HMM Summary Page: TIGR02144

Functionlysine biosynthesis enzyme LysX
Gene SymbollysX
Trusted Cutoff275.60
Domain Trusted Cutoff275.60
Noise Cutoff201.55
Domain Noise Cutoff201.55
Isology Typeequivalog
HMM Length281
AuthorSelengut J
Entry DateMar 11 2004 9:35AM
Last ModifiedMar 1 2011 11:50AM
CommentThe family of proteins found in this equivalog include the characterized LysX from Thermus thermophilus [1] which is part of a well-organized lysine biosynthesis gene cluster [2]. LysX is believed to carry out an ATP-dependent acylation of the amino group of alpha-aminoadipate in the prokaryotic version of the fungal AAA lysine biosynthesis pathway. No species having a sequence in this equivalog contains the elements of the more common diaminopimelate lysine biosythesis pathway, and none has been shown to be a lysine auxotroph. These sequences have mainly recieved the name of the related enzyme, "ribosomal protein S6 modification protein RimK". RimK has been characterized in E. coli, and acts by ATP-dependent condensation of S6 with glutamate residues [3].
ReferencesRN [1] RM PMID: 12963379 RT Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8 RA Sakai H, Vassylyeva MN, Matsuura T, Sekine S, Gotoh K, Nishiyama M, Terada T, Shirouzu M, Kuramitsu S, Vassylyev DG, Yokoyama S RL J Mol Biol. 2003 Sep 19;332(3):729-40 RN [2] RM PMID: 10613839 RT A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis RA Nishida H, Nishiyama M, Kobashi N, Kosuge T, Hoshino T, Yamane H RL Genome Res. 1999 Dec;9(12):1175-83 RN [3] RM PMID: 2570347 RT Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12 RA Kang WK, Icho T, Isono S, Kitakawa M, Isono K RL Mol Gen Genet. 1989 Jun;217(2-3):281-8
Genome PropertyGenProp0193: lysine biosynthesis via alpha-aminoadipate (AAA pathway) (HMM)