The domain within your query sequence starts at position 9 and ends at position 327; the E-value for the 2-Hacid_dh domain shown below is 1.4e-28.

VFVTGPLPAEGRAALAQAADCEVEQWNSDDPIPRKDLEQGVVGAHGLLCRLSDRVDKKLL
DAAGANLRVISTLSVGVDHLALDEIKKRGIRVGYTPGVLTDATAELAVSLLLTTCRRLPE
AIEEVKNGGWSSWSPLWMCGYGLSQSTVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPR
PQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPDTMGLCSKDFFQKMKNTAIFINISRGDV
VNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSLL
AANNLLAGLRGEAMPSELK

2-Hacid_dh

2-Hacid_dh
PFAM accession number:PF00389
Interpro abstract (IPR006139):

A number of NAD-dependent 2-hydroxyacid dehydrogenases which seem to be specific for the D-isomer of their substrate have been shown to be functionally and structurally related. The catalytic domain contains a number of conserved charged residues which may play a role in the catalytic mechanism [(PUBMED:9126843)]. The NAD-binding domain is described in IPR006140

GO process:metabolic process (GO:0008152), oxidation-reduction process (GO:0055114)
GO function:NAD binding (GO:0051287), oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry 2-Hacid_dh