
PRIDEi | P42632 |
Genome annotation databases
EnsemblBacteriai | AAT48170; AAT48170; b3114 BAE77162; BAE77162; BAE77162 |
GeneIDi | 57728239 947623 |
KEGGi | ecj:JW5522 eco:b3114 |
PATRICi | fig|1411691.4.peg.3616 |
Organism-specific databases
EchoBASEi | EB2612 |
Phylogenomic databases
eggNOGi | COG1882, Bacteria |
HOGENOMi | CLU_023898_0_0_6 |
InParanoidi | P42632 |
PhylomeDBi | P42632 |
Enzyme and pathway databases
UniPathwayi | UPA00052;UER00508 |
BioCyci | EcoCyc:KETOBUTFORMLY-INACT-MONOMER MetaCyc:KETOBUTFORMLY-INACT-MONOMER |
Miscellaneous databases
PROi | PR:P42632 |
Family and domain databases
CDDi | cd01678, PFL1, 1 hit |
InterProi | View protein in InterPro IPR005949, Form_AcTrfase IPR019777, Form_AcTrfase_GR_CS IPR001150, Gly_radical IPR004184, PFL_dom |
Pfami | View protein in Pfam PF01228, Gly_radical, 1 hit PF02901, PFL-like, 1 hit |
TIGRFAMsi | TIGR01255, pyr_form_ly_1, 1 hit |
PROSITEi | View protein in PROSITE PS00850, GLY_RADICAL_1, 1 hit PS51149, GLY_RADICAL_2, 1 hit PS51554, PFL, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TDCE_ECOLI | |
Accessioni | P42632Primary (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: | February 10, 2021 | |
This is version 149 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families