tdcD

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:

L-threonine dehydratase catabolic TdcB (tdcB)
PFL-like enzyme TdcE (tdcE)
no protein annotated in this organism
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 key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	11	MagnesiumUniRule annotation	1
Binding siteⁱ	11	ATPUniRule annotation	1
Binding siteⁱ	18	ATPUniRule annotation	1
Binding siteⁱ	86	SubstrateUniRule annotation	1
Active siteⁱ	143	Proton donor/acceptorUniRule annotation	1
Binding siteⁱ	175	ATPUniRule annotation	1
Siteⁱ	175	Transition state stabilizerUniRule annotation	1
Siteⁱ	236	Transition state stabilizerUniRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	203 – 207	ATPUniRule annotation	5
Nucleotide bindingⁱ	278 – 280	ATPUniRule annotation	3
Nucleotide bindingⁱ	326 – 330	ATPUniRule annotation	5

GO - Molecular functionⁱ

acetate kinase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 9484901
ATP binding Source: UniProtKB-KW
metal ion binding Source: UniProtKB-KW
propionate kinase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 9484901

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

anaerobic amino acid catabolic process
Source: EcoCyc
Inferred from direct assayⁱ
- 9484901
L-threonine catabolic process to propionate Source: UniProtKB-UniPathway
threonine catabolic process
Source: EcoCyc
Inferred from direct assayⁱ
- 9484901

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Transferase
Ligand	ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:PROPKIN-MONOMER MetaCyc:PROPKIN-MONOMER
UniPathwayⁱ	UPA00052;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
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11172 tdcD

EcoGeneⁱ

EG11172 tdcD

Subcellular locationⁱ

GO - Cellular componentⁱ

intracellular Source: InterPro

View the complete GO annotation on QuickGO ...

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000107652	1 – 402	Propionate kinaseAdd BLAST		402

Proteomic databases

PaxDbⁱ	P11868
PRIDEⁱ	P11868

Interactionⁱ

Subunit structureⁱ

Homodimer.UniRule annotation

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
glf	P37747	2	EBI-553884,EBI-558730

With

Entry

#Exp.

IntAct

Notes

glf

P37747

2

EBI-553884,EBI-558730

Protein-protein interaction databases

BioGridⁱ	4262417, 22 interactors
Database of interacting proteins More...DIPⁱ	DIP-10971N
IntActⁱ	P11868, 3 interactors
STRINGⁱ	316385.ECDH10B_3289

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P11868
SMRⁱ	P11868
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the acetokinase family. TdcD subfamily.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105C6H Bacteria COG0282 LUCA
HOGENOMⁱ	HOG000288399
InParanoidⁱ	P11868
KEGG Orthology (KO) More...KOⁱ	K00932
PhylomeDBⁱ	P11868

Family and domain databases

HAMAPⁱ	MF_00020 Acetate_kinase, 1 hit MF_01881 Propion_kin_subfam1, 1 hit
InterProⁱ	View protein in InterPro IPR004372 Ac/propionate_kinase IPR000890 Aliphatic_acid_kin_short-chain IPR023865 Aliphatic_acid_kinase_CS IPR024917 Propionate_kinase
PANTHERⁱ	PTHR21060 PTHR21060, 1 hit PTHR21060:SF17 PTHR21060:SF17, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00871 Acetate_kinase, 1 hit
PIRSFⁱ	PIRSF000722 Acetate_prop_kin, 1 hit
PRINTSⁱ	PR00471 ACETATEKNASE
TIGRFAMsⁱ	TIGR00016 ackA, 1 hit
PROSITEⁱ	View protein in PROSITE PS01075 ACETATE_KINASE_1, 1 hit PS01076 ACETATE_KINASE_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P11868-1 [UniParc]FASTA Add 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 differs from that shown. Reason: Frameshift at several positions.Curated

The sequence AAA57919 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

The sequence CAA32595 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	121	A → P in CAA32595 (PubMed:2660107).Curated	1
Sequence conflictⁱ	121	A → P in AAA24663 (PubMed:3053659).Curated	1
Sequence conflictⁱ	141	V → L in CAA32595 (PubMed:2660107).Curated	1
Sequence conflictⁱ	141	V → L in AAA24663 (PubMed:3053659).Curated	1
Sequence conflictⁱ	198	G → A in CAA32595 (PubMed:2660107).Curated	1
Sequence conflictⁱ	198	G → A in AAA24663 (PubMed:3053659).Curated	1
Sequence conflictⁱ	244	A → P in CAA32595 (PubMed:2660107).Curated	1
Sequence conflictⁱ	244	A → P in AAA24663 (PubMed:3053659).Curated	1
Sequence conflictⁱ	249 – 250	AS → RR in CAA32595 (PubMed:2660107).Curated	2
Sequence conflictⁱ	249 – 250	AS → RR in AAA24663 (PubMed:3053659).Curated	2
Sequence conflictⁱ	275	L → H in CAA32595 (PubMed:2660107).Curated	1
Sequence conflictⁱ	275	L → H in AAA24663 (PubMed:3053659).Curated	1
Sequence conflictⁱ	283	E → G in CAA32595 (PubMed:2660107).Curated	1
Sequence conflictⁱ	283	E → G in AAA24663 (PubMed:3053659).Curated	1
Sequence conflictⁱ	396 – 402	NAPAEFA → KEGANKRGNSSRLTQSFHFF MFEPIFSPVNALNQPI in BAE77164 (PubMed:16738553).Curated	7

