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Conserved domains on  [gi|1293299372|gb|AUA21452|]
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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

 Zoom to residue level

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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 ...
 4-161 1.18e-57

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: 177.78  E-value: 1.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKcELFQSEETAENAKKILLFFRKNNLPVIHIQHISTDktASFFLPNTHGSEINKIVFPLDNEEII 83
Cdd:cd01014     1 ALLVIDVQNGYFDGGL-PPLNNEAALENIAALIAAARAAGIPVIHVRHIDDE--GGSFAPGSEGWEIHPELAPLEGETVI 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1293299372  84 TKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKNLSWNNIEINANTVHQVF 161
Cdd:cd01014    78 EKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVLSAEEIHAHY 155
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 4-161 1.18e-57

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: 177.78  E-value: 1.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKcELFQSEETAENAKKILLFFRKNNLPVIHIQHISTDktASFFLPNTHGSEINKIVFPLDNEEII 83
Cdd:cd01014     1 ALLVIDVQNGYFDGGL-PPLNNEAALENIAALIAAARAAGIPVIHVRHIDDE--GGSFAPGSEGWEIHPELAPLEGETVI 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1293299372  84 TKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKNLSWNNIEINANTVHQVF 161
Cdd:cd01014    78 EKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVLSAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 4-172 2.46e-49

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: 157.37  E-value: 2.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKCELFQSEETAENAKKILLFFRKNNLPVIHIQHISTDKTASF---------FLPNTHGSEINKIV 74
Cdd:COG1335     1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFaefdlwpphCVPGTPGAELVPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  75 FPLDNEEIITKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKNLswnnieina 154
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP--------- 151

                         170
                  ....*....|....*...
gi 1293299372 155 nTVHQVFMASLQNSFADV 172
Cdd:COG1335   152 -EAHEAALARLRAAGATV 168
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 4-172 2.20e-38

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 129.45  E-value: 2.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKCELFQSEETAENAKKILLFFRKNNLPVIHIQHISTDKTASF---------FLPNTHGSEINKIV 74
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFalkdrpspaFPPGTTGAELVPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  75 FPLDNEEIITKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKNLSWnnieina 154
Cdd:pfam00857  82 APLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEA------- 154

                         170
                  ....*....|....*...
gi 1293299372 155 ntvHQVFMASLQNSFADV 172
Cdd:pfam00857 155 ---HDAALERLAQRGAEV 169
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
1-146 2.47e-10

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 57.31  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   1 MSIALILIDIQNDYFKNGKCELFQSEETAENAKKILLFFRKNNLPVIHIQ------HIS--------------TDKTASF 60
Cdd:PRK11609    1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQdwhpanHGSfasnhgaepgtqgeLDGLPQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  61 FLP-----NTHGSE---------INKIVFPLDNEEIitkhtpDS---FF------ETDLQSILEKKNITNLVICGMMSHM 117
Cdd:PRK11609   81 WWPdhcvqNSEGAAlhpllnqkaIDAVFHKGENPLI------DSysaFFdnghrqKTALDDWLREHGITELIVMGLATDY 154

                         170       180
                  ....*....|....*....|....*....
gi 1293299372 118 CIDTSVRTAKKLRYDITLISDACTTKNLS 146
Cdd:PRK11609  155 CVKFTVLDALALGYQVNVITDGCRGVNLQ 183
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 4-161 1.18e-57

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: 177.78  E-value: 1.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKcELFQSEETAENAKKILLFFRKNNLPVIHIQHISTDktASFFLPNTHGSEINKIVFPLDNEEII 83
Cdd:cd01014     1 ALLVIDVQNGYFDGGL-PPLNNEAALENIAALIAAARAAGIPVIHVRHIDDE--GGSFAPGSEGWEIHPELAPLEGETVI 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1293299372  84 TKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKNLSWNNIEINANTVHQVF 161
Cdd:cd01014    78 EKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVLSAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 4-172 2.46e-49

