The domain within your query sequence starts at position 124 and ends at position 424; the E-value for the Aminotran_MocR domain shown below is 7.6e-9.
AFEMLINPGDTILVNEPLFPGTLYAMKPLGCNIINVPSDEHGIIPEGLKKILSQWKPEDS KDPTKKTPKFLYTVPNGNNPTGNSLTGDRKKEIYELARKYDFLIIEDDPYYFLQFSKPWE PTFLSMDVDGRVIRADTFSKTVSSGLRVGFMTGPKTLIQNIVLHTQVSSVHACTLSQLMI LQLLHQWGEEGFLAHIDRTIDFYKNQRDSILAAADKWLRGLAEWHVPKAGMFLWIKVKGI SDTKQLIEEKAIEREVLLVPGNGFFIDGSAPTSFFRASFSLATPAQMDTAFQRLAQLIKE S
Aminotran_MocR |
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PFAM accession number: | PF12897 |
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Interpro abstract (IPR024551): | Aminotransferases (ATs) are pyridoxal phosphate (PLP)-dependent enzymes that catalyze the reversible transfer of nitrogen from an amino donor to a keto acid amino acceptor. ATs have been classified into five classes by evolutionary relationship. Aspartate aminotransferase (AspAT) belongs to class I ATs. AspAT catalyzes the reaction from L-glutamate and oxaloacetate to L-aspartate and alpha-ketoglutarate [ (PUBMED:8513804) ]. This entry represents a subgroup (Ic) of aspartate aminotransferases (AspATs) from bacteria. They contain an unique auxiliary N-terminal domain absence in humans. Proteins in this entry include aspartate aminotransferase Rv3722c from Mycobacterium tuberculosis [ (PUBMED:32327655) ] and AspT from Corynebacterium glutamicum [ (PUBMED:27355211) ]. |
GO function: | L-aspartate:2-oxoglutarate aminotransferase activity (GO:0004069) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Aminotran_MocR