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.
PIRⁱ	H65100 Q3ECTD
NCBI Reference Sequences More...RefSeqⁱ	NP_417585.2, NC_000913.3 WP_001295545.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76150; AAC76150; b3115 BAE77164; BAE77164; BAE77164
GeneIDⁱ	947635
KEGGⁱ	ecj:JW5806 eco:b3115
PATRICⁱ	fig\|511145.12.peg.3209

Protein	Similar proteins		Species	Score	Length	Source
P11868	Propionate kinase		ECOLX		406	UniRef100_P11868
Propionate kinase		ECO7I		406
Propionate kinase		Escherichia coli H386		406
Propionate kinase		ECOH1		406
Propionate kinase		Escherichia coli 907713		406
+22

Protein	Similar proteins		Species	Score	Length	Source
P11868	Propionate kinase		ECO57		402	UniRef90_P11868
Propionate kinase		ECOL6		402
Propionate kinase		ECOLX		406
Propionate kinase		ECO7I		406
Propionate kinase		Escherichia coli H386		406
+650

Protein	Similar proteins		Species	Score	Length	Source
P11868	Propionate kinase		ECO57		402	UniRef50_P11868
Propionate kinase		ECOL6		402
Propionate kinase		YERE8		406
Propionate kinase		SALTD		402
Propionate kinase	)	SALTY		402
+1112

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.
PIRⁱ	H65100 Q3ECTD
RefSeqⁱ	NP_417585.2, NC_000913.3 WP_001295545.1, NZ_LN832404.1

3D structure databases

ProteinModelPortalⁱ	P11868
SMRⁱ	P11868
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262417, 22 interactors
DIPⁱ	DIP-10971N
IntActⁱ	P11868, 3 interactors
STRINGⁱ	316385.ECDH10B_3289

Proteomic databases

PaxDbⁱ	P11868
PRIDEⁱ	P11868

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76150; AAC76150; b3115 BAE77164; BAE77164; BAE77164
GeneIDⁱ	947635
KEGGⁱ	ecj:JW5806 eco:b3115
PATRICⁱ	fig\|511145.12.peg.3209

Organism-specific databases

EchoBASEⁱ	EB1159
EcoGeneⁱ	EG11172 tdcD

Phylogenomic databases

eggNOGⁱ	ENOG4105C6H Bacteria COG0282 LUCA
HOGENOMⁱ	HOG000288399
InParanoidⁱ	P11868
KOⁱ	K00932
PhylomeDBⁱ	P11868

Enzyme and pathway databases

UniPathwayⁱ	UPA00052;UER00510
BioCycⁱ	EcoCyc:PROPKIN-MONOMER MetaCyc:PROPKIN-MONOMER

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P11868

PROⁱ

PR:P11868

Family and domain databases

HAMAPⁱ	MF_00020 Acetate_kinase, 1 hit MF_01881 Propion_kin_subfam1, 1 hit
InterProⁱ	View protein in InterPro IPR004372 Ac/propionate_kinase IPR000890 Aliphatic_acid_kin_short-chain IPR023865 Aliphatic_acid_kinase_CS IPR024917 Propionate_kinase
PANTHERⁱ	PTHR21060 PTHR21060, 1 hit PTHR21060:SF17 PTHR21060:SF17, 1 hit
Pfamⁱ	View protein in Pfam PF00871 Acetate_kinase, 1 hit
PIRSFⁱ	PIRSF000722 Acetate_prop_kin, 1 hit
PRINTSⁱ	PR00471 ACETATEKNASE
TIGRFAMsⁱ	TIGR00016 ackA, 1 hit
PROSITEⁱ	View protein in PROSITE PS01075 ACETATE_KINASE_1, 1 hit PS01076 ACETATE_KINASE_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TDCD_ECOLI
Accessionⁱ	P11868Primary (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:	November 7, 2018
	This is version 155 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P11868 (TDCD_ECOLI)

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Propionate kinase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-threonine degradation via propanoate pathway

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Pathwayⁱ: L-threonine degradation via propanoate pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