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B0S194

- LUXS_FINM2

UniProt

B0S194 - LUXS_FINM2

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Protein

S-ribosylhomocysteine lyase

Gene
luxS, FMG_0716
Organism
Finegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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) By similarity.UniRule annotation

Catalytic activityi

S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione.UniRule annotation

Cofactori

Binds 1 iron ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Iron By similarity
Metal bindingi57 – 571Iron By similarity
Metal bindingi122 – 1221Iron By similarity

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. S-ribosylhomocysteine lyase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. quorum sensing Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Autoinducer synthesis, Quorum sensing

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciFMAG334413:GJ6M-767-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
S-ribosylhomocysteine lyase (EC:4.4.1.21)
Alternative name(s):
AI-2 synthesis protein
Autoinducer-2 production protein LuxS
Gene namesi
Name:luxS
Ordered Locus Names:FMG_0716
OrganismiFinegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus)
Taxonomic identifieri334413 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiales Family XI. Incertae SedisFinegoldia
ProteomesiUP000001319: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156S-ribosylhomocysteine lyaseUniRule annotationPRO_1000093308Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi334413.FMG_0716.

Structurei

3D structure databases

ProteinModelPortaliB0S194.

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
KOiK07173.
OMAiIANDIEW.
OrthoDBiEOG68WRBM.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
PfamiPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFiPIRSF006160. AI2. 1 hit.
PRINTSiPR01487. LUXSPROTEIN.
ProDomiPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63411. SSF63411. 1 hit.

Sequencei

Sequence statusi: Complete.

B0S194-1 [UniParc]FASTAAdd to Basket

« Hide

MNKIESFKIN HLKLMPGIYV SRKDYLGNEV LTTFDLRITA PNREPVMNTA    50
EVHAIEHLGA TFLRNKLENE VIYFGPMGCR TGFYLILVGD KKSEDIVDLI 100
KELFEFISNY EGEIPGQSAK DCGNYSDMNL SMAKFYSNKY LNVINNIKKE 150
NLIYPE 156
Length:156
Mass (Da):17,927
Last modified:April 8, 2008 - v1
Checksum:iBE5D1CA61F0010F9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008971 Genomic DNA. Translation: BAG08134.1.
RefSeqiYP_001692024.1. NC_010376.1.

Genome annotation databases

EnsemblBacteriaiBAG08134; BAG08134; FMG_0716.
GeneIDi6020185.
KEGGifma:FMG_0716.
PATRICi21887109. VBIFinMag33027_0921.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008971 Genomic DNA. Translation: BAG08134.1 .
RefSeqi YP_001692024.1. NC_010376.1.

3D structure databases

ProteinModelPortali B0S194.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 334413.FMG_0716.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAG08134 ; BAG08134 ; FMG_0716 .
GeneIDi 6020185.
KEGGi fma:FMG_0716.
PATRICi 21887109. VBIFinMag33027_0921.

Phylogenomic databases

eggNOGi COG1854.
HOGENOMi HOG000040372.
KOi K07173.
OMAi IANDIEW.
OrthoDBi EOG68WRBM.

Enzyme and pathway databases

BioCyci FMAG334413:GJ6M-767-MONOMER.

Family and domain databases

Gene3Di 3.30.1360.80. 1 hit.
HAMAPi MF_00091. LuxS.
InterProi IPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view ]
Pfami PF02664. LuxS. 1 hit.
[Graphical view ]
PIRSFi PIRSF006160. AI2. 1 hit.
PRINTSi PR01487. LUXSPROTEIN.
ProDomi PD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF63411. SSF63411. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic pathogen."
    Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K., Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.
    DNA Res. 15:39-47(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29328.

Entry informationi

Entry nameiLUXS_FINM2
AccessioniPrimary (citable) accession number: B0S194
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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