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Conserved domains on  [gi|896491233|ref|WP_049400917|]
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MULTISPECIES: cysteine hydrolase family protein [Stenotrophomonas]

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

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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 7.73e-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: 117.31  E-value: 7.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  48 AVLVIDFQNEYFDGsaapgfagGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA----------QGSV 117
Cdd:COG1335    1 ALLVIDVQNDFVPP--------GALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 118 NAAFHRDLQPRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDATA 197
Cdd:COG1335   73 GAELVPELAPLPGDPVVDKTRYSAFYGTD---LDELLRERGIDTLVVAGLATDVCVLSTARDALD--LGYEVTVVEDACA 147

                        170       180       190
                 ....*....|....*....|....*....|...
gi 896491233 198 SRDLDlaggqrighraLHDASLAQIEDTFGDVM 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 7.73e-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: 117.31  E-value: 7.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  48 AVLVIDFQNEYFDGsaapgfagGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA----------QGSV 117
Cdd:COG1335    1 ALLVIDVQNDFVPP--------GALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 118 NAAFHRDLQPRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDATA 197
Cdd:COG1335   73 GAELVPELAPLPGDPVVDKTRYSAFYGTD---LDELLRERGIDTLVVAGLATDVCVLSTARDALD--LGYEVTVVEDACA 147

                        170       180       190
                 ....*....|....*....|....*....|...
gi 896491233 198 SRDLDlaggqrighraLHDASLAQIEDTFGDVM 230
Cdd:COG1335  148 SRDPE-----------AHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 47-233 1.51e-30

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 111.34  E-value: 1.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233   47 TAVLVIDFQNEYFDGSAAPgfaggrmvIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGA----------PLFAQGS 116
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPK--------VEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDadfalkdrpsPAFPPGT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  117 VNAAFHRDLQPRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDAT 196
Cdd:pfam00857  73 TGAELVPELAPLPGDLVVDKTRFSAFAGTD---LDEILRELGIDTLVLAGVATDVCVLSTARDALD--RGYEVVVVSDAC 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 896491233  197 ASRDLDlaggqrighraLHDASLAQIEDTFGDVMATD 233
Cdd:pfam00857 148 ASLSPE-----------AHDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 48-223 7.85e-30

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: 109.28  E-value: 7.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  48 AVLVIDFQNEYFDGSAAPgfaggrmvIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA---------QGSVN 118
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLL--------LPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAellwpphcvKGTEG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 119 AAFHRDLQPRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDATAS 198
Cdd:cd00431   73 AELVPELAPLPDDLVIEKTRYSAFYGTD---LDELLRERGIDTLVVCGIATDICVLATARDALD--LGYRVIVVEDACAT 147

                        170       180
                 ....*....|....*....|....*
gi 896491233 199 RDLDlaggqrighraLHDASLAQIE 223
Cdd:cd00431  148 RDEE-----------DHEAALERLA 161
PLN02621 PLN02621
nicotinamidase
 43-220 6.62e-13

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 65.19  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  43 DAAKTAVLVIDFQNeYFDGSAAPgfaggrmVIPdgvaalrQAKRVVEFADAHGIRVIHVQHV--LPAGAPLFAQ------ 114
Cdd:PLN02621  17 DPKQAALLVIDMQN-YFSSMAEP-------ILP-------ALLTTIDLCRRASIPVFFTRHShkSPSDYGMLGEwwdgdl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 115 ---GSVNAAFHRDLQ-PRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVI 190
Cdd:PLN02621  82 ildGTTEAELMPEIGrVTGPDEVVEKSTYSAFYNTR---LEERLRKIGVKEVIVTGVMTNLCCETTAREAFV--RGFRVF 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 896491233 191 VSSDATASRDLDlaggqrighraLHDASLA 220
Cdd:PLN02621 157 FSTDATATANEE-----------LHEATLK 175
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 48-230 7.73e-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: 117.31  E-value: 7.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  48 AVLVIDFQNEYFDGsaapgfagGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA----------QGSV 117
Cdd:COG1335    1 ALLVIDVQNDFVPP--------GALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 118 NAAFHRDLQPRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDATA 197
Cdd:COG1335   73 GAELVPELAPLPGDPVVDKTRYSAFYGTD---LDELLRERGIDTLVVAGLATDVCVLSTARDALD--LGYEVTVVEDACA 147

                        170       180       190
                 ....*....|....*....|....*....|...
gi 896491233 198 SRDLDlaggqrighraLHDASLAQIEDTFGDVM 230
Cdd:COG1335  148 SRDPE-----------AHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 47-233 1.51e-30

