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Q44473 (KPYK2_AGRVI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate kinase

Short name=PK
EC=2.7.1.40
Gene names
Name:ttuE
Encoded onPlasmid pTrAB4
OrganismAgrobacterium vitis (Rhizobium vitis)
Taxonomic identifier373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.

Subunit structure

Homotetramer By similarity.

Induction

By tartrate.

Sequence similarities

Belongs to the pyruvate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Pyruvate
   Molecular functionKinase
Transferase
   Technical termPlasmid
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

potassium ion binding

Inferred from electronic annotation. Source: InterPro

pyruvate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Pyruvate kinase
PRO_0000112052

Sites

Metal binding391Potassium By similarity
Metal binding411Potassium By similarity
Metal binding711Potassium By similarity
Metal binding2221Magnesium By similarity
Metal binding2461Magnesium By similarity
Binding site371Substrate By similarity
Binding site2451Substrate; via amide nitrogen By similarity
Binding site2461Substrate; via amide nitrogen By similarity
Binding site2781Substrate By similarity
Site2201Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q44473 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2D2B614589CB46E7

FASTA48251,678
        10         20         30         40         50         60 
MFIRNNRRSK IVATVGPASS SPDMLRSLFL AGVDTFRLNF SHGARADHAE VYRNIRALEQ 

        70         80         90        100        110        120 
EHDAAIAVLQ DLQGPKIRIG VLAHGRLDLA RGSTIGFILG REGGEGMNDI PLPHREIFEV 

       130        140        150        160        170        180 
AVPGMDLLID DGRIKVRIME VMDGRLVCEV LNGGALSNRK GVNVPGAVLD ISPLTAKDRE 

       190        200        210        220        230        240 
DLEFGLELGV DWVALSFVQR ARDMIEARSL VGDRAGLIAK IEKPSALDDI EDIVRLSDSV 

       250        260        270        280        290        300 
MVARGDLGVE IPPEDVPGKQ KEIIRACRLA AKPVIVATQM LDSMVSSPTP TRAEASDVAG 

       310        320        330        340        350        360 
AIYDGADAVM LSAETATGAY PVEAVEIMNR IIEKTEKHKH YRPILEATEP DVAQSPPHAV 

       370        380        390        400        410        420 
ATAAANVAVA LGSPVVVAYT SSGTTAARIS RARPALPILA LTPSEQVARR LNMFWGVVGV 

       430        440        450        460        470        480 
RSQDVHTYEA SLIHAQQAVQ EAKLASPSDH IVIVAGFPFA QQGSTNNLRV VQIAATDNLE 


IA 

« Hide

References

[1]"Sequence and mutational analysis of a tartrate utilization operon from Agrobacterium vitis."
Crouzet P., Otten L.
J. Bacteriol. 177:6518-6526(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25634 Genomic DNA. Translation: AAA68700.1.

3D structure databases

ProteinModelPortalQ44473.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ44473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00188.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPYK2_AGRVI
AccessionPrimary (citable) accession number: Q44473
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways