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UniProtKB/Swiss-Prot entry Q02499

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KPYK_BACST
Primary accession number Q02499
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on October 1, 1994 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 75)
Name and origin of the protein
Protein name Pyruvate kinase
Synonyms PK
EC 2.7.1.40
Gene name
Name: pyk
From
Bacillus stearothermophilus (Geobacillus stearothermophilus) [TaxID: 1422] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 328-346 AND 393-396.
STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924;
PubMed=8436141 [NCBI, ExPASy, EBI, Israel, Japan]
Sakai H., Ohta T.;
"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.";
Eur. J. Biochem. 211:851-859(1993).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-51.
STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924;
DOI=10.1016/0022-2836(92)90505-E; PubMed=1447787 [NCBI, ExPASy, EBI, Israel, Japan]
Walker D., Chia W.N., Muirhead H.;
"Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis.";
J. Mol. Biol. 228:265-276(1992).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D13095; BAA02406.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X57859; CAA40994.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S27330; S27330.
S29783; S29783.
3D structure databases
PDB
2E28; X-ray; 2.40 A; A=1-587.[ExPASy / RCSB / EBI]
PDBsum 2E28; -.
ModBase Q02499.
Ontologies
GO
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from InterPro).
GO:0030955; Molecular function: potassium ion binding (inferred from electronic annotation from InterPro).
GO:0004743; Molecular function: pyruvate kinase activity (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
GO:0016310; Biological process: phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR008279; PEP_mobile.
IPR001697; Pyr_Knase.
IPR015813; Pyrv/PenolPyrv_Kinase_cat.
IPR015794; Pyrv_Knase_a/b.
IPR015793; Pyrv_Knase_brl.
Graphical view of domain structure.
Gene3D G3DSA:3.50.30.10; PEP_mobile; 1.
G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.
PANTHER PTHR11817; Pyruvate_kinase; 1.
Pfam PF00391; PEP-utilizers; 1.
PF00224; PK; 1.
PF02887; PK_C; 1.
Pfam graphical view of domain structure.
PRINTS PR01050; PYRUVTKNASE.
ProDom PD001009; Pyruvate_kinase; 2.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01064; pyruv_kin; 1.
PROSITE PS00110; PYRUVATE_KINASE; 1.
ProtoNet Q02499.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Allosteric enzyme; Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding; Phosphoprotein; Pyruvate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   587  587     Pyruvate kinase. PRO_0000112055
ACT_SITE   221   221        By similarity. 
METAL   223   223        Magnesium (By similarity). 
METAL   244   244        Magnesium (By similarity). 
METAL   245   245        Magnesium (By similarity). 
MOD_RES   541   541        Phosphohistidine (By similarity). 
MUTAGEN   308   308        D->E: Reduced activity; when associated with Y-416. 
MUTAGEN   416   416        W->Y: Increased activity. 
STRAND   5    10  6      
TURN   13    15  3      
HELIX   18    27  10      
STRAND   29    35  7      
HELIX   41    57  17      
STRAND   63    67  5      
STRAND   90    96  7      
STRAND   102   108  7      
TURN   113   115  3      
STRAND   121   124  4      
TURN   125   128  4      
STRAND   129   137  9      
TURN   138   141  4      
STRAND   142   146  5      
STRAND   158   160  3      
HELIX   173   185  13      
STRAND   188   194  7      
HELIX   198   210  13      
STRAND   216   222  7      
HELIX   225   229  5      
HELIX   231   237  7      
STRAND   238   244  7      
HELIX   245   251  7      
HELIX   254   256  3      
HELIX   257   271  15      
STRAND   275   282  8      
HELIX   283   286  4      
HELIX   293   305  13      
STRAND   308   313  6      
HELIX   314   317  4      
HELIX   322   337  16      
HELIX   342   350  9      
HELIX   357   371  15      
STRAND   375   380  6      
STRAND   382   384  3      
HELIX   385   392  8      
STRAND   399   405  7      
HELIX   406   411  6      
HELIX   412   414  3      
STRAND   418   422  5      
HELIX   429   443  15      
STRAND   451   456  6      
STRAND   468   473  6      
STRAND   477   480  4      
STRAND   482   486  5      
STRAND   492   495  4      
HELIX   499   505  7      
STRAND   511   515  5      
HELIX   519   521  3      
HELIX   522   525  4      
STRAND   529   535  7      
HELIX   541   549  9      
STRAND   553   555  3      
HELIX   560   563  4      
STRAND   569   573  5      
TURN   574   577  4      
STRAND   578   582  5      
Sequence information
Length: 587 AA [This is the length of the unprocessed precursor] Molecular weight: 62318 Da [This is the MW of the unprocessed precursor] CRC64: 0794BA1A07BE0D5A [This is a checksum on the sequence] 
        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
Q02499 in FASTA format

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