Reviewed, UniProtKB/Swiss-Prot Q02499 (KPYK_BACST)

Names and origin

Protein names

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

Gene names

Name:

pyk

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	587 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Potassium.
Enzyme regulation	Regulated by phosphoenolpyruvate substrate and is allosterically activated by ribose-5-phosphate, AMP and other nucleoside monophosphates but not by fructose-1,6-bisphosphate.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the pyruvate kinase family. In the C-terminal section; belongs to the PEP-utilizing enzyme family.
Sequence caution	The sequence CAA40994.1 differs from that shown. Reason: Frameshift at position 486.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Pyruvate
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 587

587

Pyruvate kinase

PRO_0000112055

Sites

Active site

221

1

By similarity

Metal binding

223

1

Magnesium By similarity

Metal binding

244

1

Magnesium By similarity

Metal binding

245

1

Magnesium By similarity

Amino acid modifications

Modified residue

541

1

Phosphohistidine By similarity

Experimental info

Mutagenesis

308

1

D → E: Reduced activity; when associated with Y-416.

Mutagenesis

416

1

W → Y: Increased activity.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

587

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Turn

13 – 15

3

Helix

18 – 27

10

Beta strand

29 – 35

7

Helix

41 – 57

17

Beta strand

63 – 67

5

Beta strand

90 – 96

7

Beta strand

102 – 108

7

Turn

113 – 115

3

Beta strand

121 – 124

4

Turn

125 – 128

4

Beta strand

129 – 137

9

Turn

138 – 141

4

Beta strand

142 – 146

5

Beta strand

158 – 160

3

Helix

173 – 185

13

Beta strand

188 – 194

7

Helix

198 – 210

13

Beta strand

216 – 222

7

Helix

225 – 229

5

Helix

231 – 237

7

Beta strand

238 – 244

7

Helix

245 – 251

7

Helix

254 – 256

3

Helix

257 – 271

15

Beta strand

275 – 282

8

Helix

283 – 286

4

Helix

293 – 305

13

Beta strand

308 – 313

6

Helix

314 – 317

4

Helix

322 – 337

16

Helix

342 – 350

9

Helix

357 – 371

15

Beta strand

375 – 380

6

Beta strand

382 – 384

3

Helix

385 – 392

8

Beta strand

399 – 405

7

Helix

406 – 411

6

Helix

412 – 414

3

Beta strand

418 – 422

5

Helix

429 – 443

15

Beta strand

451 – 456

6

Beta strand

468 – 473

6

Beta strand

477 – 480

4

Beta strand

482 – 486

5

Beta strand

492 – 495

4

Helix

499 – 505

7

Beta strand

511 – 515

5

Helix

519 – 521

3

Helix

522 – 525

4

Beta strand

529 – 535

7

Helix

541 – 549

9

Beta strand

553 – 555

3

Helix

560 – 563

4

Beta strand

569 – 573

5

Turn

574 – 577

4

Beta strand

578 – 582

5

Sequences

	Sequence		Length	Mass (Da)
	Q02499-1 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: 0794BA1A07BE0D5A	FASTA	587	62,318
	10 20 30 40 50 60 MKRKTKIVCT IGPASESVDK LVQLMEAGMN VARLNFSHGD HEEHGRRIAN IREAAKRTGR 70 80 90 100 110 120 TVAILLDTKG PEIRTHNMEN GAIELKEGSK LVISMSEVLG TPEKISVTYP SLIDDVSVGA 130 140 150 160 170 180 KILLDDGLIS LEVNAVDKQA GEIVTTVLNG GVLKNKKGVN VPGVKVNLPG ITEKDRADIL 190 200 210 220 230 240 FGIRQGIDFI AASFVRRASD VLEIRELLEA HDALHIQIIA KIENEEGVAN IDEILEAADG 250 260 270 280 290 300 LMVARGDLGV EIPAEEVPLI QKLLIKKCNM LGKPVITATQ MLDSMQRNPR PTRAEASDVA 310 320 330 340 350 360 NAIFDGTDAV MLSGETAAGQ YPVEAVKTMH QIALRTEQAL EHRDILSQRT KESQTTITDA 370 380 390 400 410 420 IGQSVAHTAL NLDVAAIVTP TVSGKTPQMV AKYRPKAPII AVTSNEAVSR RLALVWGVYT 430 440 450 460 470 480 KEAPHVNTTD EMLDVAVDAA VRSGLVKHGD LVVITAGVPV GETGSTNLMK VHVISDLLAK 490 500 510 520 530 540 GQGIGRKSAF GKAVVAKTAE EARQKMVDGG ILVTVSTDAD MMPAIEKAAA IITEEGGLTS 550 560 570 580 HAAVVGLSLG IPVIVGVENA TTLFKDGQEI TVDGGFGAVY RGHASVL

References

[1]	"Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon." Sakai H., Ohta T. Eur. J. Biochem. 211:851-859(1993) [PubMed: 8436141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 328-346 AND 393-396. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[2]	"Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis." Walker D., Chia W.N., Muirhead H. J. Mol. Biol. 228:265-276(1992) [PubMed: 1447787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-51. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D13095 Genomic DNA. Translation: BAA02406.1.
X57859 Genomic DNA. Translation: CAA40994.1. Frameshift.

PIR

S27330.
S29783.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E28	X-ray	2.40	A	1-587	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

2.7.1.40. 266715.

Family and domain databases

InterPro

IPR008279. PEP_mobile.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
[Graphical view]

Gene3D

G3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit.

PANTHER

PTHR11817. Pyruvate_kinase. 1 hit.

Pfam

PF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]

PRINTS

PR01050. PYRUVTKNASE.

ProDom

PD001009. Pyruvate_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01064. pyruv_kin. 1 hit.

PROSITE

PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

KPYK_BACST

Accession

Primary (citable) accession number: Q02499

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)