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: 157.37  E-value: 2.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKCELFQSEETAENAKKILLFFRKNNLPVIHIQHISTDKTASF---------FLPNTHGSEINKIV 74
Cdd:COG1335     1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFaefdlwpphCVPGTPGAELVPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  75 FPLDNEEIITKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKNLswnnieina 154
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP--------- 151

                         170
                  ....*....|....*...
gi 1293299372 155 nTVHQVFMASLQNSFADV 172
Cdd:COG1335   152 -EAHEAALARLRAAGATV 168
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 4-142 6.18e-45

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: 145.87  E-value: 6.18e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKCELFQSEETAENAKKILLFFRKNNLPVIHIQHISTDKTASF--------FLPNTHGSEINKIVF 75
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFaellwpphCVKGTEGAELVPELA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1293299372  76 PLDNEEIITKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTT 142
Cdd:cd00431    81 PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACAT 147
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 4-172 2.20e-38

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 129.45  E-value: 2.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKCELFQSEETAENAKKILLFFRKNNLPVIHIQHISTDKTASF---------FLPNTHGSEINKIV 74
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFalkdrpspaFPPGTTGAELVPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  75 FPLDNEEIITKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKNLSWnnieina 154
Cdd:pfam00857  82 APLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEA------- 154

                         170
                  ....*....|....*...
gi 1293299372 155 ntvHQVFMASLQNSFADV 172
Cdd:pfam00857 155 ---HDAALERLAQRGAEV 169
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
4-176 1.84e-12

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 62.95  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNdYFkngkCELF-----QSEETAENAKKILLFFRKNNLPVIHIQHIS----------TDKTASFFLPNTHGS 68
Cdd:COG1535    21 ALLIHDMQN-YF----LRPYdpdepPIRELVANIARLRDACRAAGIPVVYTAQPGdqtpedrgllNDFWGPGLTAGPEGQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  69 EINKIVFPLDNEEIITKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAkkLRYDI--TLISDACTTKNLs 146
Cdd:COG1535    96 EIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDA--FMRDIqpFVVADAVADFSR- 172

                         170       180       190
                  ....*....|....*....|....*....|
gi 1293299372 147 wnnieinanTVHQVFMASLQNSFADVKNTD 176
Cdd:COG1535   173 ---------EEHRMALEYVAGRCGVVVTTD 193
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 4-176 1.81e-11

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: 59.72  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKCELFQSEETAENAKKILLFFRKNNLPVIHIQHISTDKTA------------SFFLPNTHGSEIN 71
Cdd:cd01015     1 ALLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTVVYDPDGAdgglwarkvpamSDLVEGSPLAAIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  72 KIVFPLDNEEIITKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKnlswnnie 151
Cdd:cd01015    81 DELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDR-------- 152

                         170       180
                  ....*....|....*....|....*
gi 1293299372 152 inANTVHQVFMASLQNSFADVKNTD 176
Cdd:cd01015   153 --APAPHEANLFDIDNKYGDVVSTD 175
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
1-146 2.47e-10

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 57.31  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   1 MSIALILIDIQNDYFKNGKCELFQSEETAENAKKILLFFRKNNLPVIHIQ------HIS--------------TDKTASF 60
Cdd:PRK11609    1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQdwhpanHGSfasnhgaepgtqgeLDGLPQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  61 FLP-----NTHGSE---------INKIVFPLDNEEIitkhtpDS---FF------ETDLQSILEKKNITNLVICGMMSHM 117
Cdd:PRK11609   81 WWPdhcvqNSEGAAlhpllnqkaIDAVFHKGENPLI------DSysaFFdnghrqKTALDDWLREHGITELIVMGLATDY 154

                         170       180
                  ....*....|....*....|....*....
gi 1293299372 118 CIDTSVRTAKKLRYDITLISDACTTKNLS 146
Cdd:PRK11609  155 CVKFTVLDALALGYQVNVITDGCRGVNLQ 183
PLN02621 PLN02621
nicotinamidase
 4-177 2.59e-08

