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Conserved domains on  [gi|15237258|ref|NP_197714|]
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nicotinamidase 2 [Arabidopsis thaliana]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 10791423)

cysteine hydrolase family protein, such as isochorismatase and nicotinamidase, catalyzes the hydrolysis of a chemical bond using an active site cysteinyl residue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02621 PLN02621
nicotinamidase
 1-198 5.28e-149

nicotinamidase


:

Pssm-ID: 178229  Cd Length: 197  Bit Score: 411.10  E-value: 5.28e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258    1 MASSSSRTYETRKREPNPKIAALLVIDMQNHFYSMAEPILQNALTTIDICRRASIPVFFTRHNHKSPTDHGMLGEWWNGD 80
Cdd:PLN02621   1 MAASSYKKYETRKRDPDPKQAALLVIDMQNYFSSMAEPILPALLTTIDLCRRASIPVFFTRHSHKSPSDYGMLGEWWDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258   81 LILDGTTDSEIIPEINRqVTGPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFST 160
Cdd:PLN02621  81 LILDGTTEAELMPEIGR-VTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFST 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15237258  161 DATATVNEELHEATLMNLAYGFAYLVDCDRLRRGLLSS 198
Cdd:PLN02621 160 DATATANEELHEATLKNLAYGFAYLVDCDRLEAGLLKK 197
 
Name Accession Description Interval E-value
PLN02621 PLN02621
nicotinamidase
 1-198 5.28e-149

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 411.10  E-value: 5.28e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258    1 MASSSSRTYETRKREPNPKIAALLVIDMQNHFYSMAEPILQNALTTIDICRRASIPVFFTRHNHKSPTDHGMLGEWWNGD 80
Cdd:PLN02621   1 MAASSYKKYETRKRDPDPKQAALLVIDMQNYFSSMAEPILPALLTTIDLCRRASIPVFFTRHSHKSPSDYGMLGEWWDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258   81 LILDGTTDSEIIPEINRqVTGPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFST 160
Cdd:PLN02621  81 LILDGTTEAELMPEIGR-VTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFST 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15237258  161 DATATVNEELHEATLMNLAYGFAYLVDCDRLRRGLLSS 198
Cdd:PLN02621 160 DATATANEELHEATLKNLAYGFAYLVDCDRLEAGLLKK 197
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 22-179 6.16e-52

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: 164.36  E-value: 6.16e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  22 ALLVIDMQNHF-------YSMAEPILQNALTTIDICRRASIPVFFTRHNHksPTDHGMLGEWWNGDLILDGTTDSEIIPE 94
Cdd:cd00431   1 ALLVVDMQNDFvpgggllLPGADELVPNINRLLAAARAAGIPVIFTRDWH--PPDDPEFAELLWPPHCVKGTEGAELVPE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  95 InrQVTGPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATVNEELHEAT 174
Cdd:cd00431  79 L--APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAA 156


                ....*
gi 15237258 175 LMNLA 179
Cdd:cd00431 157 LERLA 161
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 22-183 1.19e-51

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: 163.54  E-value: 1.19e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  22 ALLVIDMQNHF-------YSMAEPILQNALTTIDICRRASIPVFFTRHNHKSPTDHGMLGEWWNGDLILdGTTDSEIIPE 94
Cdd:COG1335   1 ALLVIDVQNDFvppgalaVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVP-GTPGAELVPE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  95 INRQvtGPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATVNEELHEAT 174
Cdd:COG1335  80 LAPL--PGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAA 157


                ....*....
gi 15237258 175 LMNLAYGFA 183
Cdd:COG1335 158 LARLRAAGA 166
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 21-187 2.27e-46

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 150.63  E-value: 2.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258    21 AALLVIDMQNHFYSMAEP-------ILQNALTTIDICRRASIPVFFTRHNHKSPTDHGMLGEWWNGDLILdGTTDSEIIP 93
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPkvegiaaILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPP-GTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258    94 EINRQVtgPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATVNEELHEA 173
Cdd:pfam00857  80 ELAPLP--GDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157

                         170
                  ....*....|....
gi 15237258   174 TLMNLAYGFAYLVD 187
Cdd:pfam00857 158 ALERLAQRGAEVTT 171
 
Name Accession Description Interval E-value
PLN02621 PLN02621
nicotinamidase
 1-198 5.28e-149

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 411.10  E-value: 5.28e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258    1 MASSSSRTYETRKREPNPKIAALLVIDMQNHFYSMAEPILQNALTTIDICRRASIPVFFTRHNHKSPTDHGMLGEWWNGD 80
Cdd:PLN02621   1 MAASSYKKYETRKRDPDPKQAALLVIDMQNYFSSMAEPILPALLTTIDLCRRASIPVFFTRHSHKSPSDYGMLGEWWDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258   81 LILDGTTDSEIIPEINRqVTGPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFST 160
Cdd:PLN02621  81 LILDGTTEAELMPEIGR-VTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFST 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15237258  161 DATATVNEELHEATLMNLAYGFAYLVDCDRLRRGLLSS 198
Cdd:PLN02621 160 DATATANEELHEATLKNLAYGFAYLVDCDRLEAGLLKK 197
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 22-179 6.16e-52

