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Conserved domains on  [gi|527037786|ref|WP_020884439|]
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MULTISPECIES: bifunctional nicotinamidase/pyrazinamidase [Enterobacter]

Protein Classification

nicotinamidase( domain architecture ID 10793596)

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
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
2-213 6.39e-159

bifunctional nicotinamidase/pyrazinamidase;


:

Pssm-ID: 183228  Cd Length: 212  Bit Score: 437.50  E-value: 6.39e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   2 TQRALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQDWHPADHGSFASQHGVEPFTQGELDGLAQT 81
Cdd:PRK11609   1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQDWHPANHGSFASNHGAEPGTQGELDGLPQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  82 FWPDHCVQQTEGAQLHPLLNQKAIDAVFHKGENPSIDSYSAFFDNGHRQKTALDGWLRHHEITELIVLGLATDYCVKFTV 161
Cdd:PRK11609  81 WWPDHCVQNSEGAALHPLLNQKAIDAVFHKGENPLIDSYSAFFDNGHRQKTALDDWLREHGITELIVMGLATDYCVKFTV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 527037786 162 LDALQLGYTVSVITDGCRGVNIQPQDSAQAFMDMAAEGATLYTLEDWLETHA 213
Cdd:PRK11609 161 LDALALGYQVNVITDGCRGVNLQPQDSAHAFMEMSAAGATLYTLADWEETQG 212
 
Name Accession Description Interval E-value
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
2-213 6.39e-159

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 437.50  E-value: 6.39e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   2 TQRALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQDWHPADHGSFASQHGVEPFTQGELDGLAQT 81
Cdd:PRK11609   1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQDWHPANHGSFASNHGAEPGTQGELDGLPQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  82 FWPDHCVQQTEGAQLHPLLNQKAIDAVFHKGENPSIDSYSAFFDNGHRQKTALDGWLRHHEITELIVLGLATDYCVKFTV 161
Cdd:PRK11609  81 WWPDHCVQNSEGAALHPLLNQKAIDAVFHKGENPLIDSYSAFFDNGHRQKTALDDWLREHGITELIVMGLATDYCVKFTV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 527037786 162 LDALQLGYTVSVITDGCRGVNIQPQDSAQAFMDMAAEGATLYTLEDWLETHA 213
Cdd:PRK11609 161 LDALALGYQVNVITDGCRGVNLQPQDSAHAFMEMSAAGATLYTLADWEETQG 212
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 4-202 4.76e-93

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: 270.29  E-value: 4.76e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   4 RALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCktRGEAVVASQDWHPADHGSFASQHGVEPFTqGELDGLAQTFW 83
Cdd:cd01011    2 DALLVVDVQNDFCPGGALAVPGGDAIVPLINALLSLF--QYDLVVATQDWHPANHASFASNHPGQMPF-ITLPPGPQVLW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  84 PDHCVQQTEGAQLHPLLNQKAIDAVFHKGENPSIDSYSAFFDNGHRQKTALDGWLRHHEITELIVLGLATDYCVKFTVLD 163
Cdd:cd01011   79 PDHCVQGTPGAELHPGLPVPDIDLIVRKGTNPDIDSYSAFFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 527037786 164 ALQLGYTVSVITDGCRGVNiqPQDSAQAFMDMAAEGATL 202
Cdd:cd01011  159 ALKAGFEVRVLEDACRAVD--PETIERAIEEMKEAGVVL 195
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 5-202 1.91e-58

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: 181.64  E-value: 1.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   5 ALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQDWHPADHGSFASQHGvepftqgeldglaqtfWP 84
Cdd:COG1335    1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDL----------------WP 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  85 DHCVQQTEGAQLHPLLNQKAIDAVFHKGenpsidSYSAFFDnghrqkTALDGWLRHHEITELIVLGLATDYCVKFTVLDA 164
Cdd:COG1335   65 PHCVPGTPGAELVPELAPLPGDPVVDKT------RYSAFYG------TDLDELLRERGIDTLVVAGLATDVCVLSTARDA 132

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 527037786 165 LQLGYTVSVITDGCRGVNiqPQDSAQAFMDMAAEGATL 202
Cdd:COG1335  133 LDLGYEVTVVEDACASRD--PEAHEAALARLRAAGATV 168
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 5-206 5.96e-35

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 121.74  E-value: 5.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786    5 ALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQDWHPADHGSFASQHgvepftqgeldglaqtFWP 84
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKD----------------RPS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   85 DHCVQQTEGAQLHPLLNQKAIDAVFHKgenpsiDSYSAFFDnghrqkTALDGWLRHHEITELIVLGLATDYCVKFTVLDA 164
Cdd:pfam00857  66 PAFPPGTTGAELVPELAPLPGDLVVDK------TRFSAFAG------TDLDEILRELGIDTLVLAGVATDVCVLSTARDA 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 527037786  165 LQLGYTVSVITDGCRGVNiqPQDSAQAFMDMAAEGATLYTLE 206
Cdd:pfam00857 134 LDRGYEVVVVSDACASLS--PEAHDAALERLAQRGAEVTTTE 173
 
