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Conserved domains on  [gi|267993164|gb|ACY88049|]
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nicotinamidase/pyrazinamidase [Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]

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 1.32e-159

bifunctional nicotinamidase/pyrazinamidase;


:

Pssm-ID: 183228  Cd Length: 212  Bit Score: 439.43  E-value: 1.32e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   2 TNRALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASQDWHPAQHGSFASQHQAEPYSQGKLDGLPQT 81
Cdd:PRK11609   1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQDWHPANHGSFASNHGAEPGTQGELDGLPQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  82 LWPDHCVQHTDGAALHPLLNQHAIDACIYKGENPLIDSYSAFFDNEHRQKTTLDTWLREHDVTELIVMGLATDYCVKFTV 161
Cdd:PRK11609  81 WWPDHCVQNSEGAALHPLLNQKAIDAVFHKGENPLIDSYSAFFDNGHRQKTALDDWLREHGITELIVMGLATDYCVKFTV 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 267993164 162 LDALELGYAVNVITDGCRGVNIHPQDSAHAFMEMASAGATLYTLADWEETQG 213
Cdd:PRK11609 161 LDALALGYQVNVITDGCRGVNLQPQDSAHAFMEMSAAGATLYTLADWEETQG 212
 
Name Accession Description Interval E-value
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
2-213 1.32e-159

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 439.43  E-value: 1.32e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   2 TNRALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASQDWHPAQHGSFASQHQAEPYSQGKLDGLPQT 81
Cdd:PRK11609   1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQDWHPANHGSFASNHGAEPGTQGELDGLPQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  82 LWPDHCVQHTDGAALHPLLNQHAIDACIYKGENPLIDSYSAFFDNEHRQKTTLDTWLREHDVTELIVMGLATDYCVKFTV 161
Cdd:PRK11609  81 WWPDHCVQNSEGAALHPLLNQKAIDAVFHKGENPLIDSYSAFFDNGHRQKTALDDWLREHGITELIVMGLATDYCVKFTV 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 267993164 162 LDALELGYAVNVITDGCRGVNIHPQDSAHAFMEMASAGATLYTLADWEETQG 213
Cdd:PRK11609 161 LDALALGYQVNVITDGCRGVNLQPQDSAHAFMEMSAAGATLYTLADWEETQG 212
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
3-202 1.84e-95

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: 276.45  E-value: 1.84e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   3 NRALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRqiPVLASQDWHPAQHGSFASQHQAEPYSqGKLDGLPQTL 82
Cdd:cd01011    1 TDALLVVDVQNDFCPGGALAVPGGDAIVPLINALLSLFQYD--LVVATQDWHPANHASFASNHPGQMPF-ITLPPGPQVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  83 WPDHCVQHTDGAALHPLLNQHAIDACIYKGENPLIDSYSAFFDNEHRQKTTLDTWLREHDVTELIVMGLATDYCVKFTVL 162
Cdd:cd01011   78 WPDHCVQGTPGAELHPGLPVPDIDLIVRKGTNPDIDSYSAFFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATAL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 267993164 163 DALELGYAVNVITDGCRGVNihPQDSAHAFMEMASAGATL 202
Cdd:cd01011  158 DALKAGFEVRVLEDACRAVD--PETIERAIEEMKEAGVVL 195
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
5-202 9.72e-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: 180.10  E-value: 9.72e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   5 ALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASQDWHPAQHGSFAsqhqaepysqgkldglPQTLWP 84
Cdd:COG1335    1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFA----------------EFDLWP 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  85 DHCVQHTDGAALHPLLNQHAIDACIYKGenplidSYSAFFDnehrqkTTLDTWLREHDVTELIVMGLATDYCVKFTVLDA 164
Cdd:COG1335   65 PHCVPGTPGAELVPELAPLPGDPVVDKT------RYSAFYG------TDLDELLRERGIDTLVVAGLATDVCVLSTARDA 132
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 267993164 165 LELGYAVNVITDGCRGVNihPQDSAHAFMEMASAGATL 202
Cdd:COG1335  133 LDLGYEVTVVEDACASRD--PEAHEAALARLRAAGATV 168
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
5-206 2.22e-34

