SMART: Pfam domain Pterin

The domain within your query sequence starts at position 363 and ends at position 601; the E-value for the Pterin_bind domain shown below is 4.6e-63.

GERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDGPSAMTRFCNS
IASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAA
VVVMAFDEEGQATETDVKVNVCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYA
INFIHATRVIKETLPGVRISGGLSNLSFSFRGMEAIREAMHGVFLYHAIKFGMDMGIVN

Pterin_bind

PFAM accession number:	PF00809
Interpro abstract (IPR000489):	The ~250-residue pterin-binding domain has been shown to adopt a (beta/alpha)8 barrel fold, which has the overall shape of a distorted cylinder. It has eight alpha-helices stacked around the outside of an inner cylinder of parallel beta-strands. The pterin ring binds at the bottom of the (beta/alpha;)8 barrel in a polar cup-like region that is relatively solvent exposed and fairly negatively charged. The pterin ring is partially buried within the (beta/alpha)8 barrel. The pterin binding residues are highly conserved and include aspartate and asparagine residues located at the C terminus of the beta-strands of the barrel, which are predicted to form hydrogen bonds with the nitrogen and oxygen atoms of the pterin ring [ (PUBMED:10997901) (PUBMED:9187658) (PUBMED:14752199) ]. Some proteins known to contain a pterin-binding domain are listed below: Prokaryotic and eukaryotic B12-dependent methionine synthase (MetH) ( EC 2.1.1.13 ), a large, modular protein that catalyzes the transfer of a methyl group from methyltetrahydrofolate (CH3-H4folate) to Hcy to form methionine, using cobalamin as an intermediate methyl carrier. Prokaryotic and eukaryotic dihydropteroate synthase (DHPS) ( EC 2.5.1.15 ). It catalyzes the condensation of para-aminobenzoic acid (pABA) with 7,8- dihydropterin-pyrophosphate (DHPPP), eliminating pyrophosphate to form 7,8- dihydropteroate which is subsequently converted to tetrahydrofolate. Moorella thermoacetica 5-methyltetrahydrofolate corrinoid/iron sulphur protein methyltransferase (MeTr). It transfers the N5-methyl group from CH3-H4folate to a cob(I)amide centre in another protein, the corrinoid iron sulphur protein.
GO process:	pteridine-containing compound metabolic process (GO:0042558)

PFAM accession number:

PF00809

Interpro abstract (IPR000489):

The ~250-residue pterin-binding domain has been shown to adopt a (beta/alpha)8 barrel fold, which has the overall shape of a distorted cylinder. It has eight alpha-helices stacked around the outside of an inner cylinder of parallel beta-strands. The pterin ring binds at the bottom of the (beta/alpha;)8 barrel in a polar cup-like region that is relatively solvent exposed and fairly negatively charged. The pterin ring is partially buried within the (beta/alpha)8 barrel. The pterin binding residues are highly conserved and include aspartate and asparagine residues located at the C terminus of the beta-strands of the barrel, which are predicted to form hydrogen bonds with the nitrogen and oxygen atoms of the pterin ring [ (PUBMED:10997901) (PUBMED:9187658) (PUBMED:14752199) ].

Some proteins known to contain a pterin-binding domain are listed below:

Prokaryotic and eukaryotic B12-dependent methionine synthase (MetH) ( EC 2.1.1.13 ), a large, modular protein that catalyzes the transfer of a methyl group from methyltetrahydrofolate (CH3-H4folate) to Hcy to form methionine, using cobalamin as an intermediate methyl carrier.
Prokaryotic and eukaryotic dihydropteroate synthase (DHPS) ( EC 2.5.1.15 ). It catalyzes the condensation of para-aminobenzoic acid (pABA) with 7,8- dihydropterin-pyrophosphate (DHPPP), eliminating pyrophosphate to form 7,8- dihydropteroate which is subsequently converted to tetrahydrofolate.
Moorella thermoacetica 5-methyltetrahydrofolate corrinoid/iron sulphur protein methyltransferase (MeTr). It transfers the N5-methyl group from CH3-H4folate to a cob(I)amide centre in another protein, the corrinoid iron sulphur protein.

GO process:

pteridine-containing compound metabolic process (GO:0042558)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Pterin_bind