Name Accession Description Interval E-value
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
2-213 6.39e-159

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 437.50  E-value: 6.39e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   2 TQRALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQDWHPADHGSFASQHGVEPFTQGELDGLAQT 81
Cdd:PRK11609   1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQDWHPANHGSFASNHGAEPGTQGELDGLPQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  82 FWPDHCVQQTEGAQLHPLLNQKAIDAVFHKGENPSIDSYSAFFDNGHRQKTALDGWLRHHEITELIVLGLATDYCVKFTV 161
Cdd:PRK11609  81 WWPDHCVQNSEGAALHPLLNQKAIDAVFHKGENPLIDSYSAFFDNGHRQKTALDDWLREHGITELIVMGLATDYCVKFTV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 527037786 162 LDALQLGYTVSVITDGCRGVNIQPQDSAQAFMDMAAEGATLYTLEDWLETHA 213
Cdd:PRK11609 161 LDALALGYQVNVITDGCRGVNLQPQDSAHAFMEMSAAGATLYTLADWEETQG 212
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 4-202 4.76e-93

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: 270.29  E-value: 4.76e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   4 RALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCktRGEAVVASQDWHPADHGSFASQHGVEPFTqGELDGLAQTFW 83
Cdd:cd01011    2 DALLVVDVQNDFCPGGALAVPGGDAIVPLINALLSLF--QYDLVVATQDWHPANHASFASNHPGQMPF-ITLPPGPQVLW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  84 PDHCVQQTEGAQLHPLLNQKAIDAVFHKGENPSIDSYSAFFDNGHRQKTALDGWLRHHEITELIVLGLATDYCVKFTVLD 163
Cdd:cd01011   79 PDHCVQGTPGAELHPGLPVPDIDLIVRKGTNPDIDSYSAFFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 527037786 164 ALQLGYTVSVITDGCRGVNiqPQDSAQAFMDMAAEGATL 202
Cdd:cd01011  159 ALKAGFEVRVLEDACRAVD--PETIERAIEEMKEAGVVL 195
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 1-207 3.25e-73

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 220.71  E-value: 3.25e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   1 MTQRALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRgeAVVASQDWHPADHGSFASQHGVEPFTQgelDGLAQ 80
Cdd:PTZ00331  10 STNDALIIVDVQNDFCKGGSLAVPDAEEVIPVINQVRQSHHFD--LVVATQDWHPPNHISFASNHGKPKILP---DGTTQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  81 TFWPDHCVQQTEGAQLHPLLNQKAIDAVFHKGENPSIDSYSAFF-DNGHrqKTALDGWLRHHEITELIVLGLATDYCVKF 159
Cdd:PTZ00331  85 GLWPPHCVQGTKGAQLHKDLVVERIDIIIRKGTNRDVDSYSAFDnDKGS--KTGLAQILKAHGVRRVFICGLAFDFCVLF 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 527037786 160 TVLDALQLGYTVSVITDGCRGVNiqPQDSAQAFMDMAAEGATLYTLED 207
Cdd:PTZ00331 163 TALDAVKLGFKVVVLEDATRAVD--PDAISKQRAELLEAGVILLTSSD 208
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 5-202 1.91e-58

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: 181.64  E-value: 1.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   5 ALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQDWHPADHGSFASQHGvepftqgeldglaqtfWP 84
Cdd:COG1335    1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDL----------------WP 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  85 DHCVQQTEGAQLHPLLNQKAIDAVFHKGenpsidSYSAFFDnghrqkTALDGWLRHHEITELIVLGLATDYCVKFTVLDA 164
Cdd:COG1335   65 PHCVPGTPGAELVPELAPLPGDPVVDKT------RYSAFYG------TDLDELLRERGIDTLVVAGLATDVCVLSTARDA 132

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 527037786 165 LQLGYTVSVITDGCRGVNiqPQDSAQAFMDMAAEGATL 202
Cdd:COG1335  133 LDLGYEVTVVEDACASRD--PEAHEAALARLRAAGATV 168
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 5-196 1.36e-50

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: 161.28  E-value: 1.36e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   5 ALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQDWHPADHGSFASQhgvepftqgeldglaqtFWP 84
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-----------------LWP 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  85 DHCVQQTEGAQLHPLLNQKAIDAVFHKGenpsidSYSAFFDnghrqkTALDGWLRHHEITELIVLGLATDYCVKFTVLDA 164
Cdd:cd00431   64 PHCVKGTEGAELVPELAPLPDDLVIEKT------RYSAFYG------TDLDELLRERGIDTLVVCGIATDICVLATARDA 131

                        170       180       190
                 ....*....|....*....|....*....|..
gi 527037786 165 LQLGYTVSVITDGCRGVNiqPQDSAQAFMDMA 196
Cdd:cd00431  132 LDLGYRVIVVEDACATRD--EEDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 5-206 5.96e-35

