ECOLI:KPYK1

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	pykF
Protein Name(s)	Pyruvate kinase I PK-1
External Links
UniProt	P0AD61
EMBL	M24636 U68703 U00096 AP009048
PIR	D64925
RefSeq	NP_416191.1 YP_489938.1
PDB	1E0T 1E0U 1PKY
PDBsum	1E0T 1E0U 1PKY
ProteinModelPortal	P0AD61
SMR	P0AD61
DIP	DIP-36221N
IntAct	P0AD61
STRING	511145.b1676
PhosSite	P0810429
SWISS-2DPAGE	P0AD61
PaxDb	P0AD61
PRIDE	P0AD61
EnsemblBacteria	AAC74746 BAA15445
GeneID	12931281 946179
KEGG	ecj:Y75_p1651 eco:b1676
PATRIC	32118658
EchoBASE	EB0797
EcoGene	EG10804
eggNOG	COG0469
HOGENOM	HOG000021559
InParanoid	P0AD61
KO	K00873
OMA	DRVMKSR
OrthoDB	EOG6GBMB0
PhylomeDB	P0AD61
BioCyc	EcoCyc:PKI-MONOMER ECOL316407:JW1666-MONOMER MetaCyc:PKI-MONOMER
SABIO-RK	P0AD61
UniPathway	UPA00109
EvolutionaryTrace	P0AD61
PRO	PR:P0AD61
Proteomes	UP000000318 UP000000625
Genevestigator	P0AD61
GO	GO:0005829 GO:0016020 GO:0005524 GO:0000287 GO:0030955 GO:0004743 GO:0006096 GO:0009408
Gene3D	2.40.33.10 3.20.20.60 3.40.1380.20
InterPro	IPR001697 IPR015813 IPR011037 IPR015794 IPR018209 IPR015793 IPR015795 IPR015806
PANTHER	PTHR11817
Pfam	PF00224 PF02887
PRINTS	PR01050
SUPFAM	SSF50800 SSF51621 SSF52935
TIGRFAMs	TIGR01064
PROSITE	PS00110

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0016020	membrane	PMID:16858726^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16858726^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006096	glycolytic process	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10803 EcoGene:EG10804 MGI:MGI:97591 PANTHER:PTN000212670 RGD:3336 RGD:3337 SGD:S000000036 UniProtKB:Q2RAK2	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10803 EcoGene:EG10804 PANTHER:PTN000212844 UniProtKB:P9WKE5	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000212670 SGD:S000000036 UniProtKB:P14618	C	Seeded From UniProt	complete
enables	GO:0004743	pyruvate kinase activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10803 EcoGene:EG10804 MGI:MGI:97591 MGI:MGI:97604 PANTHER:PTN000212670 PomBase:SPAC4H3.10c RGD:3336 RGD:3337 SGD:S000000036 SGD:S000005874 TAIR:locus:2033760 TAIR:locus:2084583 TAIR:locus:2176912 UniProtKB:C6KTA4 UniProtKB:P14618 UniProtKB:P30613 UniProtKB:Q2RAK2	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:8591049^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AD61	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AD61	F	Seeded From UniProt	complete
involved_in	GO:0051289	protein homotetramerization	PMID:387087^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AD61	P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:387087^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AD61	F	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:24580753^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004743	pyruvate kinase activity	PMID:4588693^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004743	pyruvate kinase activity	PMID:10751408^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001697 InterPro:IPR015793	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015813	F	Seeded From UniProt	complete
enables	GO:0004743	pyruvate kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001697 InterPro:IPR015793 InterPro:IPR015806 InterPro:IPR018209	F	Seeded From UniProt	complete
involved_in	GO:0006096	glycolytic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001697 InterPro:IPR015793 InterPro:IPR015806 InterPro:IPR018209	P	Seeded From UniProt	complete
enables	GO:0030955	potassium ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001697 InterPro:IPR015793	F	Seeded From UniProt	complete
enables	GO:0004743	pyruvate kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.1.40	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0021	F	Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F	Seeded From UniProt	complete
involved_in	GO:0006096	glycolytic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0324 UniPathway:UPA00109	P	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0021	P	Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Mattevi, A et al. (1995) Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition. Structure 3 729-41 PubMed GONUTS page
↑ ^4.0 ^4.1 Valentini, G et al. (1979) Two forms of pyruvate kinase in Escherichia coli. A comparison of chemical and molecular properties. Biochim. Biophys. Acta 570 248-58 PubMed GONUTS page
↑ Krisko, A et al. (2014) Inferring gene function from evolutionary change in signatures of translation efficiency. Genome Biol. 15 R44 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
↑ Waygood, EB & Sanwal, BD (1974) The control of pyruvate kinases of Escherichia coli. I. Physicochemical and regulatory properties of the enzyme activated by fructose 1,6-diphosphate. J. Biol. Chem. 249 265-74 PubMed GONUTS page
↑ Valentini, G et al. (2000) The allosteric regulation of pyruvate kinase. J. Biol. Chem. 275 18145-52 PubMed GONUTS page

[PMID:16858726-1] 1.0 ^1.1 ^1.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:21873635-2] 2.0 ^2.1 ^2.2 ^2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:8591049-3] Mattevi, A et al. (1995) Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition. Structure 3 729-41 PubMed GONUTS page

[PMID:387087-4] 4.0 ^4.1 Valentini, G et al. (1979) Two forms of pyruvate kinase in Escherichia coli. A comparison of chemical and molecular properties. Biochim. Biophys. Acta 570 248-58 PubMed GONUTS page

[PMID:24580753-5] Krisko, A et al. (2014) Inferring gene function from evolutionary change in signatures of translation efficiency. Genome Biol. 15 R44 PubMed GONUTS page

[PMID:18304323-6] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-7] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:4588693-8] Waygood, EB & Sanwal, BD (1974) The control of pyruvate kinases of Escherichia coli. I. Physicochemical and regulatory properties of the enzyme activated by fructose 1,6-diphosphate. J. Biol. Chem. 249 265-74 PubMed GONUTS page

[PMID:10751408-9] Valentini, G et al. (2000) The allosteric regulation of pyruvate kinase. J. Biol. Chem. 275 18145-52 PubMed GONUTS page

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ECOLI:KPYK1

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