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Protein

Propionate kinase

Gene

tdcD

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

Functioni

Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor.UniRule annotation1 Publication

Catalytic activityi

ATP + propanoate = ADP + propanoyl phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Pathwayi: L-threonine degradation via propanoate pathway

This protein is involved in step 4 of the subpathway that synthesizes propanoate from L-threonine.UniRule annotation
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
Metal bindingi11 – 111MagnesiumUniRule annotation
Binding sitei11 – 111ATPUniRule annotation
Binding sitei18 – 181ATPUniRule annotation
Binding sitei86 – 861SubstrateUniRule annotation
Active sitei143 – 1431Proton donor/acceptorUniRule annotation
Binding sitei175 – 1751ATPUniRule annotation
Sitei175 – 1751Transition state stabilizerUniRule annotation
Sitei236 – 2361Transition state stabilizerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi203 – 2075ATPUniRule annotation
Nucleotide bindingi278 – 2803ATPUniRule annotation
Nucleotide bindingi326 – 3305ATPUniRule annotation

GO - Molecular functioni

  • acetate kinase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • propionate kinase activity Source: EcoCyc

GO - Biological processi

  • anaerobic amino acid catabolic process Source: EcoCyc
  • L-threonine catabolic process to propionate Source: UniProtKB-UniPathway
  • threonine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PROPKIN-MONOMER.
ECOL316407:JW5806-MONOMER.
MetaCyc:PROPKIN-MONOMER.
UniPathwayiUPA00052; UER00510.

Names & Taxonomyi

Protein namesi
Recommended name:
Propionate kinaseUniRule annotation (EC:2.7.2.15UniRule annotation)
Gene namesi
Name:tdcDUniRule annotation
Synonyms:yhaA
Ordered Locus Names:b3115, JW5806
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11172. tdcD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 402402Propionate kinasePRO_0000107652Add
BLAST

Proteomic databases

PaxDbiP11868.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
glfP377471EBI-553884,EBI-558730

Protein-protein interaction databases

BioGridi4262417. 12 interactions.
DIPiDIP-10971N.
IntActiP11868. 3 interactions.
MINTiMINT-1273849.
STRINGi511145.b3115.

Structurei

3D structure databases

ProteinModelPortaliP11868.
SMRiP11868. Positions 4-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetokinase family. TdcD subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C6H. Bacteria.
COG0282. LUCA.
HOGENOMiHOG000288399.
InParanoidiP11868.
KOiK00932.
OMAiISIFEIQ.
OrthoDBiEOG69975F.
PhylomeDBiP11868.

Family and domain databases

HAMAPiMF_00020. Acetate_kinase.
MF_01881. Propion_kin_subfam1.
InterProiIPR004372. Ac/propionate_kinase.
IPR000890. Aliphatic_acid_kin_short-chain.
IPR023865. Aliphatic_acid_kinase_CS.
IPR024917. Propionate_kinase.
[Graphical view]
PANTHERiPTHR21060. PTHR21060. 1 hit.
PfamiPF00871. Acetate_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000722. Acetate_prop_kin. 1 hit.
PRINTSiPR00471. ACETATEKNASE.
TIGRFAMsiTIGR00016. ackA. 1 hit.
PROSITEiPS01075. ACETATE_KINASE_1. 1 hit.
PS01076. ACETATE_KINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11868-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEFPVVLVI NCGSSSIKFS VLDASDCEVL MSGIADGINS ENAFLSVNGG
60 70 80 90 100
EPAPLAHHSY EGALKAIAFE LEKRNLNDSV ALIGHRIAHG GSIFTESAII
110 120 130 140 150
TDEVIDNIRR VSPLAPLHNY ANLSGIESAQ QLFPGVTQVA VFDTSFHQTM
160 170 180 190 200
APEAYLYGLP WKYYEELGVR RYGFHGTSHR YVSQRAHSLL NLAEDDSGLV
210 220 230 240 250
VAHLGNGASI CAVRNGQSVD TSMGMTPLEG LMMGTRSGDV DFGAMSWVAS
260 270 280 290 300
QTNQSLGDLE RVVNKESGLL GISGLSSDLR VLEKAWHEGH ERAQLAIKTF
310 320 330 340 350
VHRIARHIAG HAASLRRLDG IIFTGGIGEN SSLIRRLVME HLAVLGLEID
360 370 380 390 400
TEMNNRSNSC GERIVSSENA RVICAVIPTN EEKMIALDAI HLGKVNAPAE

FA
Length:402
Mass (Da):43,384
Last modified:November 1, 1995 - v3
Checksum:i2E49756262C77144
GO

