NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2090333761|gb|QZY81230|]
View 

S-ribosylhomocysteine lyase [Klebsiella sp. CTHL.F3a]

Protein Classification

S-ribosylhomocysteine lyase( domain architecture ID 10011781)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK02260 PRK02260
S-ribosylhomocysteine lyase;
1-161 1.24e-109

S-ribosylhomocysteine lyase;


:

Pssm-ID: 179399  Cd Length: 158  Bit Score: 309.04  E-value: 1.24e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761   1 MPLLDSFTVDHTRMEAPAVRVAKKMNTPHGDEITVFDLRFCVPNQEVMPERGIHTLEHLFAGFMRDHLNGnGVEIIDISP 80
Cdd:PRK02260    1 MPLVESFTLDHTKVKAPYVRLAGTKDGPKGDVITKFDLRFCQPNKEAMPTAGIHTLEHLLAGFLRNHLDG-GVEIIDISP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761  81 MGCRTGFYMSLIGTPDEQRVADAWKAAMADVLkvKDQNQIPELNVYQCGTYTMHSLEEAQEIARHIIERDVRVNSNDELA 160
Cdd:PRK02260   80 MGCRTGFYLILIGTPDEEDVADALKATLEDVL--DDQEEVPGANEYQCGNYKDHSLEGAKEIARKILDQGISVNPNEELA 157

                  .
gi 2090333761 161 L 161
Cdd:PRK02260  158 L 158
 
Name Accession Description Interval E-value
PRK02260 PRK02260
S-ribosylhomocysteine lyase;
1-161 1.24e-109

S-ribosylhomocysteine lyase;


Pssm-ID: 179399  Cd Length: 158  Bit Score: 309.04  E-value: 1.24e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761   1 MPLLDSFTVDHTRMEAPAVRVAKKMNTPHGDEITVFDLRFCVPNQEVMPERGIHTLEHLFAGFMRDHLNGnGVEIIDISP 80
Cdd:PRK02260    1 MPLVESFTLDHTKVKAPYVRLAGTKDGPKGDVITKFDLRFCQPNKEAMPTAGIHTLEHLLAGFLRNHLDG-GVEIIDISP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761  81 MGCRTGFYMSLIGTPDEQRVADAWKAAMADVLkvKDQNQIPELNVYQCGTYTMHSLEEAQEIARHIIERDVRVNSNDELA 160
Cdd:PRK02260   80 MGCRTGFYLILIGTPDEEDVADALKATLEDVL--DDQEEVPGANEYQCGNYKDHSLEGAKEIARKILDQGISVNPNEELA 157

                  .
gi 2090333761 161 L 161
Cdd:PRK02260  158 L 158
LuxS COG1854
S-ribosylhomocysteine lyase LuxS, autoinducer biosynthesis [Signal transduction mechanisms];
1-154 6.62e-96

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


Pssm-ID: 441459  Cd Length: 149  Bit Score: 273.94  E-value: 6.62e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761   1 MPLLDSFTVDHTRMEAPAVRVAKKMNTPHGDEITVFDLRFCVPNQEVMPERGIHTLEHLFAGFMRDHLNGngveIIDISP 80
Cdd:COG1854     1 MPKVESFTLDHTKVKAPYVRVAGVDKGPGGDVITKFDLRFCQPNREVLPTAALHTLEHLLAGFLRNHLDG----IIDISP 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2090333761  81 MGCRTGFYMSLIGTPDEQRVADAWKAAMADVLKVkdQNQIPELNVYQCGTYTMHSLEEAQEIARHIIERDVRVN 154
Cdd:COG1854    77 MGCRTGFYLILIGEPSSEEVADALEETLEDVLEA--EGEVPAANEVQCGNYRDHSLEGAKEIARKVLEKGIEWI 148
LuxS pfam02664
S-Ribosylhomocysteinase (LuxS); This family consists of the LuxS protein involved in ...
3-149 2.71e-86

