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Conserved domains on  [gi|446086566|ref|WP_000164421|]
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MULTISPECIES: S-ribosylhomocysteine lyase [Staphylococcus]

Protein Classification

S-ribosylhomocysteine lyase( domain architecture ID 10004804)

S-ribosylhomocysteine lyase catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD), which spontaneously cyclizes and combines with borate to form autoinducer (AI-2)

CATH:  3.30.1360.80
EC:  4.4.1.21
Gene Ontology:  GO:0005506|GO:0009372|GO:0043768
SCOP:  4003557

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LuxS COG1854
S-ribosylhomocysteine lyase LuxS, autoinducer biosynthesis [Signal transduction mechanisms];
3-150 5.54e-97

S-ribosylhomocysteine lyase LuxS, autoinducer biosynthesis [Signal transduction mechanisms];


:

Pssm-ID: 441459  Cd Length: 149  Bit Score: 275.87  E-value: 5.54e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086566   3 KMNVESFNLDHTKVVAPFIRLAGTMEGLNGDVIHKYDIRFKQPNKEHMDMPGLHSLEHLMAENIRNHSDKVVDLSPMGCQ 82
Cdd:COG1854    1 MPKVESFTLDHTKVKAPYVRVAGVDKGPGGDVITKFDLRFCQPNREVLPTAALHTLEHLLAGFLRNHLDGIIDISPMGCR 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446086566  83 TGFYVSFINHDNYDDVLNIVEATLNDVLNA-TEVPACNEVQCGWAASHSLEGAKTIAQAFLDKRNEWHD 150
Cdd:COG1854   81 TGFYLILIGEPSSEEVADALEETLEDVLEAeGEVPAANEVQCGNYRDHSLEGAKEIARKVLEKGIEWID 149
 
Name Accession Description Interval E-value
LuxS COG1854
S-ribosylhomocysteine lyase LuxS, autoinducer biosynthesis [Signal transduction mechanisms];
3-150 5.54e-97

S-ribosylhomocysteine lyase LuxS, autoinducer biosynthesis [Signal transduction mechanisms];


Pssm-ID: 441459  Cd Length: 149  Bit Score: 275.87  E-value: 5.54e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086566   3 KMNVESFNLDHTKVVAPFIRLAGTMEGLNGDVIHKYDIRFKQPNKEHMDMPGLHSLEHLMAENIRNHSDKVVDLSPMGCQ 82
Cdd:COG1854    1 MPKVESFTLDHTKVKAPYVRVAGVDKGPGGDVITKFDLRFCQPNREVLPTAALHTLEHLLAGFLRNHLDGIIDISPMGCR 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446086566  83 TGFYVSFINHDNYDDVLNIVEATLNDVLNA-TEVPACNEVQCGWAASHSLEGAKTIAQAFLDKRNEWHD 150
Cdd:COG1854   81 TGFYLILIGEPSSEEVADALEETLEDVLEAeGEVPAANEVQCGNYRDHSLEGAKEIARKVLEKGIEWID 149
PRK02260 PRK02260
S-ribosylhomocysteine lyase;
5-152 9.69e-90

S-ribosylhomocysteine lyase;


Pssm-ID: 179399  Cd Length: 158  Bit Score: 258.19  E-value: 9.69e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086566   5 NVESFNLDHTKVVAPFIRLAGTMEGLNGDVIHKYDIRFKQPNKEHMDMPGLHSLEHLMAENIRNHSD---KVVDLSPMGC 81
Cdd:PRK02260   3 LVESFTLDHTKVKAPYVRLAGTKDGPKGDVITKFDLRFCQPNKEAMPTAGIHTLEHLLAGFLRNHLDggvEIIDISPMGC 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446086566  82 QTGFYVSFINHDNYDDVLNIVEATLNDVL-NATEVPACNEVQCGWAASHSLEGAKTIAQAFLDKRNEWHDVF 152
Cdd:PRK02260  83 RTGFYLILIGTPDEEDVADALKATLEDVLdDQEEVPGANEYQCGNYKDHSLEGAKEIARKILDQGISVNPNE 154
LuxS pfam02664
S-Ribosylhomocysteinase (LuxS); This family consists of the LuxS protein involved in ...
5-148 5.81e-79

S-Ribosylhomocysteinase (LuxS); This family consists of the LuxS protein involved in autoinducer AI2 synthesis and its hypothetical relatives. S-ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether bond in S-ribosylhomocysteine (SRH) to produce homocysteine and 4,5-dihydroxy-2,3-pentanedione (DPD), the precursor of type II bacterial quorum sensing molecule.


