NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25905 / AMRC-C165 / DSM 1728 / IFO 15155 / JCM 9062;
DOI=10.1038/35035069; PubMed=11029001 [NCBI, ExPASy, EBI, Israel, Japan]
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.";
Nature 407:508-513(2000).

[2]

CHARACTERIZATION.
DOI=10.1016/0378-1097(92)90636-3; PubMed=1426985 [NCBI, ExPASy, EBI, Israel, Japan]
Potter S., Fothergill-Gilmore L.A.;
"Purification and properties of pyruvate kinase from Thermoplasma acidophilum.";
FEMS Microbiol. Lett. 73:235-239(1992).

Comments

CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
COFACTOR: Magnesium.
COFACTOR: Potassium.
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5 .
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the pyruvate kinase family.
CAUTION: PubMed:1426985 has published some partial sequence, these sequences do not originate from T.acidophilum, rather they seem to be contaminated with human samples.

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

AL445065; CAC12025.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_394355.1; -.

3D structure databases

HSSP

P14178; 1E0T. [HSSP ENTRY / PDB]

ModBase

P32044.

Enzyme and pathway databases

BioCyc

TACI273075:TA0896-MON; -.

Ontologies

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).
QuickGo view.

Family and domain databases

InterPro

IPR001697; Pyr_Knase.
IPR015813; Pyrv/PenolPyrv_Kinase_cat.
IPR015794; Pyrv_Knase_a/b.
IPR015793; Pyrv_Knase_brl.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.

PANTHER

PTHR11817; Pyruvate_kinase; 1.

Pfam

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; FALSE_NEG.

Genome annotation databases

1456432; -.

AL139299_GR; Ta0896.

tac:Ta0896; -.

fig|273075.1.peg.877; -.

Phylogenomic databases

HOGENOM

P32044; -.

Genome annotation databases

CMR

P32044; Ta0896.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Glycolysis; Kinase; Magnesium; Metal-binding; Pyruvate; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 544`	`544`	`Pyruvate kinase.`	`PRO_0000112129`
`ACT_SITE`	`202 202`		`By similarity.`
`METAL`	`204 204`		`Magnesium (By similarity).`
`METAL`	`225 225`		`Magnesium (By similarity).`
`METAL`	`226 226`		`Magnesium (By similarity).`

Sequence information

Length: 544 AA [This is the length of the unprocessed precursor]

Molecular weight: 59147 Da [This is the MW of the unprocessed precursor]

CRC64: 7BD8BCAF4706A5B2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTKIVATIG PASSSPEIMK QMIDNGLSLV RINSAHADIK DVSKITQMVR SINRDVGIMI 

        70         80         90        100        110        120 
DLKGPELRTG EFAGGTLKIS SGKDYVMGKD IVLNNMNVLS AVQVGDRILM SDGEVSFEVE 

       130        140        150        160        170        180 
STDPFTIRAL NDGVLRDRSR VNIPGRFIEL GTITDRDRAF IREGIADGVD FFALSFVQKS 

       190        200        210        220        230        240 
ENVDSLRDFV IDSGGDQYII SKIETKSGLD NIEEIVKSSD GIMVARGDLG VELPLKEVVL 

       250        260        270        280        290        300 
AQKHIIKTAH EDGDFTIVAT QVLESMVNNS SPTRAEISDI TNAIIDNADA LMLSEESAIG 

       310        320        330        340        350        360 
KYPVQAVRTL KEVSDYVEDK VSFDSSYYFK GNTIAYSVAR AAKILSDDIK SDGIVALTHT 

       370        380        390        400        410        420 
GSTVRMISSL RPKAMVYAAT VSESLARKLN IYFGVLPLHM EGNAEDLSFS EIMEYIVRSG 

       430        440        450        460        470        480 
RFADGSKLVM TSGDPYFTFG GTNDVKVAVV GKFIGRGYSF GDSLSGTATY GTKGDILMSE 

       490        500        510        520        530        540 
DGRIPGTDFR AFIFTSDIKP SLMSSLKGKT VVTKARLVRQ IKEGERIYID GNTGIILMAS 


PDQK

P32044 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools