HMM Summary Page: TIGR00657

AccessionTIGR00657
Nameasp_kinases
Functionaspartate kinase
Trusted Cutoff208.70
Domain Trusted Cutoff208.70
Noise Cutoff91.15
Domain Noise Cutoff91.15
Isology Typesubfamily_domain
EC Number2.7.2.4
HMM Length442
Mainrole CategoryAmino acid biosynthesis
Subrole CategoryAspartate family
AuthorHaft DH
Entry DateDec 1 1999 10:45AM
Last ModifiedFeb 14 2011 3:27PM
CommentAspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer. The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. This may be a feature of a number of closely related forms, including a paralog from B. subtilis.
ReferencesSE AL A2 hmmalign GA hmmsearch DR EXPERIMENTAL; EGAD|9629|EC4024; monofunctional, Lys-sensitive homodimer DR EXPERIMENTAL; EGAD|9487|EC0002; bifunctional, Thr-sensitive homotetramer DR EXPERIMENTAL; EGAD|21696|EC3940; bifunctional, Met-sensistive homotetramer DR EXPERIMENTAL; EGAD|52194|YER052C; mostly Thr-sensitive DR EXPERIMENTAL; EGAD|75283|81007; bifunctional, chloroplast
Genome PropertyGenProp0160: aspartate semialdehyde biosynthesis from aspartate (HMM)
GenProp0160: aspartate semialdehyde biosynthesis from aspartate (HMM)