Pssm-ID: 426910  Cd Length: 150  Bit Score: 230.44  E-value: 5.81e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086566    5 NVESFNLDHTKVVaPFIRLAGTMEGLNGDVIHKYDIRFKQPN-KEHMDMPGLHSLEHLMAENIRNHSD---KVVDLSPMG 80
Cdd:pfam02664   1 KIESFTVDHTKLK-PGVYVSRKDTGPGGDVITTFDLRFKQPNrEPVMNTAAIHTIEHLFATFLRNHLEgddKIIYFGPMG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446086566   81 CQTGFYVSFINHDNYDDVLNIVEATLNDVLN---ATEVPACNEVQCGWAASHSLEGAKTIAQAFLDKRNEW 148
Cdd:pfam02664  80 CRTGFYLILIGDLSSEDVLPLLKETFEFIADfegEEEIPGANAKQCGNYLDHSLEMAKEEAKKYLEEVLEN 150
 
Name Accession Description Interval E-value
LuxS COG1854
S-ribosylhomocysteine lyase LuxS, autoinducer biosynthesis [Signal transduction mechanisms];
3-150 5.54e-97

S-ribosylhomocysteine lyase LuxS, autoinducer biosynthesis [Signal transduction mechanisms];


Pssm-ID: 441459  Cd Length: 149  Bit Score: 275.87  E-value: 5.54e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086566   3 KMNVESFNLDHTKVVAPFIRLAGTMEGLNGDVIHKYDIRFKQPNKEHMDMPGLHSLEHLMAENIRNHSDKVVDLSPMGCQ 82
Cdd:COG1854    1 MPKVESFTLDHTKVKAPYVRVAGVDKGPGGDVITKFDLRFCQPNREVLPTAALHTLEHLLAGFLRNHLDGIIDISPMGCR 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446086566  83 TGFYVSFINHDNYDDVLNIVEATLNDVLNA-TEVPACNEVQCGWAASHSLEGAKTIAQAFLDKRNEWHD 150
Cdd:COG1854   81 TGFYLILIGEPSSEEVADALEETLEDVLEAeGEVPAANEVQCGNYRDHSLEGAKEIARKVLEKGIEWID 149
PRK02260 PRK02260
S-ribosylhomocysteine lyase;
5-152 9.69e-90

S-ribosylhomocysteine lyase;


Pssm-ID: 179399  Cd Length: 158  Bit Score: 258.19  E-value: 9.69e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086566   5 NVESFNLDHTKVVAPFIRLAGTMEGLNGDVIHKYDIRFKQPNKEHMDMPGLHSLEHLMAENIRNHSD---KVVDLSPMGC 81
Cdd:PRK02260   3 LVESFTLDHTKVKAPYVRLAGTKDGPKGDVITKFDLRFCQPNKEAMPTAGIHTLEHLLAGFLRNHLDggvEIIDISPMGC 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446086566  82 QTGFYVSFINHDNYDDVLNIVEATLNDVL-NATEVPACNEVQCGWAASHSLEGAKTIAQAFLDKRNEWHDVF 152
Cdd:PRK02260  83 RTGFYLILIGTPDEEDVADALKATLEDVLdDQEEVPGANEYQCGNYKDHSLEGAKEIARKILDQGISVNPNE 154
LuxS pfam02664
S-Ribosylhomocysteinase (LuxS); This family consists of the LuxS protein involved in ...
5-148 5.81e-79

S-Ribosylhomocysteinase (LuxS); This family consists of the LuxS protein involved in autoinducer AI2 synthesis and its hypothetical relatives. S-ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether bond in S-ribosylhomocysteine (SRH) to produce homocysteine and 4,5-dihydroxy-2,3-pentanedione (DPD), the precursor of type II bacterial quorum sensing molecule.


Pssm-ID: 426910  Cd Length: 150  Bit Score: 230.44  E-value: 5.81e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086566    5 NVESFNLDHTKVVaPFIRLAGTMEGLNGDVIHKYDIRFKQPN-KEHMDMPGLHSLEHLMAENIRNHSD---KVVDLSPMG 80
Cdd:pfam02664   1 KIESFTVDHTKLK-PGVYVSRKDTGPGGDVITTFDLRFKQPNrEPVMNTAAIHTIEHLFATFLRNHLEgddKIIYFGPMG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446086566   81 CQTGFYVSFINHDNYDDVLNIVEATLNDVLN---ATEVPACNEVQCGWAASHSLEGAKTIAQAFLDKRNEW 148
Cdd:pfam02664  80 CRTGFYLILIGDLSSEDVLPLLKETFEFIADfegEEEIPGANAKQCGNYLDHSLEMAKEEAKKYLEEVLEN 150
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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