EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR005000 HpcH/HpaI aldolase

Protein matches Help

UniProtKB

Matches:

2371 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR005000 HpcH_HpaI

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF03328	HpcH_HpaI	2371
Signatures in BioMart

InterPro Relationships Help

Children

IPR011206 Citrate lyase, beta subunit
IPR012689 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase
IPR017648 2-dehydro-3-deoxyglucarate aldolase GarL

Contains

IPR015813 Pyruvate/Phosphoenolpyruvate kinase, catalytic core

GO Term annotation Help

Process

GO:0006725 cellular aromatic compound metabolic process

Function

GO:0016830 carbon-carbon lyase activity

InterPro annotation

Entry Details in BioMart

Abstract

This family includes 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase (EC:4.1.2) and 4-hydroxy-2-oxovalerate aldolase (EC:4.1.2).

Structural links Help

PDB - click here

SCOP: c.1.12.5

CATH: 3.20.20.60

Database links Help

PANDIT: PF03328

Blocks: IPB005000

Pfam Clan: CL0151.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005000

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O06162 Citrate lyase subunit beta-like protein

Q5I0K3 Citrate lyase subunit beta-like protein, mitochondrial

Q8N0X4 Citrate lyase subunit beta-like protein, mitochondrial

Q8R4N0 Citrate lyase subunit beta-like protein, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005000	HpcH/HpaI aldolase
IPR015813	Pyruvate/Phosphoenolpyruvate kinase, catalytic core
IPR011206	Citrate lyase, beta subunit
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Goulding CW, Bowers PM, Segelke B, Lekin T, Kim CY, Terwilliger TC, Eisenberg D. The structure and computational analysis of Mycobacterium tuberculosis protein CitE suggest a novel enzymatic function. J. Mol. Biol. 365 2007 275-83 [PubMed: 17064730] http://dx.doi.org/10.1016/j.jmb.2006.09.086
	Stringfellow JM, Turpin B, Cooper RA. Sequence of the Escherichia coli C homoprotocatechuic acid degradative operon completed with that of the 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase-encoding gene (hpcH). Gene 166 1995 73-6 [PubMed: 8529896] http://dx.doi.org/10.1016/0378-1119(95)00596-8
	Masai E, Sugiyama K, Iwashita N, Shimizu S, Hauschild JE, Hatta T, Kimbara K, Yano K, Fukuda M. The bphDEF meta-cleavage pathway genes involved in biphenyl/polychlorinated biphenyl degradation are located on a linear plasmid and separated from the initial bphACB genes in Rhodococcus sp. strain RHA1. Gene 187 1997 141-9 [PubMed: 9073078] http://dx.doi.org/10.1016/S0378-1119(96)00748-2
	Ose T, Watanabe K, Mie T, Honma M, Watanabe H, Yao M, Oikawa H, Tanaka I. Insight into a natural Diels-Alder reaction from the structure of macrophomate synthase. Nature 422 2003 185-9 [PubMed: 12634789] http://dx.doi.org/10.1038/nature01454
	Izard T, Blackwell NC. Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism. EMBO J. 19 2000 3849-56 [PubMed: 10921867] http://dx.doi.org/10.1093/emboj/19.15.3849

InterPro 23.1