P51181 (KPYK_BACLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate kinase
Short name=PK
EC=2.7.1.40

Gene names

Name:

pyk

Organism

Bacillus licheniformis

Taxonomic identifier

1402 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group

Protein attributes

Sequence length	585 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 585	585	Pyruvate kinase		PRO_0000112053
Sites
	Metal binding	34	1	Potassium By similarity
	Metal binding	36	1	Potassium By similarity
	Metal binding	66	1	Potassium By similarity
	Metal binding	67	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	222	1	Magnesium By similarity
	Metal binding	246	1	Magnesium By similarity
	Binding site	32	1	Substrate By similarity
	Binding site	245	1	Substrate; via amide nitrogen By similarity
	Binding site	246	1	Substrate; via amide nitrogen By similarity
	Binding site	278	1	Substrate By similarity
	Site	220	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P51181 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: CC2A5391827D5660	FASTA	585	61,943
	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

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.
PIR	JC4220.
3D structure databases
ProteinModelPortal	P51181.
SMR	P51181. Positions 2-585.
ModBase	Search...
Proteomic databases
PRIDE	P51181.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	2.7.1.40. 669.
UniPathway	UPA00109; UER00188.
Family and domain databases
Gene3D	2.40.33.10. 1 hit. 3.20.20.60. 2 hits. 3.40.1380.20. 1 hit.
InterPro	IPR008279. PEP-util_enz_mobile_dom. IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase. 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]
PANTHER	PTHR11817. PTHR11817. 1 hit.
Pfam	PF00391. PEP-utilizers. 1 hit. PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	SSF52009. PEP_mobile. 1 hit. SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01064. pyruv_kin. 1 hit.
PROSITE	PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYK_BACLI

Accession

Primary (citable) accession number: P51181

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program