The domain within your query sequence starts at position 214 and ends at position 309; the E-value for the UDPG_MGDP_dh domain shown below is 1.8e-34.

WSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFG
GSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDY

UDPG_MGDP_dh

 UDPG_MGDP_dh
PFAM accession number:PF00984
Interpro abstract (IPR014026):

The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate [ (PUBMED:2470755) (PUBMED:9013585) ].

The enzymes have a wide range of functions. In plants UDP-glucose dehydrogenase, EC 1.1.1.22 is an important enzyme in the synthesis of hemicellulose and pectin [ (PUBMED:12031484) ], which are the components of newly formed cell walls; while in zebrafish UDP-glucose dehydrogenase is required for cardiac valve formation [ (PUBMED:11533493) ]. In Xanthomonas campestris, a plant pathogen, UDP-glucose dehydrogenase is required for virulence [ (PUBMED:11554764) ].

GDP-mannose dehydrogenase, EC 1.1.1.132 catalyses the formation of GDP-mannuronic acid, which is the monomeric unit from which the exopolysaccharide alginate is formed. Alginate is secreted by a number of bacteria, which include Pseudomonas aeruginosa and Azotobacter vinelandii. In P. aeruginosa, alginate is believed to play an important role in the bacteria's resistance to antibiotics and the host immune response [ (PUBMED:12135385) ], while in A. vinelandii it is essential for the encystment process [ (PUBMED:9864323) ].

This entry represents an alpha helical region that serves as the dimerisation interface for these enzymes [ (PUBMED:10841783) (PUBMED:12705829) ].

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

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