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 120.59  E-value: 2.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164    5 ALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASQDWHPAqhgsfasqhqaepysqGKLDGLPQTLWP 84
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEP----------------DDADFALKDRPS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   85 DHCVQHTDGAALHPLLNQHAIDACIYKgenpliDSYSAFFDnehrqkTTLDTWLREHDVTELIVMGLATDYCVKFTVLDA 164
Cdd:pfam00857  66 PAFPPGTTGAELVPELAPLPGDLVVDK------TRFSAFAG------TDLDEILRELGIDTLVLAGVATDVCVLSTARDA 133
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 267993164  165 LELGYAVNVITDGCRGVNihPQDSAHAFMEMASAGATLYTLA 206
Cdd:pfam00857 134 LDRGYEVVVVSDACASLS--PEAHDAALERLAQRGAEVTTTE 173
 
Name Accession Description Interval E-value
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
2-213 1.32e-159

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 439.43  E-value: 1.32e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   2 TNRALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASQDWHPAQHGSFASQHQAEPYSQGKLDGLPQT 81
Cdd:PRK11609   1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPVIASQDWHPANHGSFASNHGAEPGTQGELDGLPQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  82 LWPDHCVQHTDGAALHPLLNQHAIDACIYKGENPLIDSYSAFFDNEHRQKTTLDTWLREHDVTELIVMGLATDYCVKFTV 161
Cdd:PRK11609  81 WWPDHCVQNSEGAALHPLLNQKAIDAVFHKGENPLIDSYSAFFDNGHRQKTALDDWLREHGITELIVMGLATDYCVKFTV 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 267993164 162 LDALELGYAVNVITDGCRGVNIHPQDSAHAFMEMASAGATLYTLADWEETQG 213
Cdd:PRK11609 161 LDALALGYQVNVITDGCRGVNLQPQDSAHAFMEMSAAGATLYTLADWEETQG 212
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
3-202 1.84e-95

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: 276.45  E-value: 1.84e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   3 NRALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRqiPVLASQDWHPAQHGSFASQHQAEPYSqGKLDGLPQTL 82
Cdd:cd01011    1 TDALLVVDVQNDFCPGGALAVPGGDAIVPLINALLSLFQYD--LVVATQDWHPANHASFASNHPGQMPF-ITLPPGPQVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  83 WPDHCVQHTDGAALHPLLNQHAIDACIYKGENPLIDSYSAFFDNEHRQKTTLDTWLREHDVTELIVMGLATDYCVKFTVL 162
Cdd:cd01011   78 WPDHCVQGTPGAELHPGLPVPDIDLIVRKGTNPDIDSYSAFFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATAL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 267993164 163 DALELGYAVNVITDGCRGVNihPQDSAHAFMEMASAGATL 202
Cdd:cd01011  158 DALKAGFEVRVLEDACRAVD--PETIERAIEEMKEAGVVL 195
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
1-210 9.88e-70

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 211.85  E-value: 9.88e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   1 MTNRALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQipVLASQDWHPAQHGSFASQHQAEPYSQgklDGLPQ 80
Cdd:PTZ00331  10 STNDALIIVDVQNDFCKGGSLAVPDAEEVIPVINQVRQSHHFDL--VVATQDWHPPNHISFASNHGKPKILP---DGTTQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  81 TLWPDHCVQHTDGAALHPLLNQHAIDACIYKGENPLIDSYSAFfDNEHRQKTTLDTWLREHDVTELIVMGLATDYCVKFT 160
Cdd:PTZ00331  85 GLWPPHCVQGTKGAQLHKDLVVERIDIIIRKGTNRDVDSYSAF-DNDKGSKTGLAQILKAHGVRRVFICGLAFDFCVLFT 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 267993164 161 VLDALELGYAVNVITDGCRGVNihPQDSAHAFMEMASAGATLYTLADWEE 210
Cdd:PTZ00331 164 ALDAVKLGFKVVVLEDATRAVD--PDAISKQRAELLEAGVILLTSSDLVA 211
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
5-202 9.72e-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: 180.10  E-value: 9.72e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   5 ALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASQDWHPAQHGSFAsqhqaepysqgkldglPQTLWP 84
Cdd:COG1335    1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFA----------------EFDLWP 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  85 DHCVQHTDGAALHPLLNQHAIDACIYKGenplidSYSAFFDnehrqkTTLDTWLREHDVTELIVMGLATDYCVKFTVLDA 164
Cdd:COG1335   65 PHCVPGTPGAELVPELAPLPGDPVVDKT------RYSAFYG------TDLDELLRERGIDTLVVAGLATDVCVLSTARDA 132
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 267993164 165 LELGYAVNVITDGCRGVNihPQDSAHAFMEMASAGATL 202
Cdd:COG1335  133 LDLGYEVTVVEDACASRD--PEAHEAALARLRAAGATV 168
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
5-196 3.72e-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: 160.51  E-value: 3.72e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   5 ALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASQDWHPAQHGSFASQhqaepysqgkldglpqtLWP 84
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-----------------LWP 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  85 DHCVQHTDGAALHPLLNQHAIDACIYKGenplidSYSAFFDnehrqkTTLDTWLREHDVTELIVMGLATDYCVKFTVLDA 164
Cdd:cd00431   64 PHCVKGTEGAELVPELAPLPDDLVIEKT------RYSAFYG------TDLDELLRERGIDTLVVCGIATDICVLATARDA 131
                        170       180       190
                 ....*....|....*....|....*....|..
gi 267993164 165 LELGYAVNVITDGCRGVNihPQDSAHAFMEMA 196
Cdd:cd00431  132 LDLGYRVIVVEDACATRD--EEDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
5-206 2.22e-34