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 111.34  E-value: 1.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233   47 TAVLVIDFQNEYFDGSAAPgfaggrmvIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGA----------PLFAQGS 116
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPK--------VEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDadfalkdrpsPAFPPGT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  117 VNAAFHRDLQPRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDAT 196
Cdd:pfam00857  73 TGAELVPELAPLPGDLVVDKTRFSAFAGTD---LDEILRELGIDTLVLAGVATDVCVLSTARDALD--RGYEVVVVSDAC 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 896491233  197 ASRDLDlaggqrighraLHDASLAQIEDTFGDVMATD 233
Cdd:pfam00857 148 ASLSPE-----------AHDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 48-223 7.85e-30

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: 109.28  E-value: 7.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  48 AVLVIDFQNEYFDGSAAPgfaggrmvIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA---------QGSVN 118
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLL--------LPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAellwpphcvKGTEG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 119 AAFHRDLQPRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDATAS 198
Cdd:cd00431   73 AELVPELAPLPDDLVIEKTRYSAFYGTD---LDELLRERGIDTLVVCGIATDICVLATARDALD--LGYRVIVVEDACAT 147

                        170       180
                 ....*....|....*....|....*
gi 896491233 199 RDLDlaggqrighraLHDASLAQIE 223
Cdd:cd00431  148 RDEE-----------DHEAALERLA 161
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 48-206 8.97e-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: 8.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  48 AVLVIDFQNEYFDGSAAPgfaggrmviPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPlFAQGSVNAAFHRDLQP 127
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPP---------LNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGS-FAPGSEGWEIHPELAP 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896491233 128 RKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDATASRDLDLAGG 206
Cdd:cd01014   71 LEGETVIEKTVPNAFYGTD---LEEWLREAGIDHLVICGAMTEMCVDTTVRSAFD--LGYDVTVVADACATFDLPDHGG 144
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 48-237 3.64e-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: 81.68  E-value: 3.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  48 AVLVIDFQNEYFDGSA--APGFAggrmvipdgvAALRQAKRVVEFADAHGIRVIHVQHVLPAGAP-------------LF 112
Cdd:cd01015    1 ALLVIDLVEGYTQPGSylAPGIA----------AALENVQRLLAAARAAGVPVIHTTVVYDPDGAdgglwarkvpamsDL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 113 AQGSVNAAFHRDLQPRKGETVVQKDNVSVFAGDSAAVLdqvLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVS 192
Cdd:cd01015   71 VEGSPLAAICDELAPQEDEMVLVKKYASAFFGTSLAAT---LTARGVDTLIVAGCSTSGCIRATAVDAMQ--HGFRPIVV 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 896491233 193 SDATASRdldlaggqrigHRALHDASLAQIEDTFGDVMATDAILA 237
Cdd:cd01015  146 RECVGDR-----------APAPHEANLFDIDNKYGDVVSTDDALA 179
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
28-237 5.49e-19

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 81.82  E-value: 5.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  28 PTIRHMAGAPVVASLDAAKTAVLVIDFQNeYFDGSAAPGFAGGRMVIPDgVAALRqakrvvEFADAHGIRVIHVQHvlPA 107
Cdd:COG1535    1 PTAADLPANKVSWTLDPARAALLIHDMQN-YFLRPYDPDEPPIRELVAN-IARLR------DACRAAGIPVVYTAQ--PG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 108 GAPLF-------------AQGSVNAAFHRDLQPRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVA 174
Cdd:COG1535   71 DQTPEdrgllndfwgpglTAGPEGQEIVDELAPAPGDTVLTKWRYSAFQRTD---LEERLRELGRDQLIITGVYAHIGCL 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896491233 175 GAARDAAAapRGYRVIVSSDATASRDldlaggqrighRALHDASLAQIEDTFGDVMATDAILA 237
Cdd:COG1535  148 ATAVDAFM--RDIQPFVVADAVADFS-----------REEHRMALEYVAGRCGVVVTTDEVLE 197
PLN02621 PLN02621
nicotinamidase
 43-220 6.62e-13

