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Conserved domains on  [gi|2520371918|ref|WP_285317433|]
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cysteine hydrolase family protein [Stenotrophomonas maltophilia group sp. Smal35]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 10003554)

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

CATH:  3.40.50.850
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
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 48-230 1.60e-33

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: 119.24  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  48 AVLVIDFQNEYFDakaapgfaGGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA----------QGSV 117
Cdd:COG1335     1 ALLVIDVQNDFVP--------PGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 118 NAAFHRDLQPRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDASA 197
Cdd:COG1335    73 GAELVPELAPLPGDPVVDKTRYSAFYG---TDLDELLRERGIDTLVVAGLATDVCVLSTARDALD--LGYEVTVVEDACA 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2520371918 198 SRDLDlaggqridhraLHDASLAQIEDAFGDVM 230
Cdd:COG1335   148 SRDPE-----------AHEAALARLRAAGATVV 169
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 48-230 1.60e-33

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: 119.24  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  48 AVLVIDFQNEYFDakaapgfaGGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA----------QGSV 117
Cdd:COG1335     1 ALLVIDVQNDFVP--------PGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 118 NAAFHRDLQPRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDASA 197
Cdd:COG1335    73 GAELVPELAPLPGDPVVDKTRYSAFYG---TDLDELLRERGIDTLVVAGLATDVCVLSTARDALD--LGYEVTVVEDACA 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2520371918 198 SRDLDlaggqridhraLHDASLAQIEDAFGDVM 230
Cdd:COG1335   148 SRDPE-----------AHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 47-233 2.12e-31

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 113.65  E-value: 2.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  47 TAVLVIDFQNEYFDakaapgfaGGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGA----------PLFAQGS 116
Cdd:pfam00857   1 TALLVIDMQNDFVD--------SGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDadfalkdrpsPAFPPGT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 117 VNAAFHRDLQPRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDAS 196
Cdd:pfam00857  73 TGAELVPELAPLPGDLVVDKTRFSAFAG---TDLDEILRELGIDTLVLAGVATDVCVLSTARDALD--RGYEVVVVSDAC 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2520371918 197 ASRDLDlaggqridhraLHDASLAQIEDAFGDVMSTD 233
Cdd:pfam00857 148 ASLSPE-----------AHDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 48-223 1.85e-29

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: 108.12  E-value: 1.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  48 AVLVIDFQNEYFDakaapgfaGGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA---------QGSVN 118
Cdd:cd00431     1 ALLVVDMQNDFVP--------GGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAellwpphcvKGTEG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 119 AAFHRDLQPRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDASAS 198
Cdd:cd00431    73 AELVPELAPLPDDLVIEKTRYSAFYG---TDLDELLRERGIDTLVVCGIATDICVLATARDALD--LGYRVIVVEDACAT 147

                         170       180
                  ....*....|....*....|....*
gi 2520371918 199 RDLDlaggqridhraLHDASLAQIE 223
Cdd:cd00431   148 RDEE-----------DHEAALERLA 161
PLN02621 PLN02621
nicotinamidase
 43-227 1.84e-12

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 64.03  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  43 DAAKTAVLVIDFQNeYFDAKAAPgfaggrmVIPdgvaalrQAKRVVEFADAHGIRVIHVQHV--LPAGAPLFAQ------ 114
Cdd:PLN02621   17 DPKQAALLVIDMQN-YFSSMAEP-------ILP-------ALLTTIDLCRRASIPVFFTRHShkSPSDYGMLGEwwdgdl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 115 ---GSVNAAFHRDLQ-PRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVI 190
Cdd:PLN02621   82 ildGTTEAELMPEIGrVTGPDEVVEKSTYSAFYN---TRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFV--RGFRVF 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2520371918 191 VSSDASASRDLDlaggqridhraLHDASLAQIedAFG 227
Cdd:PLN02621  157 FSTDATATANEE-----------LHEATLKNL--AYG 180
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 48-230 1.60e-33

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: 119.24  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  48 AVLVIDFQNEYFDakaapgfaGGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA----------QGSV 117
Cdd:COG1335     1 ALLVIDVQNDFVP--------PGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 118 NAAFHRDLQPRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDASA 197
Cdd:COG1335    73 GAELVPELAPLPGDPVVDKTRYSAFYG---TDLDELLRERGIDTLVVAGLATDVCVLSTARDALD--LGYEVTVVEDACA 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2520371918 198 SRDLDlaggqridhraLHDASLAQIEDAFGDVM 230
Cdd:COG1335   148 SRDPE-----------AHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 47-233 2.12e-31

