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Conserved domains on  [gi|1189281498|ref|WP_085702014|]
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MULTISPECIES: bifunctional nicotinamidase/pyrazinamidase [Pseudomonas]

Protein Classification

nicotinamidase( domain architecture ID 10099055)

nicotinamidase converts nicotinamide to nicotinic acid (niacin) and ammonia

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 6-202 3.65e-111

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: 316.13  E-value: 3.65e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   6 RTALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAGQFK--QVVISQDWHPAGHASFASSHPGRQPYdlIQLPYGEQTLW 83
Cdd:cd01011     1 TDALLVVDVQNDFCPGGALAVPGGDAIVPLINALLSLFQydLVVATQDWHPANHASFASNHPGQMPF--ITLPPGPQVLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 PDHCIQGSRGAEFHSGLDLPHAQLIIRKGCNPDIDSYSAFLEADRVTTTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:cd01011    79 PDHCVQGTPGAELHPGLPVPDIDLIVRKGTNPDIDSYSAFFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1189281498 164 ARAAGFNTFVVLDACRAIDLNGSRAtAIERMQVAGVGLI 202
Cdd:cd01011   159 ALKAGFEVRVLEDACRAVDPETIER-AIEEMKEAGVVLV 196
 
Name Accession Description Interval E-value
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 6-202 3.65e-111

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: 316.13  E-value: 3.65e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   6 RTALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAGQFK--QVVISQDWHPAGHASFASSHPGRQPYdlIQLPYGEQTLW 83
Cdd:cd01011     1 TDALLVVDVQNDFCPGGALAVPGGDAIVPLINALLSLFQydLVVATQDWHPANHASFASNHPGQMPF--ITLPPGPQVLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 PDHCIQGSRGAEFHSGLDLPHAQLIIRKGCNPDIDSYSAFLEADRVTTTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:cd01011    79 PDHCVQGTPGAELHPGLPVPDIDLIVRKGTNPDIDSYSAFFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1189281498 164 ARAAGFNTFVVLDACRAIDLNGSRAtAIERMQVAGVGLI 202
Cdd:cd01011   159 ALKAGFEVRVLEDACRAVDPETIER-AIEEMKEAGVVLV 196
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 7-207 2.81e-86

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 253.45  E-value: 2.81e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   7 TALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAG--QFKQVVISQDWHPAGHASFASSHPGRQPydliqLPYG-EQTLW 83
Cdd:PTZ00331   13 DALIIVDVQNDFCKGGSLAVPDAEEVIPVINQVRQshHFDLVVATQDWHPPNHISFASNHGKPKI-----LPDGtTQGLW 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 PDHCIQGSRGAEFHSGLDLPHAQLIIRKGCNPDIDSYSAFLEaDRVTTTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:PTZ00331   88 PPHCVQGTKGAQLHKDLVVERIDIIIRKGTNRDVDSYSAFDN-DKGSKTGLAQILKAHGVRRVFICGLAFDFCVLFTALD 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1189281498 164 ARAAGFNTFVVLDACRAIDLNGSRAtAIERMQVAGVGLIQSTEL 207
Cdd:PTZ00331  167 AVKLGFKVVVLEDATRAVDPDAISK-QRAELLEAGVILLTSSDL 209
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 8-202 2.43e-55

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: 173.55  E-value: 2.43e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   8 ALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAGQFKQ----VVISQDWHPAGHASFAsshpgrqpydliqlpygEQTLW 83
Cdd:COG1335     1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAagvpVIHTRDWHPPDGSEFA-----------------EFDLW 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 PDHCIQGSRGAEFHSGLDLPHAQLIIRKGcnpdidSYSAFLEadrvttTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:COG1335    64 PPHCVPGTPGAELVPELAPLPGDPVVDKT------RYSAFYG------TDLDELLRERGIDTLVVAGLATDVCVLSTARD 131