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: 249.70  E-value: 2.71e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761   3 LLDSFTVDHTRMEaPAVRVAKKMNTPHGDEITVFDLRFCVPNQE-VMPERGIHTLEHLFAGFMRDHLNGnGVEIIDISPM 81
Cdd:pfam02664   1 KIESFTVDHTKLK-PGVYVSRKDTGPGGDVITTFDLRFKQPNREpVMNTAAIHTIEHLFATFLRNHLEG-DDKIIYFGPM 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2090333761  82 GCRTGFYMSLIGTPDEQRVADAWKAAMADVLKVKDQNQIPELNVYQCGTYTMHSLEEAQEIARHIIER 149
Cdd:pfam02664  79 GCRTGFYLILIGDLSSEDVLPLLKETFEFIADFEGEEEIPGANAKQCGNYLDHSLEMAKEEAKKYLEE 146
 
Name Accession Description Interval E-value
PRK02260 PRK02260
S-ribosylhomocysteine lyase;
1-161 1.24e-109

S-ribosylhomocysteine lyase;


Pssm-ID: 179399  Cd Length: 158  Bit Score: 309.04  E-value: 1.24e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761   1 MPLLDSFTVDHTRMEAPAVRVAKKMNTPHGDEITVFDLRFCVPNQEVMPERGIHTLEHLFAGFMRDHLNGnGVEIIDISP 80
Cdd:PRK02260    1 MPLVESFTLDHTKVKAPYVRLAGTKDGPKGDVITKFDLRFCQPNKEAMPTAGIHTLEHLLAGFLRNHLDG-GVEIIDISP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761  81 MGCRTGFYMSLIGTPDEQRVADAWKAAMADVLkvKDQNQIPELNVYQCGTYTMHSLEEAQEIARHIIERDVRVNSNDELA 160
Cdd:PRK02260   80 MGCRTGFYLILIGTPDEEDVADALKATLEDVL--DDQEEVPGANEYQCGNYKDHSLEGAKEIARKILDQGISVNPNEELA 157

                  .
gi 2090333761 161 L 161
Cdd:PRK02260  158 L 158
LuxS COG1854
S-ribosylhomocysteine lyase LuxS, autoinducer biosynthesis [Signal transduction mechanisms];
1-154 6.62e-96

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


Pssm-ID: 441459  Cd Length: 149  Bit Score: 273.94  E-value: 6.62e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761   1 MPLLDSFTVDHTRMEAPAVRVAKKMNTPHGDEITVFDLRFCVPNQEVMPERGIHTLEHLFAGFMRDHLNGngveIIDISP 80
Cdd:COG1854     1 MPKVESFTLDHTKVKAPYVRVAGVDKGPGGDVITKFDLRFCQPNREVLPTAALHTLEHLLAGFLRNHLDG----IIDISP 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2090333761  81 MGCRTGFYMSLIGTPDEQRVADAWKAAMADVLKVkdQNQIPELNVYQCGTYTMHSLEEAQEIARHIIERDVRVN 154
Cdd:COG1854    77 MGCRTGFYLILIGEPSSEEVADALEETLEDVLEA--EGEVPAANEVQCGNYRDHSLEGAKEIARKVLEKGIEWI 148
LuxS pfam02664
S-Ribosylhomocysteinase (LuxS); This family consists of the LuxS protein involved in ...
3-149 2.71e-86

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: 249.70  E-value: 2.71e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090333761   3 LLDSFTVDHTRMEaPAVRVAKKMNTPHGDEITVFDLRFCVPNQE-VMPERGIHTLEHLFAGFMRDHLNGnGVEIIDISPM 81
Cdd:pfam02664   1 KIESFTVDHTKLK-PGVYVSRKDTGPGGDVITTFDLRFKQPNREpVMNTAAIHTIEHLFATFLRNHLEG-DDKIIYFGPM 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2090333761  82 GCRTGFYMSLIGTPDEQRVADAWKAAMADVLKVKDQNQIPELNVYQCGTYTMHSLEEAQEIARHIIER 149
Cdd:pfam02664  79 GCRTGFYLILIGDLSSEDVLPLLKETFEFIADFEGEEEIPGANAKQCGNYLDHSLEMAKEEAKKYLEE 146
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH