SMART: MoCF_biosynth domain annotation

MoCF_biosynth Probable molybdopterin binding domain

SMART accession number:	SM00852
Description:	This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Family alignment:	View or

There are 4714 MoCF_biosynth domains in 2278 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with MoCF_biosynth domain is also avaliable.

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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
Cellular role (predicted cellular role)
Cellular role: metabolism
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Sola M, Kneussel M, Heck IS, Betz H, Weissenhorn W
- X-ray crystal structure of the trimeric N-terminal domain of gephyrin.
- J Biol Chem. 2001; 276: 25294-301
- Display abstract
- Gephyrin is a ubiquitously expressed protein that, in the central nervoussystem, forms a submembraneous scaffold for anchoring inhibitoryneurotransmitter receptors in the postsynaptic membrane. The N- andC-terminal domains of gephyrin are homologous to the Escherichia colienzymes MogA and MoeA, respectively, both of which are involved inmolybdenum cofactor biosynthesis. This enzymatic pathway is highlyconserved from bacteria to mammals, as underlined by the ability ofgephyrin to rescue molybdenum cofactor deficiencies in differentorganisms. Here we report the x-ray crystal structure of the N-terminaldomain (amino acids 2-188) of rat gephyrin at 1.9-A resolution.Gephyrin-(2-188) forms trimers in solution, and a sequence motif thoughtto be involved in molybdopterin binding is highly conserved betweengephyrin and the E. coli protein. The atomic structure of gephyrin-(2-188)resembles MogA, albeit with two major differences. The path of theC-terminal ends of gephyrin-(2-188) indicates that the central andC-terminal domains, absent in this structure, should follow a similar3-fold arrangement as the N-terminal region. In addition, a centralbeta-hairpin loop found in MogA is lacking in gephyrin-(2-188). Despitethese differences, both structures show a high degree of surface chargeconservation, which is consistent with their common catalytic function.
Metabolism (metabolic pathways involving proteins which contain this domain)

Structure (3D structures containing this domain)

3D Structures of MoCF_biosynth domains in PDB

PDB code	Main view	Title
1di6		1.45 a crystal structure of the molybdenumm cofactor biosynthesis protein moga from escherichia coli
1di7		1.60 angstrom crystal structure of the molybdenum cofactor biosynthesis protein moga from escherichia coli
1eav		Crystal structures of human gephyrin and plant cnx1 g domains-comparative analysis and functional implications
1fc5		Crystal structure of molybdopterin biosynthesis moea protein
1g8l		Crystal structure of escherichia coli moea
1g8r		Moea
1ihc		X-ray structure of gephyrin n-terminal domain
1jlj		1.6 angstrom crystal structure of the human neuroreceptor anchoring and molybdenum cofactor biosynthesis protein gephyrin
1mkz		Crystal structure of moab protein at 1.6 a resolution.
1o8n		The active site of the molybdenum cofactor biosynthetic protein domain cnx1g
1o8o		The active site of the molybdenum cofactor biosynthetic protein domain cnx1g
1o8q		The active site of the molybdenum cofactor biosenthetic protein domain cnx1g
1r2k		Crystal structure of moab from escherichia coli
1t3e		Structural basis of dynamic glycine receptor clustering
1uux		Structure of a molybdopterin-bound cnx1g domain links molybdenum and copper metabolism
1uuy		Structure of a molybdopterin-bound cnx1g domain links molybdenum and copper metabolism
1uz5		The crystal structure of molybdopterin biosynthesis moea protein from pyrococcus horikosii
1wu2		Crystal structure of molybdopterin biosynthesis moea protein from pyrococcus horikoshii ot3
1xi8		Molybdenum cofactor biosynthesis protein from pyrococcus furiosus pfu-1657500-001
1y5e		Crystal structure of molybdenum cofactor biosynthesis protein b
2f7w		Crystal structure of molybdenum cofactor biosynthesis protein mog from shewanella oneidensis
2f7y		Crystal structure of molybdenum cofactor biosynthesis protein mog from shewanella oneidensis
2fts		Crystal structure of the glycine receptor-gephyrin complex
2fu3		Crystal structure of gephyrin e-domain
2g2c		Putative molybdenum cofactor biosynthesis protein from corynebacterium diphtheriae.
2g4r		Anomalous substructure of moga
2is8		Crystal structure of the molybdopterin biosynthesis enzyme moab (ttha0341) from thermus theromophilus hb8
2nqk		Moea d59n mutant
2nqm		Moea t100a mutant
2nqn		Moea t100w
2nqq		Moea r137q
2nqr		Moea d142n
2nqs		Moea e188a
2nqu		Moea e188q
2nqv		Moea d228a
2nro		Moea k279q
2nrp		Moea r350a
2nrs		Moea s371w
2pbq		Crystal structure of molybdenum cofactor biosynthesis (aq_061) from aquifex aeolicus vf5
2qq1		Crystal structure of molybdenum cofactor biosynthesis (aq_061) other form from aquifex aeolicus vf5
3iwt
3k6a

Links (links to other resources describing this domain)
PFAM MoCF_biosynth