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InterPro: IPR006657 Molydopterin dinucleotide-binding domain

Protein matches Help

UniProtKB

Matches:

6091 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

IPR006657 MoPterin_dinucl-bd_dom

Secondary

IPR001467

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01568	Molydop_binding	6091
Signatures in BioMart

InterPro Relationships Help

Parent

IPR009010 Aspartate decarboxylase-like fold

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
IPR011887 Trimethylamine-N-oxide reductase TorA
IPR011888 Anaerobic dimethyl sulphoxide reductase, subunit A, DmsA/YnfE
IPR012040 Formylmethanofuran dehydrogenase, subunit D
IPR012048 Formylmethanofuran dehydrogenase, fused subunit C/D
IPR014066 Arsenite oxidase, large subunit
IPR017840 DMSO reductase family, type II, molybdopterin subunit

GO Term annotation Help

Function

GO:0016491 oxidoreductase activity
GO:0030151 molybdenum ion binding

InterPro annotation

Entry Details in BioMart

Abstract

A domain in this entry corresponds to the C-terminal domain IV in dimethyl sulphoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules [1].

Structural links Help

PDB - click here

SCOP: b.52.2.2

CATH: 2.40.40.20

Database links Help

Enzyme: EC:1

PANDIT: PF01568

Blocks: IPB006657

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006657

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A0B6C9 Putative thymidine phosphorylase

O87948 Trimethylamine-N-oxide reductase

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
IPR013102	Pyrimidine nucleoside phosphorylase, C-terminal
IPR017909	Twin arginine translocation signal, Tat
IPR017459	Glycosyl transferase, family 3, N-terminal
IPR006963	Molybdopterin oxidoreductase, Fe4S4 domain
IPR006655	Molybdopterin oxidoreductase, prokaryotic, conserved site
IPR013466	Thymidine phosphorylase related
IPR009010	Aspartate decarboxylase-like fold
IPR000053	Pyrimidine-nucleoside phosphorylase
IPR006657	Molydopterin dinucleotide-binding domain
IPR006656	Molybdopterin oxidoreductase
IPR017713	AMP phosphorylase
IPR017872	Pyrimidine-nucleoside phosphorylase, conserved site
IPR000312	Glycosyl transferase, family 3
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	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 53-69 1996 [PubMed: 8890912] http://dx.doi.org/10.1006/jmbi.1996.0555

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
	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 1998 389-93 [PubMed: 9818358] http://dx.doi.org/10.1007/s002030050658
	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
	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