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: IPR006655 Molybdopterin oxidoreductase, prokaryotic, conserved site

Protein matches Help

UniProtKB

Matches:

4679 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

IPR006655 Mopterin_OxRdtase_prok_CS

Secondary

IPR001467

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00490	MOLYBDOPTERIN_PROK_2	2422
PROSITE pattern	PS00551	MOLYBDOPTERIN_PROK_1	2472
PROSITE pattern	PS00932	MOLYBDOPTERIN_PROK_3	1845
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006443 Formate dehydrogenase, alpha subunit, anaerobic
IPR006468 Nitrate reductase, alpha subunit
IPR006478 Formate dehydrogenase, alpha subunit
IPR006656 Molybdopterin oxidoreductase
IPR006658 Molybdopterin guanine dinucleotide-containing S/N-oxide reductase
IPR006963 Molybdopterin oxidoreductase, Fe4S4 domain
IPR010051 Nitrate reductase, large subunit, periplasmic
IPR011887 Trimethylamine-N-oxide reductase TorA
IPR011888 Anaerobic dimethyl sulphoxide reductase, subunit A, DmsA/YnfE

GO Term annotation Help

Function

GO:0009055 electron carrier activity
GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

Members of this family include 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: b.52.2.2 , c.81.1.1

CATH: 2.20.25.90 , 2.40.40.20 , 3.40.50.740

Database links Help

PDBe-motif: PS00490 , PS00551 , PS00932

Enzyme: EC:1.7

PROSITE doc: PDOC00392

Blocks: IPB006655

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006655

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O87948 Trimethylamine-N-oxide reductase

P06131 Formate dehydrogenase subunit alpha

P39458 Nitrate reductase

P73448 Nitrate reductase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006311	Twin-arginine translocation pathway, signal sequence
IPR011887	Trimethylamine-N-oxide reductase TorA
IPR017909	Twin arginine translocation signal, Tat
IPR006478	Formate dehydrogenase, alpha subunit
IPR006655	Molybdopterin oxidoreductase, prokaryotic, conserved site
IPR006963	Molybdopterin oxidoreductase, Fe4S4 domain
IPR009010	Aspartate decarboxylase-like fold
IPR006657	Molydopterin dinucleotide-binding domain
IPR006656	Molybdopterin oxidoreductase
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

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
	Bilous PT, Cole ST, Anderson WF, Weiner JH. Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli. Mol. Microbiol. 2 1988 785-95 [PubMed: 3062312] http://dx.doi.org/10.1111/j.1365-2958.1988.tb00090.x
	Bertero MG, Rothery RA, Boroumand N, Palak M, Blasco F, Ginet N, Weiner JH, Strynadka NC. Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A. J. Biol. Chem. 280 2005 14836-43 [PubMed: 15615728] http://dx.doi.org/10.1074/jbc.M410457200
	Mejean V, Iobbi-Nivol C, Lepelletier M, Giordano G, Chippaux M, Pascal MC. TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon. Mol. Microbiol. 11 1994 1169-79 [PubMed: 8022286] http://dx.doi.org/10.1111/j.1365-2958.1994.tb00393.x
	Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC. Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat. Struct. Biol. 10 2003 681-7 [PubMed: 12910261] http://dx.doi.org/10.1038/nsb969
	Wootton JC, Nicolson RE, Cock JM, Walters DE, Burke JF, Doyle WA, Bray RC. Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains. Biochim. Biophys. Acta 1057 1991 157-85 [PubMed: 2015248] http://dx.doi.org/10.1016/S0005-2728(05)80100-8
	Trieber CA, Rothery RA, Weiner JH. Multiple pathways of electron transfer in dimethyl sulfoxide reductase of Escherichia coli. J. Biol. Chem. 269 1994 7103-9 [PubMed: 8125918] http://intl.jbc.org/cgi/content/abstract/269/10/7103
	Rothery RA, Bertero MG, Cammack R, Palak M, Blasco F, Strynadka NC, Weiner JH. The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state. Biochemistry 43 2004 5324-33 [PubMed: 15122898] http://dx.doi.org/10.1021/bi049938l
	Jormakka M, Richardson D, Byrne B, Iwata S. Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes. Structure 12 2004 95-104 [PubMed: 14725769] http://dx.doi.org/10.1016/j.str.2003.11.020
	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

InterPro 23.1