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InterPro: IPR002192 Pyruvate phosphate dikinase, PEP/pyruvate-binding

Protein matchesHelp
UniProtKB
Matches:
2157 proteins
AccessionHelp IPR002192 PPDK_PEP_bd
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR006319 Phosphoenolpyruvate synthase
IPR010121 Pyruvate, phosphate dikinase
Contains IPR013815 ATP-grasp fold, subdomain 1
GO Term annotationHelp
Process GO:0016310 phosphorylation
Function GO:0005524 ATP binding
GO:0016301 kinase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This enzyme catalyses the reversible conversion of ATP to AMP, pyrophosphate and phosphoenolpyruvate (PEP) [1]. Residues at the N terminus correspond to the transit peptide which is indispensable for the transport of the precursor protein into chloroplasts in plants [2]. This domain is present at the N terminus of some PEP-utilizing enzymes.

Structural linksHelp
SCOP: d.142.1.5
Database linksHelp
Enzyme: EC:2.7.9
PANDIT: PF01326
Blocks: IPB002192

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002192 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O23404 Pyruvate, phosphate dikinase 1, chloroplastic

O27190 Probable phosphoenolpyruvate synthase

P22983 Pyruvate, phosphate dikinase

Q2QTC2 Phosphoglucan, water dikinase, chloroplastic

Q55905 Phosphoenolpyruvate synthase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002044 Glycoside hydrolase, carbohydrate-binding
IPR013784 Carbohydrate-binding-like fold
IPR013815 ATP-grasp fold, subdomain 1
IPR013816 ATP-grasp fold, subdomain 2
IPR000121 PEP-utilising enzyme
IPR002192 Pyruvate phosphate dikinase, PEP/pyruvate-binding
IPR013783 Immunoglobulin-like fold
IPR010121 Pyruvate, phosphate dikinase
IPR008279 PEP-utilising enzyme, mobile domain
IPR018274 PEP-utilising enzyme, mobile region, conserved site
IPR006319 Phosphoenolpyruvate synthase
IPR015813 Pyruvate/Phosphoenolpyruvate kinase, catalytic core
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Herzberg O, Chen CC, Kapadia G, McGuire M, Carroll LJ, Noh SJ, Dunaway-Mariano D.
Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites.
Proc. Natl. Acad. Sci. U.S.A. 93 2652-7 1996 [PubMed: 8610096]
http://dx.doi.org/10.1073/pnas.93.7.2652
2. Matsuoka M, Ozeki Y, Yamamoto N, Hirano H, Kano-Murakami Y, Tanaka Y.
Primary structure of maize pyruvate, orthophosphate dikinase as deduced from cDNA sequence.
J. Biol. Chem. 263 11080-3 1988 [PubMed: 2841317]
http://intl.jbc.org/cgi/reprint/263/23/11080.pdf

Additional ReadingHelp
Cosenza LW, Bringaud F, Baltz T, Vellieux FM.
The 3.0 A resolution crystal structure of glycosomal pyruvate phosphate dikinase from Trypanosoma brucei.
J. Mol. Biol. 318 2002 1417-32 [PubMed: 12083528]
http://dx.doi.org/10.1016/S0022-2836(02)00113-4
Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, Ye D, Dunaway-Mariano D.
Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis.
Biochemistry 41 2002 780-7 [PubMed: 11790099]
http://dx.doi.org/10.1021/bi011799+
Lim K, Read RJ, Chen CC, Tempczyk A, Wei M, Ye D, Wu C, Dunaway-Mariano D, Herzberg O.
Swiveling domain mechanism in pyruvate phosphate dikinase.
Biochemistry 46 2007 14845-53 [PubMed: 18052212]
http://dx.doi.org/10.1021/bi701848w
Nakanishi T, Nakatsu T, Matsuoka M, Sakata K, Kato H.
Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion.
Biochemistry 44 2005 1136-44 [PubMed: 15667207]
http://dx.doi.org/10.1021/bi0484522
Nakanishi T, Ohki Y, Oda J, Matsuoka M, Sakata K, Kato H.
Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 193-4 [PubMed: 14684927]
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InterPro 23.1