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 113.65  E-value: 2.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  47 TAVLVIDFQNEYFDakaapgfaGGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGA----------PLFAQGS 116
Cdd:pfam00857   1 TALLVIDMQNDFVD--------SGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDadfalkdrpsPAFPPGT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 117 VNAAFHRDLQPRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDAS 196
Cdd:pfam00857  73 TGAELVPELAPLPGDLVVDKTRFSAFAG---TDLDEILRELGIDTLVLAGVATDVCVLSTARDALD--RGYEVVVVSDAC 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2520371918 197 ASRDLDlaggqridhraLHDASLAQIEDAFGDVMSTD 233
Cdd:pfam00857 148 ASLSPE-----------AHDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 48-223 1.85e-29

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: 108.12  E-value: 1.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  48 AVLVIDFQNEYFDakaapgfaGGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA---------QGSVN 118
Cdd:cd00431     1 ALLVVDMQNDFVP--------GGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAellwpphcvKGTEG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 119 AAFHRDLQPRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDASAS 198
Cdd:cd00431    73 AELVPELAPLPDDLVIEKTRYSAFYG---TDLDELLRERGIDTLVVCGIATDICVLATARDALD--LGYRVIVVEDACAT 147

                         170       180
                  ....*....|....*....|....*
gi 2520371918 199 RDLDlaggqridhraLHDASLAQIE 223
Cdd:cd00431   148 RDEE-----------DHEAALERLA 161
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 48-206 9.26e-28

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: 103.82  E-value: 9.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  48 AVLVIDFQNEYFDakaapgfagGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPlFAQGSVNAAFHRDLQP 127
Cdd:cd01014     1 ALLVIDVQNGYFD---------GGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGS-FAPGSEGWEIHPELAP 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2520371918 128 RQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDASASRDLDLAGG 206
Cdd:cd01014    71 LEGETVIEKTVPNAFYG---TDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFD--LGYDVTVVADACATFDLPDHGG 144
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 48-237 1.77e-19

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: 82.84  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  48 AVLVIDFQNEYFDAKA--APGFAggrmvipdgvAALRQAKRVVEFADAHGIRVIHVQHVLPAGAP-------------LF 112
Cdd:cd01015     1 ALLVIDLVEGYTQPGSylAPGIA----------AALENVQRLLAAARAAGVPVIHTTVVYDPDGAdgglwarkvpamsDL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 113 AQGSVNAAFHRDLQPRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVS 192
Cdd:cd01015    71 VEGSPLAAICDELAPQEDEMVLVKKYASAFFG---TSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQ--HGFRPIVV 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2520371918 193 SDASASRdldlaggqridHRALHDASLAQIEDAFGDVMSTDAILA 237
Cdd:cd01015   146 RECVGDR-----------APAPHEANLFDIDNKYGDVVSTDDALA 179
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
28-237 5.27e-19

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 81.82  E-value: 5.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  28 PTIRHMAGAPVAASLDAAKTAVLVIDFQNeYFDAKAAPGFAGGRMVIPDgVAALRqakrvvEFADAHGIRVIHVQHvlPA 107
Cdd:COG1535     1 PTAADLPANKVSWTLDPARAALLIHDMQN-YFLRPYDPDEPPIRELVAN-IARLR------DACRAAGIPVVYTAQ--PG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 108 GAPLF-------------AQGSVNAAFHRDLQPRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVA 174
Cdd:COG1535    71 DQTPEdrgllndfwgpglTAGPEGQEIVDELAPAPGDTVLTKWRYSAFQR---TDLEERLRELGRDQLIITGVYAHIGCL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2520371918 175 GAARDAAAapRGYRVIVSSDASASRDldlaggqridhRALHDASLAQIEDAFGDVMSTDAILA 237
Cdd:COG1535   148 ATAVDAFM--RDIQPFVVADAVADFS-----------REEHRMALEYVAGRCGVVVTTDEVLE 197
PLN02621 PLN02621
nicotinamidase
 43-227 1.84e-12

