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InterPro: IPR019752 Pyruvate/ketoisovalerate oxidoreductase

Protein matches Help

UniProtKB

Matches:

2337 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

IPR019752 Pyrv/ketoisovalerate_OxRed

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.920.10	Pyrv_Fd/Flavodoxin_OxRdtase	2031
Pfam	PF01558	POR	2301
Signatures in BioMart

InterPro Relationships Help

Parent

IPR002869 Pyruvate-flavodoxin oxidoreductase, central domain

Children

IPR011894 2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate
IPR017719 Indolepyruvate ferredoxin oxidoreductase, beta subunit

Found in

IPR011895 Pyruvate-flavodoxin oxidoreductase

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016903 oxidoreductase activity, acting on the aldehyde or oxo group of donors

InterPro annotation

Entry Details in BioMart

Abstract

This domain is found in prokaryotes. It includes a region of the large protein pyruvate-flavodoxin oxidoreductase and the whole pyruvate ferredoxin oxidoreductase gamma subunit protein. It is not known whether the gamma subunit has a catalytic or regulatory role. Pyruvate oxidoreductase (POR) catalyses the final step in the fermentation of carbohydrates in anaerobic microorganisms [1]. This involves the oxidative decarboxylation of pyruvate with the participation of thiamine followed by the transfer of an acetyl moiety to coenzyme A for the synthesis of acetyl-CoA [1]. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited [2].

Structural links Help

PDB - click here

SCOP: c.64.1.1

CATH: 3.40.920.10

Database links Help

Enzyme: EC:1.2.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR019752

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O05650 Pyruvate synthase subunit porC

O07836 Indolepyruvate oxidoreductase subunit iorB

P52965 Putative pyruvate-flavodoxin oxidoreductase

Q06879 Pyruvate-flavodoxin oxidoreductase

Q94IN5 Pyruvate dehydrogenase [NADP+], mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003097	FAD-binding, type 1
IPR017719	Indolepyruvate ferredoxin oxidoreductase, beta subunit
IPR017896	4Fe-4S ferredoxin, iron-sulpur binding domain
IPR019456	Pyruvate-flavodoxin oxidoreductase, EKR domain
IPR001094	Flavodoxin-like
IPR001450	4Fe-4S ferredoxin, iron-sulphur binding, subgroup
IPR001433	Oxidoreductase FAD/NAD(P)-binding
IPR017927	Ferredoxin reductase-type FAD-binding domain
IPR002880	Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal
IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
IPR019752	Pyruvate/ketoisovalerate oxidoreductase
IPR011766	Thiamine pyrophosphate enzyme, C-terminal TPP-binding
IPR015702	NADPH Cytochrome P450 Reductase
IPR017938	Riboflavin synthase-like beta-barrel
IPR008254	Flavodoxin/nitric oxide synthase
IPR017900	4Fe-4S ferredoxin, iron-sulphur binding, conserved site
IPR009014	Transketolase, C-terminal/Pyruvate-ferredoxin oxidoreductase, domain II
IPR002869	Pyruvate-flavodoxin oxidoreductase, central domain
IPR011894	2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate
IPR011895	Pyruvate-flavodoxin oxidoreductase
IPR015941	Transketolase-like, C-terminal
	PDB Chain
	ModBase
	SWISS-MODEL

Publications Open in usermanual
1.	Kletzin A, Adams MW. Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima. J. Bacteriol. 178 248-57 1996 [PubMed: 8550425] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8550425&action=stream&blobtype=pdf
2.	Bauer CC, Scappino L, Haselkorn R. Growth of the cyanobacterium Anabaena on molecular nitrogen: NifJ is required when iron is limited. Proc. Natl. Acad. Sci. U.S.A. 90 8812-6 1993 [PubMed: 8415612] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8415612

Additional Reading Open in usermanual
	Chabriere E, Vernede X, Guigliarelli B, Charon MH, Hatchikian EC, Fontecilla-Camps JC. Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase. Science 294 2001 2559-63 [PubMed: 11752578] http://dx.doi.org/10.1126/science.1066198
	Chabriere E, Charon MH, Volbeda A, Pieulle L, Hatchikian EC, Fontecilla-Camps JC. Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate. Nat. Struct. Biol. 6 1999 182-90 [PubMed: 10048931] http://dx.doi.org/10.1038/5870
	Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC. Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate. Structure 14 2006 217-24 [PubMed: 16472741] http://dx.doi.org/10.1016/j.str.2005.10.013

InterPro 23.1