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InterPro: IPR002880 Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal

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UniProtKB

Matches:

2154 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

IPR002880 Pyrv_Fd/Flavodoxin_OxRdtase_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01855	POR_N	2154
Signatures in BioMart

InterPro Relationships Help

Found in

IPR011895 Pyruvate-flavodoxin oxidoreductase
IPR017721 Indolepyruvate ferredoxin oxidoreductase, alpha subunit

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

This family includes the N-terminal region of the pyruvate ferredoxin oxidoreductase, corresponding to the first two structural domains. This region is involved in inter subunit contacts [1]. Pyruvate oxidoreductase (POR) catalyses the final step in the fermentation of carbohydrates in anaerobic microorganisms [2]. 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 [2]. 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 [3].

Structural links Help

PDB - click here

SCOP: c.36.1.8

CATH: 3.40.50.970

Database links Help

Enzyme: EC:1.2.7

PANDIT: PF01855

Blocks: IPB002880

Pfam Clan: CL0254.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002880

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O05651 Pyruvate synthase subunit porA

O07835 Indolepyruvate oxidoreductase subunit iorA

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
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
IPR015941	Transketolase-like, C-terminal
IPR011895	Pyruvate-flavodoxin oxidoreductase
IPR017721	Indolepyruvate ferredoxin oxidoreductase, alpha subunit
	ModBase
	SWISS-MODEL

Publications Open in usermanual
1.	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. 6 182-90 1999 [PubMed: 10048931] http://dx.doi.org/10.1038/5870
2.	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
3.	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
	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