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InterPro: IPR000510 Nitrogenase/oxidoreductase, component 1

Protein matches Help

UniProtKB

Matches:

2050 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

IPR000510 Nase/OxRdtase_comp1

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00148	Oxidored_nitro	2050
Signatures in BioMart

InterPro Relationships Help

Found in

IPR005969 Light-independent protochlorophyllide reductase, B subunit
IPR005972 Nitrogenase molybdenum-iron protein alpha chain
IPR005973 Nitrogenase MoFe cofactor biosynthesis protein NifE
IPR005974 Nitrogenase alpha chain
IPR005975 Nitrogenase molybdenum-iron cofactor biosynthesis protein
IPR005976 Nitrogenase molybdenum-iron protein beta chain
IPR010142 Nitrogenase vanadium-iron protein, alpha chain
IPR010143 Nitrogenase component 1, alpha chain
IPR010244 Chlorophyllide reductase subunit Z
IPR010245 Chlorophyllide reductase subunit Y
IPR011290 Nitrogenase iron-iron protein, alpha chain
IPR014280 Nitrogenase iron-iron, beta subunit
IPR014281 Nitrogenase vanadium-iron, beta subunit
IPR016209 Protochlorophyllide reductase, ChlB, light independent
IPR017675 Putative methanogenesis marker 13 metalloprotein

Contains

IPR000318 Nitrogenase component 1, conserved site

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

Enzymes belonging to this family include cofactor-requiring nitrogenases and protochlorophyllide reductase. The key enzymatic reactions in nitrogen fixation are catalysed by the nitrogenase complex, which has two components, the iron protein (component 2), and a component (component 1) which is either a molybdenum-iron, vanadium-iron or iron-iron protein. The enzyme (EC:1.18.6.1) forms a hexamer of two alpha, two beta and two delta chains. Protochlorophyllide reductase (EC:1.3.1.33) is involved in the light-dependent accumulation of chlorophyll, probably at the step of reduction of protochlorophyllide to chlorophyllide.

Structural links Help

PDB - click here

SCOP: c.92.2.3

CATH: 1.20.89.10 , 3.40.50.1980

Database links Help

Enzyme: EC:1.18

PANDIT: PF00148

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000510

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2BQ25 Light-independent protochlorophyllide reductase subunit B

O27566 Uncharacterized protein MTH_1522

P00466 Nitrogenase molybdenum-iron protein alpha chain

P28372 Light-independent protochlorophyllide reductase subunit N

P48099 Light-independent protochlorophyllide reductase subunit B

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010143	Nitrogenase component 1, alpha chain
IPR013580	Proto-chlorophyllide reductase 57kDa subunit
IPR000318	Nitrogenase component 1, conserved site
IPR016209	Protochlorophyllide reductase, ChlB, light independent
IPR005970	Light-independent protochlorophyllide reductase, N subunit
IPR005972	Nitrogenase molybdenum-iron protein alpha chain
IPR005969	Light-independent protochlorophyllide reductase, B subunit
IPR000510	Nitrogenase/oxidoreductase, component 1
IPR017675	Putative methanogenesis marker 13 metalloprotein
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, Howard JB, Rees DC. Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor. Science 297 2002 1696-700 [PubMed: 12215645] http://dx.doi.org/10.1126/science.1073877
	Mayer SM, Gormal CA, Smith BE, Lawson DM. Crystallographic analysis of the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae identifies citrate as a ligand to the molybdenum of iron molybdenum cofactor (FeMoco). J. Biol. Chem. 277 2002 35263-6 [PubMed: 12133839] http://dx.doi.org/10.1074/jbc.M205888200
	Schmid B, Ribbe MW, Einsle O, Yoshida M, Thomas LM, Dean DR, Rees DC, Burgess BK. Structure of a cofactor-deficient nitrogenase MoFe protein. Science 296 2002 352-6 [PubMed: 11951047] http://dx.doi.org/10.1126/science.1070010
	Schmid B, Einsle O, Chiu HJ, Willing A, Yoshida M, Howard JB, Rees DC. Biochemical and structural characterization of the cross-linked complex of nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure. Biochemistry 41 2002 15557-65 [PubMed: 12501184] http://dx.doi.org/10.1021/bi026642b
	Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC. Nitrogenase complexes: multiple docking sites for a nucleotide switch protein. Science 309 2005 1377-80 [PubMed: 16123301] http://dx.doi.org/10.1126/science.1115653

InterPro 23.1