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 121.74  E-value: 5.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786    5 ALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQDWHPADHGSFASQHgvepftqgeldglaqtFWP 84
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKD----------------RPS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   85 DHCVQQTEGAQLHPLLNQKAIDAVFHKgenpsiDSYSAFFDnghrqkTALDGWLRHHEITELIVLGLATDYCVKFTVLDA 164
Cdd:pfam00857  66 PAFPPGTTGAELVPELAPLPGDLVVDK------TRFSAFAG------TDLDEILRELGIDTLVLAGVATDVCVLSTARDA 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 527037786  165 LQLGYTVSVITDGCRGVNiqPQDSAQAFMDMAAEGATLYTLE 206
Cdd:pfam00857 134 LDRGYEVVVVSDACASLS--PEAHDAALERLAQRGAEVTTTE 173
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 5-178 6.42e-19

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: 79.56  E-value: 6.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   5 ALLLVDLQNDFCAGGaLAVAEGDSTVDVANTLIEWCKTRGEAVVasqdwhpadhgsFASQHGVEPftqgeldglaQTFWP 84
Cdd:cd01014    1 ALLVIDVQNGYFDGG-LPPLNNEAALENIAALIAAARAAGIPVI------------HVRHIDDEG----------GSFAP 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  85 dhcvqQTEGAQLHPLLNQKAIDAVFHKGENpsidsySAFFDnghrqkTALDGWLRHHEITELIVLGLATDYCVKFTVLDA 164
Cdd:cd01014   58 -----GSEGWEIHPELAPLEGETVIEKTVP------NAFYG------TDLEEWLREAGIDHLVICGAMTEMCVDTTVRSA 120

                        170
                 ....*....|....
gi 527037786 165 LQLGYTVSVITDGC 178
Cdd:cd01014  121 FDLGYDVTVVADAC 134
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
5-178 3.19e-13

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 65.64  E-value: 3.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   5 ALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQdwHPADHgsfasqhgvepftQGELDGLAQTFWP 84
Cdd:COG1535   21 ALLIHDMQNYFLRPYDPDEPPIRELVANIARLRDACRAAGIPVVYTA--QPGDQ-------------TPEDRGLLNDFWG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  85 DHCVQQTEGAQLHPLLNQKAIDAVFHKgenpsiDSYSAFFdnghrqKTALDGWLRHHEITELIVLGLATDYCVKFTVLDA 164
Cdd:COG1535   86 PGLTAGPEGQEIVDELAPAPGDTVLTK------WRYSAFQ------RTDLEERLRELGRDQLIITGVYAHIGCLATAVDA 153

                        170
                 ....*....|....
gi 527037786 165 LQLGYTVSVITDGC 178
Cdd:COG1535  154 FMRDIQPFVVADAV 167
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 146-206 5.61e-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: 52.98  E-value: 5.61e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527037786 146 LIVLGLATDYCVKFTVLDALQLGYTVSVITDGCRGVNiqPQDSAQAFMDMAAEGATLYTLE 206
Cdd:cd01012   91 VVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRS--KEDHELALARMRQAGAVLTTSE 149
PLN02621 PLN02621
nicotinamidase
 5-196 9.57e-06

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 44.77  E-value: 9.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   5 ALLLVDLQNDFCAggalaVAEgdSTVDVANTLIEWCKTRGEAVVASQDWH--PADHGSFasqhgvepftqGEldglaqtF 82
Cdd:PLN02621  22 ALLVIDMQNYFSS-----MAE--PILPALLTTIDLCRRASIPVFFTRHSHksPSDYGML-----------GE-------W 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  83 WP-DHCVQQTEGAQLHPLLNQKA-IDAVFHKgenpsiDSYSAFFdnghrqKTALDGWLRHHEITELIVLGLATDYCVKFT 160
Cdd:PLN02621  77 WDgDLILDGTTEAELMPEIGRVTgPDEVVEK------STYSAFY------NTRLEERLRKIGVKEVIVTGVMTNLCCETT 144

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 527037786 161 VLDALQLGYTVSVITDGCRGVNIQPQDSaqAFMDMA 196
Cdd:PLN02621 145 AREAFVRGFRVFFSTDATATANEELHEA--TLKNLA 178
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 5-178 6.86e-05

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: 42.00  E-value: 6.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786   5 ALLLVDLQNDFCAGGALAVAEGDSTVDVANTLIEWCKTRGEAVVASQ---DWHPADHGSFASqhGVEPFTQ-GELDGLAQ 80
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTvvyDPDGADGGLWAR--KVPAMSDlVEGSPLAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037786  81 TfwpDHCVQQTEGaqlhpllnqkaiDAVFHKGENpsidsySAFFdnghrqKTALDGWLRHHEITELIVLGLATDYCVKFT 160
Cdd:cd01015   79 I---CDELAPQED------------EMVLVKKYA------SAFF------GTSLAATLTARGVDTLIVAGCSTSGCIRAT 131

                        170
                 ....*....|....*...
gi 527037786 161 VLDALQLGYTVSVITDGC 178
Cdd:cd01015  132 AVDAMQHGFRPIVVRECV 149
 
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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