S-ribosylhomocysteine lyase
Details
- Name
- S-ribosylhomocysteine lyase
- Synonyms
- 4.4.1.21
- AI-2 synthesis protein
- Autoinducer-2 production protein LuxS
- ytjB
- Gene Name
- luxS
- Organism
- Bacillus subtilis (strain 168)
- Amino acid sequence
>lcl|BSEQ0011058|S-ribosylhomocysteine lyase MPSVESFELDHNAVVAPYVRHCGVHKVGTDGVVNKFDIRFCQPNKQAMKPDTIHTLEHLL AFTIRSHAEKYDHFDIIDISPMGCQTGYYLVVSGEPTSAEIVDLLEDTMKEAVEITEIPA ANEKQCGQAKLHDLEGAKRLMRFWLSQDKEELLKVFG
- Number of residues
- 157
- Molecular Weight
- 17714.11
- Theoretical pI
- 5.25
- GO Classification
- Functionsiron ion binding / S-ribosylhomocysteine lyase activityProcessesquorum sensing
- General Function
- S-ribosylhomocysteine lyase activity
- Specific Function
- Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
- Pfam Domain Function
- LuxS (PF02664)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011059|S-ribosylhomocysteine lyase (luxS) ATGCCTTCAGTAGAAAGTTTTGAGCTTGATCATAATGCGGTTGTTGCTCCATATGTAAGA CATTGCGGCGTGCATAAAGTGGGAACAGACGGCGTTGTAAATAAATTTGACATTCGTTTT TGCCAGCCAAATAAACAGGCGATGAAGCCTGACACCATTCACACACTCGAGCATTTGCTC GCGTTTACGATTCGTTCTCACGCTGAGAAATACGATCATTTTGATATCATTGATATTTCT CCAATGGGCTGCCAGACAGGCTATTATCTAGTTGTGAGCGGAGAGCCGACATCAGCGGAA ATCGTTGATCTGCTTGAAGACACAATGAAGGAAGCGGTAGAGATTACAGAAATACCTGCT GCGAATGAAAAGCAGTGCGGCCAAGCGAAGCTTCATGATCTGGAAGGCGCTAAACGTTTA ATGCGTTTCTGGCTTTCACAGGATAAAGAAGAATTGCTAAAAGTATTTGGCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O34667 UniProtKB Entry Name LUXS_BACSU GenBank Protein ID 2293157 GenBank Gene ID AF008220 - General References
- Lapidus A, Galleron N, Sorokin A, Ehrlich SD: Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region. Microbiology. 1997 Nov;143 ( Pt 11):3431-41. [Article]
- Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, Bertero MG, Bessieres P, Bolotin A, Borchert S, Borriss R, Boursier L, Brans A, Braun M, Brignell SC, Bron S, Brouillet S, Bruschi CV, Caldwell B, Capuano V, Carter NM, Choi SK, Cordani JJ, Connerton IF, Cummings NJ, Daniel RA, Denziot F, Devine KM, Dusterhoft A, Ehrlich SD, Emmerson PT, Entian KD, Errington J, Fabret C, Ferrari E, Foulger D, Fritz C, Fujita M, Fujita Y, Fuma S, Galizzi A, Galleron N, Ghim SY, Glaser P, Goffeau A, Golightly EJ, Grandi G, Guiseppi G, Guy BJ, Haga K, Haiech J, Harwood CR, Henaut A, Hilbert H, Holsappel S, Hosono S, Hullo MF, Itaya M, Jones L, Joris B, Karamata D, Kasahara Y, Klaerr-Blanchard M, Klein C, Kobayashi Y, Koetter P, Koningstein G, Krogh S, Kumano M, Kurita K, Lapidus A, Lardinois S, Lauber J, Lazarevic V, Lee SM, Levine A, Liu H, Masuda S, Mauel C, Medigue C, Medina N, Mellado RP, Mizuno M, Moestl D, Nakai S, Noback M, Noone D, O'Reilly M, Ogawa K, Ogiwara A, Oudega B, Park SH, Parro V, Pohl TM, Portelle D, Porwollik S, Prescott AM, Presecan E, Pujic P, Purnelle B, Rapoport G, Rey M, Reynolds S, Rieger M, Rivolta C, Rocha E, Roche B, Rose M, Sadaie Y, Sato T, Scanlan E, Schleich S, Schroeter R, Scoffone F, Sekiguchi J, Sekowska A, Seror SJ, Serror P, Shin BS, Soldo B, Sorokin A, Tacconi E, Takagi T, Takahashi H, Takemaru K, Takeuchi M, Tamakoshi A, Tanaka T, Terpstra P, Togoni A, Tosato V, Uchiyama S, Vandebol M, Vannier F, Vassarotti A, Viari A, Wambutt R, Wedler H, Weitzenegger T, Winters P, Wipat A, Yamamoto H, Yamane K, Yasumoto K, Yata K, Yoshida K, Yoshikawa HF, Zumstein E, Yoshikawa H, Danchin A: The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 1997 Nov 20;390(6657):249-56. [Article]
- Zhu J, Dizin E, Hu X, Wavreille AS, Park J, Pei D: S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein. Biochemistry. 2003 Apr 29;42(16):4717-26. [Article]
- Ruzheinikov SN, Das SK, Sedelnikova SE, Hartley A, Foster SJ, Horsburgh MJ, Cox AG, McCleod CW, Mekhalfia A, Blackburn GM, Rice DW, Baker PJ: The 1.2 A structure of a novel quorum-sensing protein, Bacillus subtilis LuxS. J Mol Biol. 2001 Oct 12;313(1):111-22. [Article]
- Hilgers MT, Ludwig ML: Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site. Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11169-74. Epub 2001 Sep 11. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02321 5-(3-Amino-4,4-Dihyroxy-Butylsulfanylmethyl)-Tetrahydro-Furan-2,3,4-Triol experimental unknown Details DB03661 L-cysteic acid experimental unknown Details DB04182 (S)-2-Amino-4-[(2s,3r)-2,3,5-Trihydroxy-4-Oxo-Pentyl]Mercapto-Butyric Acid experimental unknown Details DB04422 Homocysteine experimental unknown Details