O51323 (KPYK_BORBU) 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
Ordered Locus Names:	BB_0348

Organism

Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) [Reference proteome] [HAMAP]

Taxonomic identifier

224326 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group › Borrelia burgdorferi

Protein attributes

Sequence length	477 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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
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 – 477	477	Pyruvate kinase		PRO_0000112057
Sites
	Metal binding	36	1	Potassium By similarity
	Metal binding	64	1	Potassium By similarity
	Metal binding	65	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	216	1	Magnesium By similarity
	Metal binding	240	1	Magnesium By similarity
	Binding site	34	1	Substrate By similarity
	Binding site	239	1	Substrate; via amide nitrogen By similarity
	Binding site	240	1	Substrate; via amide nitrogen By similarity
	Binding site	272	1	Substrate By similarity
	Site	214	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	O51323 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 40D3CCAC9ACB7D98	FASTA	477	53,032
	10 20 30 40 50 60 MISKLTKIVA TISDLRCEPE HIKDLHDAGV NVIRLNTAHQ SHEDTIKVID NVRKISNKIA 70 80 90 100 110 120 LMIDTKGPEV RTANIENPII VKTGDKVIIS TSPINEPNNF QTNYDGFVKE VPQGSKVLID 130 140 150 160 170 180 DGELEMTVVA KLPDRLICEI KNDGQIKNKK SINTPGISLK LQSVTEKDKG FIELAAKYNV 190 200 210 220 230 240 DFIAHSFVRH SKDVQDVQEI LTASGNPDVK IISKIENQEG IDNIEEIAKA SYGIMVARGD 250 260 270 280 290 300 MGVEIPAEDV PIAQLKITQT CIKYGIPVIT ATQMLHTMIE NPRPTRAEVS DIANAILNGT 310 320 330 340 350 360 DAIMLSGETA YGKYPIEAVK MMTSIAKKVE KHRKMTLYKD ELFYDKSITR NYIIKCAIDA 370 380 390 400 410 420 TKLMDIKAII VDSLKGKTAR IMATYRASVP LFITTNSERL ARELALSYGV YSNLVDNNFK 430 440 450 460 470 RTTEFVVTSL KMLKEQGVVN DKDTVIIISG NPNRNIEKGT EFMEINTVED AIKGRNI

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000783 Genomic DNA. Translation: AAC66733.1.
PIR	C70143.
RefSeq	NP_212482.1. NC_001318.1.
3D structure databases
ProteinModelPortal	O51323.
ModBase	Search...
Protein-protein interaction databases
STRING	224326.BB0348.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC66733; AAC66733; BB_0348.
GeneID	1195185.
KEGG	bbu:BB_0348.
PATRIC	20557308. VBIBorBur75917_0744.
Phylogenomic databases
eggNOG	COG0469.
KO	K00873.
OMA	TDVYFAV.
ProtClustDB	PRK05826.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0348-MONOMER.
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	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	PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	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_BORBU

Accession

Primary (citable) accession number: O51323

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program