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Phosphoenolpyruvate carboxylase (EC 4.1.1.31) (PEPcase) catalyzes the irreversible β-carboxylation of phosphoenolpyruvate by bicarbonate to yield oxaloacetate and phosphate. The enzyme is found in all plants and in a variety of microorganisms. A histidine [1] and a lysine [2] have been implicated in the catalytic mechanism of this enzyme; the regions around these active site residues are highly conserved in PEPcase from various plants, bacteria and cyanobacteria and can be used as a signature patterns for this type of enzyme.

December 2004 / Patterns and text revised.

PROSITE methods (with tools and information) covered by this documentation:

PEPCASE_1, PS00781; Phosphoenolpyruvate carboxylase active site 1  (PATTERN)

Consensus pattern: [VTI]-x-T-A-H-P-T-[EQ]-x(2)-R-[KRHAQ] H is an active site residue Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00781 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00781 • Scan Swiss-Prot/TrEMBL entries against PS00781 • view ligand binding statistics

Matching PDB structures: 1FIY 1JQN 1JQO 1QB4 ... [ALL]

PEPCASE_2, PS00393; Phosphoenolpyruvate carboxylase active site 2  (PATTERN)

Consensus pattern: [IVLC]-M-[LIVM]-G-Y-S-D-S-x-K-[DF]-[STAG]-G K is an active site residue Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00393 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00393 • Scan Swiss-Prot/TrEMBL entries against PS00393 • view ligand binding statistics

Matching PDB structures: 1FIY 1JQN 1JQO 1QB4 ... [ALL]

1	Authors	Terada K., Izui K.
	Title	Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction.
	Source	Eur. J. Biochem. 202:797-803(1991).
	PubMed ID	1765093

2	Authors	Jiao J.-A., Podesta F.E., Chollet R., O'Leary M.H., Andreo C.S.
	Title	Isolation and sequence of an active-site peptide from maize leaf phosphoenolpyruvate carboxylase inactivated by pyridoxal 5'-phosphate.
	Source	Biochim. Biophys. Acta 1041:291-295(1990).
	PubMed ID	2268676

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