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 65.19  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  43 DAAKTAVLVIDFQNeYFDGSAAPgfaggrmVIPdgvaalrQAKRVVEFADAHGIRVIHVQHV--LPAGAPLFAQ------ 114
Cdd:PLN02621  17 DPKQAALLVIDMQN-YFSSMAEP-------ILP-------ALLTTIDLCRRASIPVFFTRHShkSPSDYGMLGEwwdgdl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 115 ---GSVNAAFHRDLQ-PRKGETVVQKDNVSVFAGDSaavLDQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVI 190
Cdd:PLN02621  82 ildGTTEAELMPEIGrVTGPDEVVEKSTYSAFYNTR---LEERLRKIGVKEVIVTGVMTNLCCETTAREAFV--RGFRVF 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 896491233 191 VSSDATASRDLDlaggqrighraLHDASLA 220
Cdd:PLN02621 157 FSTDATATANEE-----------LHEATLK 175
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 40-202 1.19e-08

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 53.53  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  40 ASLDAAKTAVLVIDFQNEYFDGSAAPgFAGGRMVIPdGVAALRQA---KRVVEFADAHgiRVIHVQHVLPAGAPLFA--- 113
Cdd:PTZ00331   6 ITVSSTNDALIIVDVQNDFCKGGSLA-VPDAEEVIP-VINQVRQShhfDLVVATQDWH--PPNHISFASNHGKPKILpdg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 114 -----------QGSVNAAFHRDLQPRKGETVVQK------DNVSVFAGDSAAV--LDQVLKDAGIDTLIVTGLQTHACVA 174
Cdd:PTZ00331  82 ttqglwpphcvQGTKGAQLHKDLVVERIDIIIRKgtnrdvDSYSAFDNDKGSKtgLAQILKAHGVRRVFICGLAFDFCVL 161

                        170       180
                 ....*....|....*....|....*...
gi 896491233 175 GAARDAAAAprGYRVIVSSDATASRDLD 202
Cdd:PTZ00331 162 FTALDAVKL--GFKVVVLEDATRAVDPD 187
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
46-173 1.75e-08

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 53.07  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  46 KTAVLVIDFQNEYFdgsaapgfAGGRMVIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFA------------ 113
Cdd:PRK11609   2 KRALLLVDLQNDFC--------AGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQDWHPANHGSFAsnhgaepgtqge 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 114 --------------QGSVNAAFHRDLQPRKGETVVQK------DNVSVFAGD---SAAVLDQVLKDAGIDTLIVTGLQTH 170
Cdd:PRK11609  74 ldglpqtwwpdhcvQNSEGAALHPLLNQKAIDAVFHKgenpliDSYSAFFDNghrQKTALDDWLREHGITELIVMGLATD 153


                 ...
gi 896491233 171 ACV 173
Cdd:PRK11609 154 YCV 156
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 46-202 2.44e-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: 49.57  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  46 KTAVLVIDFQNEYFDGSAAPgFAGGRMVIP--DGVAALRQAKRVVEFADAHGIRVIH--VQHvlpAGAPLFA-------- 113
Cdd:cd01011    1 TDALLVVDVQNDFCPGGALA-VPGGDAIVPliNALLSLFQYDLVVATQDWHPANHASfaSNH---PGQMPFItlppgpqv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 114 -------QGSVNAAFHRDLQPRKGETVVQK------DNVSVFAGDSAAV---LDQVLKDAGIDTLIVTGLQTHACVAGAA 177
Cdd:cd01011   77 lwpdhcvQGTPGAELHPGLPVPDIDLIVRKgtnpdiDSYSAFFDNDRRSstgLAEYLRERGIDRVDVVGLATDYCVKATA 156

                        170       180
                 ....*....|....*....|....*
gi 896491233 178 RDAAAAprGYRVIVSSDATASRDLD 202
Cdd:cd01011  157 LDALKA--GFEVRVLEDACRAVDPE 179
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 48-204 1.49e-04

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: 41.04  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233  48 AVLVIDFQneyfdgsaaPGFAGGrmvIPDGVAALRQAKRVVEFADAHGIRVIHVQHVLPAGAPLFAQgsvnaafHRDLQP 127
Cdd:cd01012    1 ALLLVDVQ---------EKLAPA---IKSFDELINNTVKLAKAAKLLDVPVILTEQYPKGLGPTVPE-------LREVFP 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896491233 128 rkGETVVQKDNVSvFAGDSAAVldQVLKDAGIDTLIVTGLQTHACVAGAARDAAAapRGYRVIVSSDATASR---DLDLA 204
Cdd:cd01012   62 --DAPVIEKTSFS-CWEDEAFR--KALKATGRKQVVLAGLETHVCVLQTALDLLE--EGYEVFVVADACGSRskeDHELA 134
 
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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