Sequence cautioni

The sequence AAA24663.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAA57919.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA32595.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211A → P in CAA32595 (PubMed:2660107).Curated
Sequence conflicti121 – 1211A → P in AAA24663 (PubMed:3053659).Curated
Sequence conflicti141 – 1411V → L in CAA32595 (PubMed:2660107).Curated
Sequence conflicti141 – 1411V → L in AAA24663 (PubMed:3053659).Curated
Sequence conflicti198 – 1981G → A in CAA32595 (PubMed:2660107).Curated
Sequence conflicti198 – 1981G → A in AAA24663 (PubMed:3053659).Curated
Sequence conflicti244 – 2441A → P in CAA32595 (PubMed:2660107).Curated
Sequence conflicti244 – 2441A → P in AAA24663 (PubMed:3053659).Curated
Sequence conflicti249 – 2502AS → RR in CAA32595 (PubMed:2660107).Curated
Sequence conflicti249 – 2502AS → RR in AAA24663 (PubMed:3053659).Curated
Sequence conflicti275 – 2751L → H in CAA32595 (PubMed:2660107).Curated
Sequence conflicti275 – 2751L → H in AAA24663 (PubMed:3053659).Curated
Sequence conflicti283 – 2831E → G in CAA32595 (PubMed:2660107).Curated
Sequence conflicti283 – 2831E → G in AAA24663 (PubMed:3053659).Curated
Sequence conflicti396 – 4027NAPAEFA → KEGANKRGNSSRLTQSFHFF MFEPIFSPVNALNQPI in BAE77164 (PubMed:16738553).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA57919.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76150.2.
AP009048 Genomic DNA. Translation: BAE77164.1.
X14430 Genomic DNA. Translation: CAA32595.1. Frameshift.
M23638 Genomic DNA. Translation: AAA24663.1. Frameshift.
PIRiH65100. Q3ECTD.
RefSeqiNP_417585.2. NC_000913.3.
WP_001295545.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76150; AAC76150; b3115.
BAE77164; BAE77164; BAE77164.
GeneIDi947635.
KEGGiecj:JW5806.
eco:b3115.
PATRICi32121646. VBIEscCol129921_3209.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA57919.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76150.2.
AP009048 Genomic DNA. Translation: BAE77164.1.
X14430 Genomic DNA. Translation: CAA32595.1. Frameshift.
M23638 Genomic DNA. Translation: AAA24663.1. Frameshift.
PIRiH65100. Q3ECTD.
RefSeqiNP_417585.2. NC_000913.3.
WP_001295545.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP11868.
SMRiP11868. Positions 4-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262417. 12 interactions.
DIPiDIP-10971N.
IntActiP11868. 3 interactions.
MINTiMINT-1273849.
STRINGi511145.b3115.

Proteomic databases

PaxDbiP11868.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76150; AAC76150; b3115.
BAE77164; BAE77164; BAE77164.
GeneIDi947635.
KEGGiecj:JW5806.
eco:b3115.
PATRICi32121646. VBIEscCol129921_3209.

Organism-specific databases

EchoBASEiEB1159.
EcoGeneiEG11172. tdcD.

Phylogenomic databases

eggNOGiENOG4105C6H. Bacteria.
COG0282. LUCA.
HOGENOMiHOG000288399.
InParanoidiP11868.
KOiK00932.
OMAiISIFEIQ.
OrthoDBiEOG69975F.
PhylomeDBiP11868.

Enzyme and pathway databases

UniPathwayiUPA00052; UER00510.
BioCyciEcoCyc:PROPKIN-MONOMER.
ECOL316407:JW5806-MONOMER.
MetaCyc:PROPKIN-MONOMER.

Miscellaneous databases

PROiP11868.

Family and domain databases

HAMAPiMF_00020. Acetate_kinase.
MF_01881. Propion_kin_subfam1.
InterProiIPR004372. Ac/propionate_kinase.
IPR000890. Aliphatic_acid_kin_short-chain.
IPR023865. Aliphatic_acid_kinase_CS.
IPR024917. Propionate_kinase.
[Graphical view]
PANTHERiPTHR21060. PTHR21060. 1 hit.
PfamiPF00871. Acetate_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000722. Acetate_prop_kin. 1 hit.
PRINTSiPR00471. ACETATEKNASE.
TIGRFAMsiTIGR00016. ackA. 1 hit.
PROSITEiPS01075. ACETATE_KINASE_1. 1 hit.
PS01076. ACETATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. "The complete nucleotide sequence of the tdc region of Escherichia coli."
    Schweizer H., Datta P.
    Nucleic Acids Res. 17:3994-3994(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-331.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Molecular characterization of the tdc operon of Escherichia coli K-12."
    Goss T.J., Schweizer H.P., Datta P.
    J. Bacteriol. 170:5352-5359(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-331.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Regulation of the Bacillus subtilis acetate kinase gene by CcpA."
    Grundy F.J., Waters D.A., Allen S.H.G., Henkin T.M.
    J. Bacteriol. 175:7348-7355(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "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: FUNCTION AS A PROPIONATE KINASE AND IN THREONINE CATABOLISM, SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiTDCD_ECOLI
AccessioniPrimary (citable) accession number: P11868
Secondary accession number(s): P76666, Q2M992
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1995
Last modified: January 20, 2016
This is version 143 of the entry and version 3 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.