O06134 (KPYK_MYCTU) 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
Synonyms:	pykA
Ordered Locus Names:	Rv1617, MT1653
ORF Names:	MTCY01B2.09

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate. Ref.3
Cofactor	Magnesium. Potassium.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer By similarity.
Post-translational modification	Phosphorylated by PknJ. Dephosphorylated by PstP. Ref.3
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
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE
Cellular_component	cytosol Inferred from direct assay PubMed 15525680. Source: MTBBASE plasma membrane Inferred from direct assay PubMed 14532352. Source: MTBBASE
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 – 472	472	Pyruvate kinase		PRO_0000112082
Sites
	Metal binding	35	1	Potassium By similarity
	Metal binding	37	1	Potassium By similarity
	Metal binding	67	1	Potassium By similarity
	Metal binding	220	1	Magnesium By similarity
	Metal binding	244	1	Magnesium By similarity
	Binding site	33	1	Substrate By similarity
	Binding site	243	1	Substrate; via amide nitrogen By similarity
	Binding site	244	1	Substrate; via amide nitrogen By similarity
	Binding site	276	1	Substrate By similarity
	Site	218	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	37	1	Phosphoserine; by PknJ; in vitro Ref.3
Experimental info
	Mutagenesis	37	1	S → A: Partial loss of phosphorylation. Decrease in activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O06134 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 2228960E0A45806B	FASTA	472	50,699
	10 20 30 40 50 60 MTRRGKIVCT LGPATQRDDL VRALVEAGMD VARMNFSHGD YDDHKVAYER VRVASDATGR 70 80 90 100 110 120 AVGVLADLQG PKIRLGRFAS GATHWAEGET VRITVGACEG SHDRVSTTYK RLAQDAVAGD 130 140 150 160 170 180 RVLVDDGKVA LVVDAVEGDD VVCTVVEGGP VSDNKGISLP GMNVTAPALS EKDIEDLTFA 190 200 210 220 230 240 LNLGVDMVAL SFVRSPADVE LVHEVMDRIG RRVPVIAKLE KPEAIDNLEA IVLAFDAVMV 250 260 270 280 290 300 ARGDLGVELP LEEVPLVQKR AIQMARENAK PVIVATQMLD SMIENSRPTR AEASDVANAV 310 320 330 340 350 360 LDGADALMLS GETSVGKYPL AAVRTMSRII CAVEENSTAA PPLTHIPRTK RGVISYAARD 370 380 390 400 410 420 IGERLDAKAL VAFTQSGDTV RRLARLHTPL PLLAFTAWPE VRSQLAMTWG TETFIVPKMQ 430 440 450 460 470 STDGMIRQVD KSLLELARYK RGDLVVIVAG APPGTVGSTN LIHVHRIGED DV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical characterization and identification of novel substrate pyruvate kinase A." Arora G., Sajid A., Gupta M., Bhaduri A., Kumar P., Basu-Modak S., Singh Y. PLoS ONE 5:E10772-E10772(2010) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-37, DEPHOSPHORYLATION, MUTAGENESIS OF SER-37. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842577 Genomic DNA. Translation: CAB08894.1. AE000516 Genomic DNA. Translation: AAK45923.1. AL123456 Genomic DNA. Translation: CCP44381.1.
PIR	G70557.
RefSeq	NP_216133.1. NC_000962.3. NP_336109.1. NC_002755.2. YP_006515006.1. NC_018143.1.
3D structure databases
ProteinModelPortal	O06134.
SMR	O06134. Positions 1-469.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv1617.
Proteomic databases
PRIDE	O06134.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK45923; AAK45923; MT1653.
GeneID	13316395. 885501. 924212.
KEGG	mtc:MT1653. mtu:Rv1617. mtv:RVBD_1617.
PATRIC	18125398. VBIMycTub22151_1814.
Organism-specific databases
TubercuList	Rv1617.
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021558.
KO	K00873.
OMA	SHVPRTK.
ProtClustDB	PRK06247.
Enzyme and pathway databases
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_MYCTU

Accession

Primary (citable) accession number: O06134
Secondary accession number(s): L0T783

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program