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 51.32  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNdYFKNgkcelfQSEETAENAKKILLFFRKNNLPVIHIQHISTDKT----------ASFFLPNTHGSEI-NK 72
Cdd:PLN02621   22 ALLVIDMQN-YFSS------MAEPILPALLTTIDLCRRASIPVFFTRHSHKSPSdygmlgewwdGDLILDGTTEAELmPE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  73 IVFPLDNEEIITKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKNLSwnniei 152
Cdd:PLN02621   95 IGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEE------ 168

                         170       180
                  ....*....|....*....|....*
gi 1293299372 153 nantVHQVFMASLQNSFADVKNTDK 177
Cdd:PLN02621  169 ----LHEATLKNLAYGFAYLVDCDR 189
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 4-140 2.65e-07

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 48.52  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNGKCELFQSEETAENAKKI-------LLFFRKNNLPVIHIQHISTDKTASFFLPNTH---------- 66
Cdd:PTZ00331   14 ALIIVDVQNDFCKGGSLAVPDAEEVIPVINQVrqshhfdLVVATQDWHPPNHISFASNHGKPKILPDGTTqglwpphcvq 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  67 ---GSEINKIVFPLDNEEIITKHTP---DSF--FE------TDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYD 132
Cdd:PTZ00331   94 gtkGAQLHKDLVVERIDIIIRKGTNrdvDSYsaFDndkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTALDAVKLGFK 173


                  ....*...
gi 1293299372 133 ITLISDAC 140
Cdd:PTZ00331  174 VVVLEDAT 181
PRK11440 PRK11440
putative hydrolase; Provisional
 4-180 8.15e-07

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 47.03  E-value: 8.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDY--FKNGKcelFQSEETAENAKKILLFFRKNNLPVIHIQ-HISTDKTASFFLP-----NTHGSEINKIVF 75
Cdd:PRK11440   10 ALVVIDLQEGIlpFAGGP---HTADEVVARAARLAAKFRASGSPVVLVRvGWSADYAEALKQPvdapsPAKVLPENWWQH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  76 PL-----DNEEIITKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTknlswnni 150
Cdd:PRK11440   87 PAalgktDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSA-------- 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1293299372 151 einANTV-HQVFMASLQNSFADVKNTDKFLS 180
Cdd:PRK11440  159 ---ASAEqHQNSMNHIFPRIARVRSVEEILN 186
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 4-144 1.37e-06

YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.


Pssm-ID: 238494 [Multi-domain]  Cd Length: 157  Bit Score: 46.05  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   4 ALILIDIQNDYFKNgkceLFQSEETAENAKKILLFFRKNNLPVIHiqhistdkTASFFLPNTHGSEINKIVFPldNEEII 83
Cdd:cd01012     1 ALLLVDVQEKLAPA----IKSFDELINNTVKLAKAAKLLDVPVIL--------TEQYPKGLGPTVPELREVFP--DAPVI 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1293299372  84 TKHTPDSFFETDLQSILEKKNITNLVICGMMSHMCIDTSVRTAKKLRYDITLISDACTTKN 144
Cdd:cd01012    67 EKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRS 127
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 2-140 2.01e-06

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: 46.10  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372   2 SIALILIDIQNDYFKNGkcELFQSE---------ETAENAKKILLFFRKNNLPVIHIQHISTDKTASFFL---------- 62
Cdd:cd01011     1 TDALLVVDVQNDFCPGG--ALAVPGgdaivplinALLSLFQYDLVVATQDWHPANHASFASNHPGQMPFItlppgpqvlw 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293299372  63 -----PNTHGSEINKIVFPLDNEEIITKHT-PDS-----FFE------TDLQSILEKKNITNLVICGMMSHMCIDTSVRT 125
Cdd:cd01011    79 pdhcvQGTPGAELHPGLPVPDIDLIVRKGTnPDIdsysaFFDndrrssTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158

                         170
                  ....*....|....*
gi 1293299372 126 AKKLRYDITLISDAC 140
Cdd:cd01011   159 ALKAGFEVRVLEDAC 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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