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Conserved domains on  [gi|2053417437|gb|QWS62267|]
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cysteine hydrolase [Clostridioides difficile]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 10099067)

cysteine hydrolase family protein related to isochorismatase and nicotinamidase; catalyzes the hydrolysis of a chemical bond using an active site cysteinyl residue

EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 2-150 5.20e-51

Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.


:

Pssm-ID: 238496 [Multi-domain]  Cd Length: 155  Bit Score: 160.45  E-value: 5.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQKLI--TNERLYKFNEFVVNVENLIDTARKNNIEVIYVRHDDGVENELTKGKNGFEIYEKFKPCNGEKIFDKK 79
Cdd:cd01014     1 ALLVIDVQNGYfdGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGSFAPGSEGWEIHPELAPLEGETVIEKT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053417437  80 VNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPAYSNTTVDNFF----MSAEQSYKYY 150
Cdd:cd01014    81 VPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDhggvLSAEEIHAHY 155
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 2-150 5.20e-51

Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.


Pssm-ID: 238496 [Multi-domain]  Cd Length: 155  Bit Score: 160.45  E-value: 5.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQKLI--TNERLYKFNEFVVNVENLIDTARKNNIEVIYVRHDDGVENELTKGKNGFEIYEKFKPCNGEKIFDKK 79
Cdd:cd01014     1 ALLVIDVQNGYfdGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGSFAPGSEGWEIHPELAPLEGETVIEKT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053417437  80 VNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPAYSNTTVDNFF----MSAEQSYKYY 150
Cdd:cd01014    81 VPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDhggvLSAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 2-130 2.47e-30

Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]; Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440946 [Multi-domain]  Cd Length: 169  Bit Score: 108.45  E-value: 2.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQKLITNE---RLYKFNEFVVNVENLIDTARKNNIEVIYVRHD-----------DGVENELTKGKNGFEIYEKF 67
Cdd:COG1335     1 ALLVIDVQNDFVPPgalAVPGADAVVANIARLLAAARAAGVPVIHTRDWhppdgsefaefDLWPPHCVPGTPGAELVPEL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2053417437  68 KPCNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPA 130
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVE 143
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 3-130 3.80e-27

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 100.17  E-value: 3.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   3 LLIVDAQKLITNERLYK---FNEFVVNVENLIDTARKNNIEVIYVRH-----------DDGVENELTKGKNGFEIYEKFK 68
Cdd:pfam00857   3 LLVIDMQNDFVDSGGPKvegIAAILENINRLLKAARKAGIPVIFTRQvpepddadfalKDRPSPAFPPGTTGAELVPELA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2053417437  69 PCNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPA 130
Cdd:pfam00857  83 PLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVS 144
PLN02621 PLN02621
nicotinamidase
 2-137 2.03e-09

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 54.02  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQklitnERLYKFNEFVV-NVENLIDTARKNNIEVIYVRH--------------------DDG-VENELTKGKN 59
Cdd:PLN02621   22 ALLVIDMQ-----NYFSSMAEPILpALLTTIDLCRRASIPVFFTRHshkspsdygmlgewwdgdliLDGtTEAELMPEIG 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2053417437  60 GFEiyekfkpcNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPAYSNTTVD 137
Cdd:PLN02621   97 RVT--------GPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN 166
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 2-150 5.20e-51

Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.


Pssm-ID: 238496 [Multi-domain]  Cd Length: 155  Bit Score: 160.45  E-value: 5.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQKLI--TNERLYKFNEFVVNVENLIDTARKNNIEVIYVRHDDGVENELTKGKNGFEIYEKFKPCNGEKIFDKK 79
Cdd:cd01014     1 ALLVIDVQNGYfdGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGSFAPGSEGWEIHPELAPLEGETVIEKT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053417437  80 VNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPAYSNTTVDNFF----MSAEQSYKYY 150
Cdd:cd01014    81 VPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDhggvLSAEEIHAHY 155
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 2-130 5.84e-36

Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine amidohydrolase), involved in creatine metabolism and nicotinamidase, converting nicotinamide to nicotinic acid and ammonia in the pyridine nucleotide cycle. It also contains isochorismatase, an enzyme that catalyzes the conversion of isochorismate to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of the vinyl ether bond, and other related enzymes with unknown function.


Pssm-ID: 238245 [Multi-domain]  Cd Length: 161  Bit Score: 122.38  E-value: 5.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQKLITN---ERLYKFNEFVVNVENLIDTARKNNIEVIYVRH----DDGVENE------LTKGKNGFEIYEKFK 68
Cdd:cd00431     1 ALLVVDMQNDFVPgggLLLPGADELVPNINRLLAAARAAGIPVIFTRDwhppDDPEFAEllwpphCVKGTEGAELVPELA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2053417437  69 PCNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPA 130
Cdd:cd00431    81 PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVE 142
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 2-130 2.47e-30

Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]; Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440946 [Multi-domain]  Cd Length: 169  Bit Score: 108.45  E-value: 2.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQKLITNE---RLYKFNEFVVNVENLIDTARKNNIEVIYVRHD-----------DGVENELTKGKNGFEIYEKF 67
Cdd:COG1335     1 ALLVIDVQNDFVPPgalAVPGADAVVANIARLLAAARAAGVPVIHTRDWhppdgsefaefDLWPPHCVPGTPGAELVPEL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2053417437  68 KPCNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPA 130
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVE 143
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 3-130 3.80e-27

