Propionate kinase - Escherichia coli (strain K12)

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P11868 (TDCD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Propionate kinase
EC=2.7.2.15

Gene names

Name:	tdcD
Synonyms:	yhaA
Ordered Locus Names:	b3115, JW5806

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor. Ref.6
Catalytic activity	ATP + propanoate = ADP + propanoyl phosphate. HAMAP-Rule MF_01881
Cofactor	Mg²⁺ By similarity.
Pathway	Amino-acid degradation; L-threonine degradation via propanoate pathway; propanoate from L-threonine: step 4/4. HAMAP-Rule MF_01881
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the acetokinase family. TdcD subfamily.
Sequence caution	The sequence AAA24663.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAA57919.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA32595.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-threonine catabolic process to propionate Inferred from electronic annotation. Source: UniProtKB-UniPathway anaerobic amino acid catabolic process Inferred from direct assay Ref.6. Source: EcoCyc threonine catabolic process Inferred from direct assay Ref.6. Source: EcoCyc
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate kinase activity Inferred from direct assay Ref.6. Source: EcoCyc propionate kinase activity Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
glf	P37747	1	EBI-553884,EBI-558730

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 402

402

Propionate kinase HAMAP-Rule MF_01881

PRO_0000107652

Regions

Nucleotide binding

203 – 207

ATP By similarity

Nucleotide binding

278 – 280

ATP By similarity

Nucleotide binding

326 – 330

ATP By similarity

Sites

Active site

143

Proton donor/acceptor By similarity

Metal binding

Magnesium By similarity

Binding site

ATP By similarity

Binding site

ATP By similarity

Binding site

Substrate By similarity

Binding site

175

ATP By similarity

Site

175

Transition state stabilizer By similarity

Site

236

Transition state stabilizer By similarity

Experimental info

Sequence conflict

121

A → P in CAA32595. Ref.3

Sequence conflict

121

A → P in AAA24663. Ref.4

Sequence conflict

141

V → L in CAA32595. Ref.3

Sequence conflict

141

V → L in AAA24663. Ref.4

Sequence conflict

198

G → A in CAA32595. Ref.3

Sequence conflict

198

G → A in AAA24663. Ref.4

Sequence conflict

244

A → P in CAA32595. Ref.3

Sequence conflict

244

A → P in AAA24663. Ref.4

Sequence conflict

249 – 250

AS → RR in CAA32595. Ref.3

Sequence conflict

249 – 250

AS → RR in AAA24663. Ref.4

Sequence conflict

275

L → H in CAA32595. Ref.3

Sequence conflict

275

L → H in AAA24663. Ref.4

Sequence conflict

283

E → G in CAA32595. Ref.3

Sequence conflict

283

E → G in AAA24663. Ref.4

Sequence conflict

396 – 402

NAPAEFA → KEGANKRGNSSRLTQSFHFF MFEPIFSPVNALNQPI in BAE77164. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P11868 [UniParc].

Last modified November 1, 1995. Version 3.
Checksum: 2E49756262C77144
Show »

FASTA

402

43,384

        10         20         30         40         50         60 
MNEFPVVLVI NCGSSSIKFS VLDASDCEVL MSGIADGINS ENAFLSVNGG EPAPLAHHSY 

        70         80         90        100        110        120 
EGALKAIAFE LEKRNLNDSV ALIGHRIAHG GSIFTESAII TDEVIDNIRR VSPLAPLHNY 

       130        140        150        160        170        180 
ANLSGIESAQ QLFPGVTQVA VFDTSFHQTM APEAYLYGLP WKYYEELGVR RYGFHGTSHR 

       190        200        210        220        230        240 
YVSQRAHSLL NLAEDDSGLV VAHLGNGASI CAVRNGQSVD TSMGMTPLEG LMMGTRSGDV 

       250        260        270        280        290        300 
DFGAMSWVAS QTNQSLGDLE RVVNKESGLL GISGLSSDLR VLEKAWHEGH ERAQLAIKTF 

       310        320        330        340        350        360 
VHRIARHIAG HAASLRRLDG IIFTGGIGEN SSLIRRLVME HLAVLGLEID TEMNNRSNSC 

       370        380        390        400 
GERIVSSENA RVICAVIPTN EEKMIALDAI HLGKVNAPAE FA

« Hide

References

	« Hide 'large scale' referencesShow '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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	Q3ECTD. H65100.
RefSeq	NP_417585.2. NC_000913.2. YP_491305.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P11868.
SMR	P11868. Positions 4-397.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10971N.
IntAct	P11868. 3 interactions.
MINT	MINT-1273849.
STRING	511145.b3115.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76150; AAC76150; b3115. BAE77164; BAE77164; BAE77164.
GeneID	12933423. 947635.
KEGG	ecj:Y75_p3039. eco:b3115.
PATRIC	32121646. VBIEscCol129921_3209.
Organism-specific databases
EchoBASE	EB1159.
EcoGene	EG11172. tdcD.
Phylogenomic databases
eggNOG	COG0282.
HOGENOM	HOG000288399.
KO	K00932.
OMA	HEGHARA.
ProtClustDB	PRK12379.
Enzyme and pathway databases
BioCyc	EcoCyc:PROPKIN-MONOMER. ECOL316407:JW5806-MONOMER. MetaCyc:PROPKIN-MONOMER.
UniPathway	UPA00052; UER00510.
Gene expression databases
Genevestigator	P11868.
Family and domain databases
HAMAP	MF_01881. Propion_kin_subfam1.
InterPro	IPR004372. Ac/Proprionate_kinase. IPR000890. Aliphatic_acid_kin_short-chain. IPR023865. Aliphatic_acid_kinase_CS. IPR024917. Propionate_kinase. [Graphical view]
PANTHER	PTHR21060. PTHR21060. 1 hit. PTHR21060:SF9. PTHR21060:SF9. 1 hit.
Pfam	PF00871. Acetate_kinase. 1 hit. [Graphical view]
PIRSF	PIRSF000722. Acetate_prop_kin. 1 hit.
PRINTS	PR00471. ACETATEKNASE.
TIGRFAMs	TIGR00016. ackA. 1 hit.
PROSITE	PS01075. ACETATE_KINASE_1. 1 hit. PS01076. ACETATE_KINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TDCD_ECOLI

Accession

Primary (citable) accession number: P11868
Secondary accession number(s): P76666, Q2M992

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic 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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents