The domain within your query sequence starts at position 88 and ends at position 377; the E-value for the MTHFR domain shown below is 2.3e-121.

KMRRRMDSGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLFVDVTWHPAGDPGSDKET
SSMMIASTAVNYCGLETILHMTCCQQRPEEITGHLHRAKQLGLKNIMALRGDPVGDHWEA
EEGGFSYATDLVKHIRTEFADYFDICVAGYPRGHPDAESFEDDLKHLKEKVSAGADFIIT
QLFFEASTFFSFVKACTEIGISCPILPGIFPIQGYTSLRQLVKLSKLEVPQKIKDVIEPI
KDNDAAIRNYGIELAVSLCRELLDSGLVPGLHFYTLNREVATMEVLKQLG

MTHFR

 MTHFR
PFAM accession number:PF02219
Interpro abstract (IPR003171):

This represents the catalytic domain of 5,10-methylenetetrahydrofolate reductase from prokaryotes and methylenetetrahydrofolate reductase (MTHFR) from eukaryotes ( EC 1.5.1.20 ). Both convert 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate.

Mammalian and yeast MTHFRs are homodimers in which each subunit contains an N-terminal catalytic domain, and a C-terminal regulatory domain to which the allosteric inhibitor adenosylmethionine binds [ (PUBMED:19610625) ]. NADPH is the preferred reductant. In humans, there are several clinically significant mutations in MTHFR that result in hyperhomocysteinemia, which is a risk factor for the development of cardiovascular disease [ (PUBMED:10201405) ].

The bacterial enzyme is a homotetramer. MTHFRs of enteric bacteria comprise shorter chains around 300 residues in length. Their sequences can be aligned with the N-terminal catalytic domains of the eukaryotic MTHFRs [ (PUBMED:10201405) ]. Escherichia coli MTHFR, along with plant MTHFRs, prefer NADHs as the source of reducing equivalents [ (PUBMED:19610625) ]. The structure of E. coli MTHFR is known to be a TIM barrel [ (PUBMED:10201405) ].

GO process:oxidation-reduction process (GO:0055114), methionine metabolic process (GO:0006555)
GO function:methylenetetrahydrofolate reductase (NAD(P)H) activity (GO:0004489)

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