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: 164.36  E-value: 6.16e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  22 ALLVIDMQNHF-------YSMAEPILQNALTTIDICRRASIPVFFTRHNHksPTDHGMLGEWWNGDLILDGTTDSEIIPE 94
Cdd:cd00431   1 ALLVVDMQNDFvpgggllLPGADELVPNINRLLAAARAAGIPVIFTRDWH--PPDDPEFAELLWPPHCVKGTEGAELVPE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  95 InrQVTGPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATVNEELHEAT 174
Cdd:cd00431  79 L--APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAA 156


                ....*
gi 15237258 175 LMNLA 179
Cdd:cd00431 157 LERLA 161
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 22-183 1.19e-51

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: 163.54  E-value: 1.19e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  22 ALLVIDMQNHF-------YSMAEPILQNALTTIDICRRASIPVFFTRHNHKSPTDHGMLGEWWNGDLILdGTTDSEIIPE 94
Cdd:COG1335   1 ALLVIDVQNDFvppgalaVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVP-GTPGAELVPE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  95 INRQvtGPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATVNEELHEAT 174
Cdd:COG1335  80 LAPL--PGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAA 157


                ....*....
gi 15237258 175 LMNLAYGFA 183
Cdd:COG1335 158 LARLRAAGA 166
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
15-198 2.87e-51

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 163.87  E-value: 2.87e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  15 EPNPKIAALLVIDMQNHF---YSMAEP----ILQNALTTIDICRRASIPVFFTRHNHK-SPTDHGMLGEWWnGDLILDGT 86
Cdd:COG1535  14 TLDPARAALLIHDMQNYFlrpYDPDEPpireLVANIARLRDACRAAGIPVVYTAQPGDqTPEDRGLLNDFW-GPGLTAGP 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  87 TDSEIIPEINRQvtgPDEIV-EKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATAT 165
Cdd:COG1535  93 EGQEIVDELAPA---PGDTVlTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVAD 169

                       170       180       190
                ....*....|....*....|....*....|...
gi 15237258 166 VNEELHEATLMNLAYGFAYLVDCDRLRRGLLSS 198
Cdd:COG1535 170 FSREEHRMALEYVAGRCGVVVTTDEVLEALRAA 202
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 21-187 2.27e-46

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 150.63  E-value: 2.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258    21 AALLVIDMQNHFYSMAEP-------ILQNALTTIDICRRASIPVFFTRHNHKSPTDHGMLGEWWNGDLILdGTTDSEIIP 93
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPkvegiaaILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPP-GTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258    94 EINRQVtgPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATVNEELHEA 173
Cdd:pfam00857  80 ELAPLP--GDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157

                         170
                  ....*....|....
gi 15237258   174 TLMNLAYGFAYLVD 187
Cdd:pfam00857 158 ALERLAQRGAEVTT 171
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 22-175 3.95e-33

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: 116.15  E-value: 3.95e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  22 ALLVIDMQNHFYSMAEPILQN--ALTTI----DICRRASIPVFFTRHNHKSPtdhgmlgewwngDLILDGTTDSEIIPEI 95
Cdd:cd01014   1 ALLVIDVQNGYFDGGLPPLNNeaALENIaaliAAARAAGIPVIHVRHIDDEG------------GSFAPGSEGWEIHPEL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  96 NRQvtGPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATVNEELHEATL 175
Cdd:cd01014  69 APL--EGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVL 146
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 16-175 1.79e-24

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: 95.10  E-value: 1.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  16 PNPKIAALLVIDMQNHFY----SMAEPI---LQNALTTIDICRRASIPVFFT-RHNHKSPTDHGMLGEWWnGDLILDGTT 87
Cdd:cd01013  25 IDPKRAVLLVHDMQRYFLdfydESAEPVpqlIANIARLRDWCRQAGIPVVYTaQPGNQTPEQRALLNDFW-GPGLTASPE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  88 DSEIIPEINRQvtgPDEIV-EKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATV 166
Cdd:cd01013 104 ETKIVTELAPQ---PDDTVlTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADF 180


                ....*....
gi 15237258 167 NEELHEATL 175
Cdd:cd01013 181 SLEEHRMAL 189
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 22-189 2.31e-20

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: 83.61  E-value: 2.31e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  22 ALLVIDMQNHFYSMAEP-------ILQNALTTIDICRRASIPVFFTRHNHKSPT-DHGMlgeWWNG----DLILDGTTDS 89
Cdd:cd01015   1 ALLVIDLVEGYTQPGSYlapgiaaALENVQRLLAAARAAGVPVIHTTVVYDPDGaDGGL---WARKvpamSDLVEGSPLA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  90 EIIPEINRQvtgPDEIV-EKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATVNE 168
Cdd:cd01015  78 AICDELAPQ---EDEMVlVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAP 154