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1189281498 164 ARAAGFNTFVVLDACRAIDLnGSRATAIERMQVAGVGLI 202
Cdd:COG1335   132 ALDLGYEVTVVEDACASRDP-EAHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 7-202 4.54e-33

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 116.73  E-value: 4.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   7 TALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAGQFKQ----VVISQDWHPAGHASFASSHPgrqpydliqlpygeqtl 82
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKagipVIFTRQVPEPDDADFALKDR----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  83 WPDHCIQGSRGAEFHSGLDLPHAQLIIRKGCnpdidsYSAFleadrvTTTGLAGYLKERGIDTVYMVGLALDFCVMFSAL 162
Cdd:pfam00857  64 PSPAFPPGTTGAELVPELAPLPGDLVVDKTR------FSAF------AGTDLDEILRELGIDTLVLAGVATDVCVLSTAR 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1189281498 163 DARAAGFNTFVVLDACRAIDLNGsRATAIERMQVAGVGLI 202
Cdd:pfam00857 132 DALDRGYEVVVVSDACASLSPEA-HDAALERLAQRGAEVT 170
 
Name Accession Description Interval E-value
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 6-202 3.65e-111

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: 316.13  E-value: 3.65e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   6 RTALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAGQFK--QVVISQDWHPAGHASFASSHPGRQPYdlIQLPYGEQTLW 83
Cdd:cd01011     1 TDALLVVDVQNDFCPGGALAVPGGDAIVPLINALLSLFQydLVVATQDWHPANHASFASNHPGQMPF--ITLPPGPQVLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 PDHCIQGSRGAEFHSGLDLPHAQLIIRKGCNPDIDSYSAFLEADRVTTTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:cd01011    79 PDHCVQGTPGAELHPGLPVPDIDLIVRKGTNPDIDSYSAFFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1189281498 164 ARAAGFNTFVVLDACRAIDLNGSRAtAIERMQVAGVGLI 202
Cdd:cd01011   159 ALKAGFEVRVLEDACRAVDPETIER-AIEEMKEAGVVLV 196
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 7-207 2.81e-86

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 253.45  E-value: 2.81e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   7 TALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAG--QFKQVVISQDWHPAGHASFASSHPGRQPydliqLPYG-EQTLW 83
Cdd:PTZ00331   13 DALIIVDVQNDFCKGGSLAVPDAEEVIPVINQVRQshHFDLVVATQDWHPPNHISFASNHGKPKI-----LPDGtTQGLW 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 PDHCIQGSRGAEFHSGLDLPHAQLIIRKGCNPDIDSYSAFLEaDRVTTTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:PTZ00331   88 PPHCVQGTKGAQLHKDLVVERIDIIIRKGTNRDVDSYSAFDN-DKGSKTGLAQILKAHGVRRVFICGLAFDFCVLFTALD 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1189281498 164 ARAAGFNTFVVLDACRAIDLNGSRAtAIERMQVAGVGLIQSTEL 207
Cdd:PTZ00331  167 AVKLGFKVVVLEDATRAVDPDAISK-QRAELLEAGVILLTSSDL 209
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
6-208 1.67e-75

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 226.41  E-value: 1.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   6 RTALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAGQFKQ----VVISQDWHPAGHASFASSHpGRQPYDLIQLPYGEQT 81
Cdd:PRK11609    2 KRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSrgipVIASQDWHPANHGSFASNH-GAEPGTQGELDGLPQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  82 LWPDHCIQGSRGAEFHSGLDLPHAQLIIRKGCNPDIDSYSAFLEADRVTTTGLAGYLKERGIDTVYMVGLALDFCVMFSA 161
Cdd:PRK11609   81 WWPDHCVQNSEGAALHPLLNQKAIDAVFHKGENPLIDSYSAFFDNGHRQKTALDDWLREHGITELIVMGLATDYCVKFTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1189281498 162 LDARAAGFNTFVVLDACRAIDLN-GSRATAIERMQVAGVGLIQSTELL 208
Cdd:PRK11609  161 LDALALGYQVNVITDGCRGVNLQpQDSAHAFMEMSAAGATLYTLADWE 208
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 8-202 2.43e-55