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 100.17  E-value: 3.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   3 LLIVDAQKLITNERLYK---FNEFVVNVENLIDTARKNNIEVIYVRH-----------DDGVENELTKGKNGFEIYEKFK 68
Cdd:pfam00857   3 LLVIDMQNDFVDSGGPKvegIAAILENINRLLKAARKAGIPVIFTRQvpepddadfalKDRPSPAFPPGTTGAELVPELA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2053417437  69 PCNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPA 130
Cdd:pfam00857  83 PLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVS 144
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 3-129 6.81e-14

N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, carbon dioxide and ammonia. CSHase is involved in one of the two alternative pathways for creatinine degradation to glycine in microorganisms.This CSHase-containing pathway degrades creatinine via N-methylhydantoin N-carbamoylsarcosine and sarcosine to glycine. Enzymes of this pathway are used in the diagnosis for renal disfunction, for determining creatinine levels in urine and serum.


Pssm-ID: 238497 [Multi-domain]  Cd Length: 179  Bit Score: 65.89  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   3 LLIVDAQKLITNERLYKFNEFVVNVEN---LIDTARKNNIEVIY--VRHDDG------------VENELTKGKNGFEIYE 65
Cdd:cd01015     2 LLVIDLVEGYTQPGSYLAPGIAAALENvqrLLAAARAAGVPVIHttVVYDPDgadgglwarkvpAMSDLVEGSPLAAICD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2053417437  66 KFKPCNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVP 129
Cdd:cd01015    82 ELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVV 145
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
2-130 4.15e-12

Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 61.40  E-value: 4.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQklitnerlYKF-----------NEFVVNVENLIDTARKNNIEVIYVRH-------DDGVENE-----LTKGK 58
Cdd:COG1535    21 ALLIHDMQ--------NYFlrpydpdeppiRELVANIARLRDACRAAGIPVVYTAQpgdqtpeDRGLLNDfwgpgLTAGP 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2053417437  59 NGFEIYEKFKPCNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPA 130
Cdd:COG1535    93 EGQEIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVA 164
PLN02621 PLN02621
nicotinamidase
 2-137 2.03e-09

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 54.02  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQklitnERLYKFNEFVV-NVENLIDTARKNNIEVIYVRH--------------------DDG-VENELTKGKN 59
Cdd:PLN02621   22 ALLVIDMQ-----NYFSSMAEPILpALLTTIDLCRRASIPVFFTRHshkspsdygmlgewwdgdliLDGtTEAELMPEIG 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2053417437  60 GFEiyekfkpcNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNIIVPAYSNTTVD 137
Cdd:PLN02621   97 RVT--------GPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN 166
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 60-128 6.95e-09

Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, converts nicotinamide to nicotinic acid (niacin) and ammonia, which in turn can be recycled to make nicotinamide adenine dinucleotide (NAD). The same enzyme is also called pyrazinamidase, because in converts the tuberculosis drug pyrazinamide (PZA) into its active form pyrazinoic acid (POA).


Pssm-ID: 238493  Cd Length: 196  Bit Score: 52.65  E-value: 6.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437  60 GFEIYEKFKPCNGEKIFDKKVN------SAFKE------TGLLEYLTNNGEKDIIIAGLQTDYCIDATIKCGFEHGFNII 127
Cdd:cd01011    88 GAELHPGLPVPDIDLIVRKGTNpdidsySAFFDndrrssTGLAEYLRERGIDRVDVVGLATDYCVKATALDALKAGFEVR 167


                  .
gi 2053417437 128 V 128
Cdd:cd01011   168 V 168
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 2-105 8.55e-08

Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the conversion of isochorismate, in the presence of water, to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of a vinyl ether, an uncommon reaction in biological systems. Isochorismatase is part of the phenazine biosynthesis pathway. Phenazines are antimicrobial compounds that provide the competitive advantage for certain bacteria.


Pssm-ID: 238495  Cd Length: 203  Bit Score: 49.64  E-value: 8.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417437   2 VLLIVDAQKLITN---ERLYKFNEFVVNVENLIDTARKNNIEVIYVRH-------DDGVENE-----LTKGKNGFEIYEK 66
Cdd:cd01013    31 VLLVHDMQRYFLDfydESAEPVPQLIANIARLRDWCRQAGIPVVYTAQpgnqtpeQRALLNDfwgpgLTASPEETKIVTE 110

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2053417437  67 FKPCNGEKIFDKKVNSAFKETGLLEYLTNNGEKDIIIAG 105
Cdd:cd01013   111 LAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITG 149
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 56-121 3.08e-04

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 39.66  E-value: 3.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2053417437  56 KGKN-GFEIYEKFKPCNGEKifdkkvnsafkeTGLLEYLTNNGEKDIIIAGLQTDYCIDAT----IKCGFE 121
Cdd:PTZ00331  115 KGTNrDVDSYSAFDNDKGSK------------TGLAQILKAHGVRRVFICGLAFDFCVLFTaldaVKLGFK 173
 
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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