                       170       180
                ....*....|....*....|.
gi 15237258 169 ELHEATLMNLAYGFAYLVDCD 189
Cdd:cd01015 155 APHEANLFDIDNKYGDVVSTD 175
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 22-179 6.01e-17

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: 74.17  E-value: 6.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  22 ALLVIDMQNHFYS-MAEP--ILQNALTTIDICRRASIPVFFTRHNHKSptdhgmlgewwNGDlildgttdseIIPEInRQ 98
Cdd:cd01012   1 ALLLVDVQEKLAPaIKSFdeLINNTVKLAKAAKLLDVPVILTEQYPKG-----------LGP----------TVPEL-RE 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  99 VTGPDEIVEKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRVFFSTDATATVNEELHEATLMNL 178
Cdd:cd01012  59 VFPDAPVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARM 138


                .
gi 15237258 179 A 179
Cdd:cd01012 139 R 139
PRK11440 PRK11440
putative hydrolase; Provisional
 17-178 5.61e-15

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 69.76  E-value: 5.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258   17 NPKIAALLVIDMQNHF-------YSmAEPILQNALTTIDICRRASIPVFFTR--------HNHKSPTD-----HGMLGEW 76
Cdd:PRK11440   5 NAKTTALVVIDLQEGIlpfaggpHT-ADEVVARAARLAAKFRASGSPVVLVRvgwsadyaEALKQPVDapspaKVLPENW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258   77 WNGDLILdGTTDSEIipeinrQVTgpdeiveKSTYSAFNNTHLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVKGFRV 156
Cdd:PRK11440  84 WQHPAAL-GKTDSDI------EVT-------KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNL 149

                        170       180
                 ....*....|....*....|..
gi 15237258  157 FFSTDATATVNEELHEATLMNL 178
Cdd:PRK11440 150 VIAEDACSAASAEQHQNSMNHI 171
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 21-169 1.06e-14

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 69.33  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258   21 AALLVIDMQNHFYSMAEPILQNALTTIDICR--RASIP---VFFTR--H--NHKS-PTDHGMLGEWWNGDLIL------- 83
Cdd:PTZ00331  13 DALIIVDVQNDFCKGGSLAVPDAEEVIPVINqvRQSHHfdlVVATQdwHppNHISfASNHGKPKILPDGTTQGlwpphcv 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258   84 DGTTDSEIIPEInrQVTGPDEIVEKST------YSAFNN-----THLQEKLDKIGVKEVIVIGVMTNLCCETTAREAFVK 152
Cdd:PTZ00331  93 QGTKGAQLHKDL--VVERIDIIIRKGTnrdvdsYSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTALDAVKL 170

                        170
                 ....*....|....*..
gi 15237258  153 GFRVFFSTDATATVNEE 169
Cdd:PTZ00331 171 GFKVVVLEDATRAVDPD 187
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 22-179 7.00e-14

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: 66.90  E-value: 7.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  22 ALLVIDMQNHF-----------YSMAEPIlqNALttIDICRRAsiPVFFTR----HNHKS-----------PTDHGMLGE 75
Cdd:cd01011   3 ALLVVDVQNDFcpggalavpggDAIVPLI--NAL--LSLFQYD--LVVATQdwhpANHASfasnhpgqmpfITLPPGPQV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258  76 WWNgDLILDGTTDSEIIPEINrqVTGPDEIVEKST------YSAFN------NTHLQEKLDKIGVKEVIVIGVMTNLCCE 143
Cdd:cd01011  77 LWP-DHCVQGTPGAELHPGLP--VPDIDLIVRKGTnpdidsYSAFFdndrrsSTGLAEYLRERGIDRVDVVGLATDYCVK 153

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15237258 144 TTAREAFVKGFRVFFSTDATATVNEELHEATLMNLA 179
Cdd:cd01011 154 ATALDALKAGFEVRVLEDACRAVDPETIERAIEEMK 189
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
21-179 6.37e-10

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 56.15  E-value: 6.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258   21 AALLVIDMQNHF-------YSMAEPILQNALTTIDICRRASIPVFFTRHNHksPTDH-----------GMLGE------- 75
Cdd:PRK11609   3 RALLLVDLQNDFcaggalaVPEGDSTIDVANRLIDWCQSRGIPVIASQDWH--PANHgsfasnhgaepGTQGEldglpqt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237258   76 WWNgDLILDGTTDSEIIPEINRQVTgpDEIVEKST------YSAF------NNTHLQEKLDKIGVKEVIVIGVMTNLCCE 143
Cdd:PRK11609  81 WWP-DHCVQNSEGAALHPLLNQKAI--DAVFHKGEnplidsYSAFfdnghrQKTALDDWLREHGITELIVMGLATDYCVK 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15237258  144 TTAREAFVKGFRVFFSTDATATVN----------EEL--HEATLMNLA 179
Cdd:PRK11609 158 FTVLDALALGYQVNVITDGCRGVNlqpqdsahafMEMsaAGATLYTLA 205
 
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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