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: 173.55  E-value: 2.43e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   8 ALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAGQFKQ----VVISQDWHPAGHASFAsshpgrqpydliqlpygEQTLW 83
Cdd:COG1335     1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAagvpVIHTRDWHPPDGSEFA-----------------EFDLW 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 PDHCIQGSRGAEFHSGLDLPHAQLIIRKGcnpdidSYSAFLEadrvttTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:COG1335    64 PPHCVPGTPGAELVPELAPLPGDPVVDKT------RYSAFYG------TDLDELLRERGIDTLVVAGLATDVCVLSTARD 131

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1189281498 164 ARAAGFNTFVVLDACRAIDLnGSRATAIERMQVAGVGLI 202
Cdd:COG1335   132 ALDLGYEVTVVEDACASRDP-EAHEAALARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 8-194 7.93e-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: 7.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   8 ALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAGQFKQ----VVISQDWHPAGHASFASshpgrqpydliqlpygeqTLW 83
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAagipVIFTRDWHPPDDPEFAE------------------LLW 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 PDHCIQGSRGAEFHSGLDLPHAQLIIRKGcnpdidSYSAFLEadrvttTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:cd00431    63 PPHCVKGTEGAELVPELAPLPDDLVIEKT------RYSAFYG------TDLDELLRERGIDTLVVCGIATDICVLATARD 130

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1189281498 164 ARAAGFNTFVVLDACRAIDLNGSRAtAIERM 194
Cdd:cd00431   131 ALDLGYRVIVVEDACATRDEEDHEA-ALERL 160
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 7-202 4.54e-33

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 116.73  E-value: 4.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   7 TALLVIDVQNDFIPGGQLAVPEGDLIVPLINRLAGQFKQ----VVISQDWHPAGHASFASSHPgrqpydliqlpygeqtl 82
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKagipVIFTRQVPEPDDADFALKDR----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  83 WPDHCIQGSRGAEFHSGLDLPHAQLIIRKGCnpdidsYSAFleadrvTTTGLAGYLKERGIDTVYMVGLALDFCVMFSAL 162
Cdd:pfam00857  64 PSPAFPPGTTGAELVPELAPLPGDLVVDKTR------FSAF------AGTDLDEILRELGIDTLVLAGVATDVCVLSTAR 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1189281498 163 DARAAGFNTFVVLDACRAIDLNGsRATAIERMQVAGVGLI 202
Cdd:pfam00857 132 DALDRGYEVVVVSDACASLSPEA-HDAALERLAQRGAEVT 170
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 8-183 2.08e-17

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: 75.71  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   8 ALLVIDVQNDFIPGGqLAVPEGDLIVPLINRLAGQFKQ----VVISQdwhpaghasfassHPGRQPYDLiqlpygeqtlw 83
Cdd:cd01014     1 ALLVIDVQNGYFDGG-LPPLNNEAALENIAALIAAARAagipVIHVR-------------HIDDEGGSF----------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 pdhcIQGSRGAEFHSGLDLPHAQLIIRKGCNpdidsySAFLEadrvttTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:cd01014    56 ----APGSEGWEIHPELAPLEGETVIEKTVP------NAFYG------TDLEEWLREAGIDHLVICGAMTEMCVDTTVRS 119

                         170       180
                  ....*....|....*....|
gi 1189281498 164 ARAAGFNTFVVLDACRAIDL 183
Cdd:cd01014   120 AFDLGYDVTVVADACATFDL 139
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
6-178 7.67e-12

