The domain within your query sequence starts at position 17 and ends at position 187; the E-value for the YjeF_N domain shown below is 5.1e-31.
ERRFLSASEAAALERELLEEYRFGRQQLVELCGHASAVAVTKAFPLPSLSRKQRTVLVVC GPEQNGAVGLACARHLRVFEYQPSIFCPARSADALHRDLTTQCEKMDIPFLSFLPAEVRL IDDAYGLVVDAVLGPGVRLAEAGGHCARALATLKRLSIPLVSLDVPSGWDA
YjeF_N |
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PFAM accession number: | PF03853 |
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Interpro abstract (IPR004443): | In bacteria or archaea, YjeF N-terminal domains occur either as single proteins or fused with other domains and are commonly associated with enzymes. YjeF N-terminal domains are often fused to a YjeF C-terminal domain. It is a bifunctional enzyme that catalyses the epimerisation of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP [ (PUBMED:21994945) ]. Structurally, YjeF N-terminal domains represent a novel version of the Rossmann fold, one of the most common protein folds in nature. The YjeF N-terminal domain is comprised of a three-layer alpha-beta-alpha sandwich with a central beta-sheet surrounded by helices. This domain contains a putative catalytic site [ (PUBMED:15257761) ]. The YjeF N-terminal domain is homologous to AIBP in mammals and YNL200C in budding yeasts. AIBP and YNL200C are NAD(P)H-hydrate epimerases that catalyses the epimerisation of the S- and R-forms of NAD(P)HX, at the expense of ATP, which is converted to ADP [ (PUBMED:21994945) ]. Some proteins known to contain a YjeF N-terminal domain are listed below:
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This is a PFAM domain. For full annotation and more information, please see the PFAM entry YjeF_N