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InterPro: IPR006656 Molybdopterin oxidoreductase

Protein matches Help

UniProtKB

Matches:

10543 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

IPR006656 Mopterin_OxRdtase

Secondary

IPR001467

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00384	Molybdopterin	10543
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006443 Formate dehydrogenase, alpha subunit, anaerobic
IPR006468 Nitrate reductase, alpha subunit
IPR006478 Formate dehydrogenase, alpha subunit
IPR010046 Oxidoreductase alpha (molybdopterin) subunit
IPR010051 Nitrate reductase, large subunit, periplasmic
IPR010228 NADH:ubiquinone oxidoreductase, subunit G
IPR011887 Trimethylamine-N-oxide reductase TorA
IPR011888 Anaerobic dimethyl sulphoxide reductase, subunit A, DmsA/YnfE
IPR014066 Arsenite oxidase, large subunit
IPR016457 Formylmethanofuran dehydrogenase, subunit B
IPR017840 DMSO reductase family, type II, molybdopterin subunit

Contains

IPR006655 Molybdopterin oxidoreductase, prokaryotic, conserved site

GO Term annotation Help

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

This domain is found in a number of molybdopterin-containing oxidoreductases, tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where a single domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyses the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor [1].

Structural links Help

PDB - click here

SCOP: c.81.1.1

CATH: 3.40.228.10 , 3.40.50.740 , 3.90.55.10

Database links Help

Enzyme: EC:1

PANDIT: PF00384

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006656

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P28331 NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

P73448 Nitrate reductase

Q91VD9 NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

Q94511 NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

Q9FGI6 NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006655	Molybdopterin oxidoreductase, prokaryotic, conserved site
IPR006963	Molybdopterin oxidoreductase, Fe4S4 domain
IPR000283	NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site
IPR009010	Aspartate decarboxylase-like fold
IPR019574	NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding
IPR006657	Molydopterin dinucleotide-binding domain
IPR001041	Ferredoxin
IPR006656	Molybdopterin oxidoreductase
IPR015405	NADH-quinone oxidoreductase, chain G, C-terminal
IPR010228	NADH:ubiquinone oxidoreductase, subunit G
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Hochheimer A, Hedderich R, Thauer RK. The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme. Arch. Microbiol. 170 389-93 1998 [PubMed: 9818358] http://dx.doi.org/10.1007/s002030050658

Additional Reading Open in usermanual
	Gonzalez PJ, Rivas MG, Brondino CD, Bursakov SA, Moura I, Moura JJ. EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774. J. Biol. Inorg. Chem. 11 2006 609-16 [PubMed: 16791644] http://dx.doi.org/10.1007/s00775-006-0110-0
	Najmudin S, Gonzalez PJ, Trincao J, Coelho C, Mukhopadhyay A, Cerqueira NM, Romao CC, Moura I, Moura JJ, Brondino CD, Romao MJ. Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum. J. Biol. Inorg. Chem. 13 2008 737-53 [PubMed: 18327621] http://dx.doi.org/10.1007/s00775-008-0359-6
	Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein J. Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution. J. Mol. Biol. 263 1996 53-69 [PubMed: 8890912] http://dx.doi.org/10.1006/jmbi.1996.0555
	Jepson BJ, Mohan S, Clarke TA, Gates AJ, Cole JA, Butler CS, Butt JN, Hemmings AM, Richardson DJ. Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli. J. Biol. Chem. 282 2007 6425-37 [PubMed: 17130127] http://dx.doi.org/10.1074/jbc.M607353200
	Raaijmakers HC, Romao MJ. Formate-reduced E. coli formate dehydrogenase H: The reinterpretation of the crystal structure suggests a new reaction mechanism. J. Biol. Inorg. Chem. 11 2006 849-54 [PubMed: 16830149] http://dx.doi.org/10.1007/s00775-006-0129-2
	Sazanov LA, Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311 2006 1430-6 [PubMed: 16469879] http://dx.doi.org/10.1126/science.1123809

InterPro 23.1