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 64.03  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  43 DAAKTAVLVIDFQNeYFDAKAAPgfaggrmVIPdgvaalrQAKRVVEFADAHGIRVIHVQHV--LPAGAPLFAQ------ 114
Cdd:PLN02621   17 DPKQAALLVIDMQN-YFSSMAEP-------ILP-------ALLTTIDLCRRASIPVFFTRHShkSPSDYGMLGEwwdgdl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 115 ---GSVNAAFHRDLQ-PRQGETVVQKDNVSVFAGnsaTVLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVI 190
Cdd:PLN02621   82 ildGTTEAELMPEIGrVTGPDEVVEKSTYSAFYN---TRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFV--RGFRVF 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2520371918 191 VSSDASASRDLDlaggqridhraLHDASLAQIedAFG 227
Cdd:PLN02621  157 FSTDATATANEE-----------LHEATLKNL--AYG 180
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
46-173 1.73e-10

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 58.85  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  46 KTAVLVIDFQNEYFdakaapgfAGGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA------------ 113
Cdd:PRK11609    2 KRALLLVDLQNDFC--------AGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQDWHPANHGSFAsnhgaepgtqge 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 114 --------------QGSVNAAFHRDLQPRQGETVVQK------DNVSVFAGN---SATVLDQVLKDAGIDTLIVTGLQTH 170
Cdd:PRK11609   74 ldglpqtwwpdhcvQNSEGAALHPLLNQKAIDAVFHKgenpliDSYSAFFDNghrQKTALDDWLREHGITELIVMGLATD 153


                  ...
gi 2520371918 171 ACV 173
Cdd:PRK11609  154 YCV 156
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 40-202 2.74e-08

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 52.76  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  40 ASLDAAKTAVLVIDFQNEyFDAKAAPGFAGGRMVIPdGVAALRQA---KRVVEFADAHgiRVIHVQHVLPAGAPLFA--- 113
Cdd:PTZ00331    6 ITVSSTNDALIIVDVQND-FCKGGSLAVPDAEEVIP-VINQVRQShhfDLVVATQDWH--PPNHISFASNHGKPKILpdg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 114 -----------QGSVNAAFHRDLQPRQGETVVQK------DNVSVFAGNSA--TVLDQVLKDAGIDTLIVTGLQTHACVA 174
Cdd:PTZ00331   82 ttqglwpphcvQGTKGAQLHKDLVVERIDIIIRKgtnrdvDSYSAFDNDKGskTGLAQILKAHGVRRVFICGLAFDFCVL 161

                         170       180
                  ....*....|....*....|....*...
gi 2520371918 175 GAARDAAAAprGYRVIVSSDASASRDLD 202
Cdd:PTZ00331  162 FTALDAVKL--GFKVVVLEDATRAVDPD 187
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 46-202 5.22e-07

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: 48.80  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  46 KTAVLVIDFQNEYFDAKAAPgFAGGRMVIP--DGVAALRQAKRVVEFADAHGIRVIH--VQHvlpAGAPLFA-------- 113
Cdd:cd01011     1 TDALLVVDVQNDFCPGGALA-VPGGDAIVPliNALLSLFQYDLVVATQDWHPANHASfaSNH---PGQMPFItlppgpqv 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 114 -------QGSVNAAFHRDLQPRQGETVVQK------DNVSVFAGN---SATVLDQVLKDAGIDTLIVTGLQTHACVAGAA 177
Cdd:cd01011    77 lwpdhcvQGTPGAELHPGLPVPDIDLIVRKgtnpdiDSYSAFFDNdrrSSTGLAEYLRERGIDRVDVVGLATDYCVKATA 156

                         170       180
                  ....*....|....*....|....*
gi 2520371918 178 RDAAAAprGYRVIVSSDASASRDLD 202
Cdd:cd01011   157 LDALKA--GFEVRVLEDACRAVDPE 179
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 48-236 1.44e-05

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: 43.74  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918  48 AVLVIDFQneyfdakaaPGFAGGrmvIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFAQgsvnaafHRDLQP 127
Cdd:cd01012     1 ALLLVDVQ---------EKLAPA---IKSFDELINNTVKLAKAAKLLDVPVILTEQYPKGLGPTVPE-------LREVFP 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520371918 128 rqGETVVQKDNVSvFAGNSATVldQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDASASRdldlaggq 207
Cdd:cd01012    62 --DAPVIEKTSFS-CWEDEAFR--KALKATGRKQVVLAGLETHVCVLQTALDLLE--EGYEVFVVADACGSR-------- 126

                         170       180
                  ....*....|....*....|....*....
gi 2520371918 208 ridHRALHDASLAQIEDAFGDVMSTDAIL 236
Cdd:cd01012   127 ---SKEDHELALARMRQAGAVLTTSESVL 152
 
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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