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P51181 (KPYK_BACLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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:pyk
OrganismBacillus licheniformis
Taxonomic identifier1402 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Sequence similarities

Belongs to the pyruvate kinase family.

In the C-terminal section; belongs to the PEP-utilizing enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585Pyruvate kinase
PRO_0000112053

Sites

Metal binding341Potassium By similarity
Metal binding361Potassium By similarity
Metal binding661Potassium By similarity
Metal binding671Potassium; via carbonyl oxygen By similarity
Metal binding2221Magnesium By similarity
Metal binding2461Magnesium By similarity
Binding site321Substrate 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
P51181 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CC2A5391827D5660

FASTA58561,943
        10         20         30         40         50         60 
MRKTKIVCTI GPASESVEKL TQLMEAGMNV ARLNFSHGDF EEHGARIKNI REAAGKLGKD 

        70         80         90        100        110        120 
IGILLDTKGP EIRTHTMENG SIELAAGSQL IVSMDEVIGT PDKISVTYDG LIHDVSVGST 

       130        140        150        160        170        180 
ILLDDGLVGL EVTDINKDKR EIVTKVMNSG TLKNKKGVNV PGVSVNLPGI TEKDANDIVF 

       190        200        210        220        230        240 
GIEQGVDFIA ASFVRRPSDV LEIRELLEEH NAADIQIIPK IENQEGVDNI DAILEVSDGL 

       250        260        270        280        290        300 
MVARGDLGVE IPAEEVPLVQ KELIKKCNAL GKPVITATQM LDSMQRNPRP TRAEASDVAN 

       310        320        330        340        350        360 
AIFDGTDAIM LSGETAAGNY PVEAVQTMHN IASRSEEALN HKKILSARSK QVSMSITDAI 

       370        380        390        400        410        420 
GQSVAHTAIN LDVNAIVTPT ESGHTARMIS KYRPQAPIVA VTVNDAVSRK LSLVFGVFAT 

       430        440        450        460        470        480 
SGQNHSSTDE MLEKAVQKSL DTGIVRHGDL IVITAGAVGE AGTTNLMKVY VVGDVVAKGQ 

       490        500        510        520        530        540 
GIGRKSAFGE VVIAQNAQEA AKKMKDGAVL VTKSTDRDMM ASLEKAAALI TEEGGLTSHA 

       550        560        570        580 
AVVGLSLGIP VIVGMENATS ILKEGEDITV DSARGAVYKG RASVL 

« Hide

References

[1]"Molecular cloning of the genes for pyruvate kinase of two bacilli, Bacillus psychrophilus and Bacillus licheniformis, and comparison of the properties of the enzymes produced in Escherichia coli."
Tanaka K., Sakai H., Ohta T., Matsuzawa H.
Biosci. Biotechnol. Biochem. 59:1536-1542(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31955 Genomic DNA. Translation: BAA06727.1.
PIRJC4220.

3D structure databases

ProteinModelPortalP51181.
SMRP51181. Positions 2-585.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP51181.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.7.1.40. 669.
UniPathwayUPA00109; UER00188.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProIPR008279. PEP-util_enz_mobile_dom.
IPR001697. 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.
PfamPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52009. SSF52009. 1 hit.
SSF52935. SSF52935. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPYK_BACLI
AccessionPrimary (citable) accession number: P51181
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 81 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