pyk

pyk
168

pyruvate kinase, glycolytic enzyme, involved in control of DNA replication

Locus
BSU_29180
Molecular weight
62.00 kDa
Isoelectric point
4.88
Protein length
585 aaSequenceBlast
Gene length
1758 bpSequenceBlast
Function
catabolic enzyme in glycolysis, control of DNA replication
Product
pyruvate kinase
Essential
no
E.C.
2.7.1.40
Synonyms
pyk, pykA
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG3848 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
2,984,788 → 2,986,545
Phenotypes of a mutant
unable to grow with non-PtsI carbohydrates (such as glucitol or  glycerol) as single carbon source
suppression of ''ftsZ''(ts) mutation (reverted by addition of pyruvate) PubMed
the mutant cells are thinner and shorter than wild type cells PubMed
a ndk pyk double mutant is unable to grow on minimal medium with glucose due to lack of NTP production PubMed
inactivation of pyk can overcome the toxicity of guanosine to a rel sasA sasB triple mutant PubMed
The protein
Catalyzed reaction/ biological activity
ADP + PEP → ATP + pyruvate PubMed
GDP + PEP → GTP + pyruvate PubMed
UDP + PEP → UTP + pyruvate PubMed
CDP + PEP → CTP + pyruvate PubMed
The reaction is irreversible under physiological conditions
Protein family
C-terminal part: PEP-utilizing enzyme family (according to UniProt)
pyruvate kinase family (single member, according to UniProt)
Domains
extra C-terminal domain (ECTD): aa 475 - 585 PubMed
Cofactors
Mg2+, K+
Structure
2E28 (PDB) (Geobacillus stearothermophilus) PubMed
P80885 (AlphaFold)
Modification
phosphorylation on Ser36 PubMed, PubMed, phosphorylation on Ser536 or Ser546 PubMed, please note that the Ser is not on position 536 but rather at 538
Effectors of protein activity
activated by PEP (Hill Coefficient 1,8) PubMed PubMed
allosterically activated by AMP, this requires the extra C-terminal domain PubMed
activation by r5p and ADP, this requires the extra C-terminal domain PubMed
inhibition by ADP and fructose-1,6-bisphosphate in high concentrations; and ATP, this requires the extra C-terminal domain PubMed
Localization
cytoplasm PubMed
Additional information
the enzyme is a tetramer with four active sites PubMed
belongs to the 100 most abundant proteins PubMed
the enzyme is inhibited under gluconeogenetic conditions PubMed
Expression and Regulation
Operons
Genes
pfkA-pyk-ytzA
Description
PubMed
Regulation
twofold induced by glucose PubMed
Open in new tab

pfkA→ytzA

2025-03-27 23:21:38

ghost

156

3e720e37e7e06a91981319daa83ab3e348821a29

ACACB4724EE381AF70927026EEFB4585C5430E1B

Biological materials
Mutant
GP589 (pyk::cat), available in Jörg Stülke's lab, PubMed
GP600 (pyk::erm), available in Jörg Stülke's lab, PubMed
GP1745: BSB1 pyk::aphA3, available in Jörg Stülke' lab
BKE29180 (Δpyk::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATTTGGTTCACTTCCTTCT,  downstream forward: _UP4_TAATTACAGGTGAAAATGGA
BKK29180 (Δpyk::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATTTGGTTCACTTCCTTCT,  downstream forward: _UP4_TAATTACAGGTGAAAATGGA
Expression vectors
expression in E. coli, N-terminal His-tag: pGP1100 (in pWH844), available in Jörg Stülke's lab, PubMed
expression in B. subtilis, native protein: pGP1411 (in pBQ200), available in Jörg Stülke's lab
expression in B. subtilis, N-terminal Strep-tag: pGP1409 (in pGP380), available in Jörg Stülke's lab
expression in B. subtilis, C-terminal Strep-tag: pGP1410 (in pGP382), available in Jörg Stülke's lab
Two-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab, PubMed
LacZ fusion
see ''pfkA
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany Homepage
References
Loading

F76A03A71DADC32C7166E37B994EFED019FDF8A4

Page visits: 17787

Time of last update: 2025-04-01 07:48:57

Author of last update: Jstuelk