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Protein

Pyruvate kinase

Gene

pyk

Organism
Bacillus licheniformis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Pathway:iglycolysis

This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Pyruvate kinase (pyk)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321SubstrateBy similarity
Metal bindingi34 – 341PotassiumBy similarity
Metal bindingi36 – 361PotassiumBy similarity
Metal bindingi66 – 661PotassiumBy similarity
Metal bindingi67 – 671Potassium; via carbonyl oxygenBy similarity
Sitei220 – 2201Transition state stabilizerBy similarity
Metal bindingi222 – 2221MagnesiumBy similarity
Binding sitei245 – 2451Substrate; via amide nitrogenBy similarity
Metal bindingi246 – 2461MagnesiumBy similarity
Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity
Binding sitei278 – 2781SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

BRENDAi2.7.1.40. 669.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:pyk
OrganismiBacillus licheniformis
Taxonomic identifieri1402 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Pyruvate kinasePRO_0000112053Add
BLAST

Proteomic databases

PRIDEiP51181.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi279010.BLi03067.

Structurei

3D structure databases

ProteinModelPortaliP51181.
SMRiP51181. Positions 2-585.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated
In the C-terminal section; belongs to the PEP-utilizing enzyme family.Curated

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. 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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52009. SSF52009. 1 hit.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51181-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKTKIVCTI GPASESVEKL TQLMEAGMNV ARLNFSHGDF EEHGARIKNI
60 70 80 90 100
REAAGKLGKD IGILLDTKGP EIRTHTMENG SIELAAGSQL IVSMDEVIGT
110 120 130 140 150
PDKISVTYDG LIHDVSVGST ILLDDGLVGL EVTDINKDKR EIVTKVMNSG
160 170 180 190 200
TLKNKKGVNV PGVSVNLPGI TEKDANDIVF GIEQGVDFIA ASFVRRPSDV
210 220 230 240 250
LEIRELLEEH NAADIQIIPK IENQEGVDNI DAILEVSDGL MVARGDLGVE
260 270 280 290 300
IPAEEVPLVQ KELIKKCNAL GKPVITATQM LDSMQRNPRP TRAEASDVAN
310 320 330 340 350
AIFDGTDAIM LSGETAAGNY PVEAVQTMHN IASRSEEALN HKKILSARSK
360 370 380 390 400
QVSMSITDAI GQSVAHTAIN LDVNAIVTPT ESGHTARMIS KYRPQAPIVA
410 420 430 440 450
VTVNDAVSRK LSLVFGVFAT SGQNHSSTDE MLEKAVQKSL DTGIVRHGDL
460 470 480 490 500
IVITAGAVGE AGTTNLMKVY VVGDVVAKGQ GIGRKSAFGE VVIAQNAQEA
510 520 530 540 550
AKKMKDGAVL VTKSTDRDMM ASLEKAAALI TEEGGLTSHA AVVGLSLGIP
560 570 580
VIVGMENATS ILKEGEDITV DSARGAVYKG RASVL
Length:585
Mass (Da):61,943
Last modified:October 1, 1996 - v1
Checksum:iCC2A5391827D5660
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31955 Genomic DNA. Translation: BAA06727.1.
PIRiJC4220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31955 Genomic DNA. Translation: BAA06727.1.
PIRiJC4220.

3D structure databases

ProteinModelPortaliP51181.
SMRiP51181. Positions 2-585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279010.BLi03067.

Proteomic databases

PRIDEiP51181.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BRENDAi2.7.1.40. 669.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. 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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52009. SSF52009. 1 hit.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiKPYK_BACLI
AccessioniPrimary (citable) accession number: P51181
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.