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 61.79  E-value: 7.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   6 RTALLVIDVQNDFI-PGGQLAvPEGDLIVPLINRLAGQFKQvvisqdwhpAGHASFASSHPGRQPydliQLPYG-EQTLW 83
Cdd:COG1535    19 RAALLIHDMQNYFLrPYDPDE-PPIRELVANIARLRDACRA---------AGIPVVYTAQPGDQT----PEDRGlLNDFW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  84 PDHCIQGSRGAEFHSGLDLPHAQLIIRKgcnpdiDSYSAFLEadrvttTGLAGYLKERGIDTVYMVGLALDFCVMFSALD 163
Cdd:COG1535    85 GPGLTAGPEGQEIVDELAPAPGDTVLTK------WRYSAFQR------TDLEERLRELGRDQLIITGVYAHIGCLATAVD 152

                         170
                  ....*....|....*
gi 1189281498 164 ARAAGFNTFVVLDAC 178
Cdd:COG1535   153 AFMRDIQPFVVADAV 167
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 138-208 1.35e-09

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: 54.52  E-value: 1.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189281498 138 LKERGIDTVYMVGLALDFCVMFSALDARAAGFNTFVVLDACRAIDlNGSRATAIERMQVAGVGLIQSTELL 208
Cdd:cd01012    83 LKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRS-KEDHELALARMRQAGAVLTTSESVL 152
PLN02621 PLN02621
nicotinamidase
 1-189 7.18e-07

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 47.85  E-value: 7.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   1 MPISPRTALLVIDVQNDFipgGQLAVPegdlIVPLINRLAGQFKQvvisqdwhpAGHASFASSHPGRQPYDLIQLpyGEq 80
Cdd:PLN02621   15 DPDPKQAALLVIDMQNYF---SSMAEP----ILPALLTTIDLCRR---------ASIPVFFTRHSHKSPSDYGML--GE- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  81 tLWP-DHCIQGSRGAEFHSGLD-LPHAQLIIRKgcnpdiDSYSAFleadrvTTTGLAGYLKERGIDTVYMVGLALDFCVM 158
Cdd:PLN02621   76 -WWDgDLILDGTTEAELMPEIGrVTGPDEVVEK------STYSAF------YNTRLEERLRKIGVKEVIVTGVMTNLCCE 142

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1189281498 159 FSALDARAAGFNTFVVLDACRAIDLNGSRAT 189
Cdd:PLN02621  143 TTAREAFVRGFRVFFSTDATATANEELHEAT 173
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 132-190 8.77e-07

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: 47.40  E-value: 8.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1189281498 132 TGLAGYLKERGIDTVYMVGLALDFCVMFSALDARAAGFNTFVVLDACraidlnGSRATA 190
Cdd:cd01015   103 TSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECV------GDRAPA 155
PLN02743 PLN02743
nicotinamidase
 6-183 2.64e-05

nicotinamidase


Pssm-ID: 215396  Cd Length: 239  Bit Score: 43.57  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498   6 RTALLVIDVQNDF--IPGGQLAVPEGD-LIVPLIN---RLAGQFKqvviSQDWhPAghASFASSHPGRQPydliQLPYge 79
Cdd:PLN02743   27 RTGLVLVDEVNGFctVGAGNLAPREPDkQISKMVDesaRLAREFC----ERKW-PV--LAFLDSHHPDKP----EHPY-- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189281498  80 qtlwPDHCIQGSRGAEFHSGL----DLPHAqLIIRKGCnpdIDSYSAFLEADRVTTtgLAGYLKERGIDTVYMVGLALDF 155
Cdd:PLN02743   94 ----PPHCIVGTGEENLVPALqwleNDPNV-TLRRKDC---IDGFVGAIEKDGSNV--FVDWVNNNKIKVILVVGICTDI 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1189281498 156 CVM---FSALDARAAGF-----NTFVVLDACRAIDL 183
Cdd:PLN02743  164 CVLdfvASALSARNHGIlppleDVVVYSRGCATYDL 199
 
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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