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 120.59  E-value: 2.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164    5 ALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASQDWHPAqhgsfasqhqaepysqGKLDGLPQTLWP 84
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEP----------------DDADFALKDRPS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   85 DHCVQHTDGAALHPLLNQHAIDACIYKgenpliDSYSAFFDnehrqkTTLDTWLREHDVTELIVMGLATDYCVKFTVLDA 164
Cdd:pfam00857  66 PAFPPGTTGAELVPELAPLPGDLVVDK------TRFSAFAG------TDLDEILRELGIDTLVLAGVATDVCVLSTARDA 133
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 267993164  165 LELGYAVNVITDGCRGVNihPQDSAHAFMEMASAGATLYTLA 206
Cdd:pfam00857 134 LDRGYEVVVVSDACASLS--PEAHDAALERLAQRGAEVTTTE 173
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
5-178 2.56e-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: 80.71  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   5 ALLLVDLQNDFCAGGaLAVAEGDSTIDIANALIDWCQPRQIPVLasqdwHpAQHgsfasqHQAEPYSqgkldglpqtLWP 84
Cdd:cd01014    1 ALLVIDVQNGYFDGG-LPPLNNEAALENIAALIAAARAAGIPVI-----H-VRH------IDDEGGS----------FAP 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  85 DhcvqhTDGAALHPLLNQHAIDACIYKGENplidsySAFFDnehrqkTTLDTWLREHDVTELIVMGLATDYCVKFTVLDA 164
Cdd:cd01014   58 G-----SEGWEIHPELAPLEGETVIEKTVP------NAFYG------TDLEEWLREAGIDHLVICGAMTEMCVDTTVRSA 120
                        170
                 ....*....|....
gi 267993164 165 LELGYAVNVITDGC 178
Cdd:cd01014  121 FDLGYDVTVVADAC 134
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
5-178 4.66e-13

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 65.26  E-value: 4.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   5 ALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASqdwhpaqhgsfasqhqAEPYSQGKLD-GLPQTLW 83
Cdd:COG1535   21 ALLIHDMQNYFLRPYDPDEPPIRELVANIARLRDACRAAGIPVVYT----------------AQPGDQTPEDrGLLNDFW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  84 PDHCVQHTDGAALHPLLNQHAIDACIYKgenpliDSYSAFFdnehrqKTTLDTWLREHDVTELIVMGLATDYCVKFTVLD 163
Cdd:COG1535   85 GPGLTAGPEGQEIVDELAPAPGDTVLTK------WRYSAFQ------RTDLEERLRELGRDQLIITGVYAHIGCLATAVD 152
                        170
                 ....*....|....*
gi 267993164 164 ALELGYAVNVITDGC 178
Cdd:COG1535  153 AFMRDIQPFVVADAV 167
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
130-204 3.68e-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: 53.75  E-value: 3.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164 130 QKTTLDTW--------LREHDVTELIVMGLATDYCVKFTVLDALELGYAVNVITDGCRGVNihPQDSAHAFMEMASAGAT 201
Cdd:cd01012   67 EKTSFSCWedeafrkaLKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRS--KEDHELALARMRQAGAV 144

                 ...
gi 267993164 202 LYT 204
Cdd:cd01012  145 LTT 147
PLN02743 PLN02743
nicotinamidase
6-190 1.48e-05

nicotinamidase


Pssm-ID: 215396  Cd Length: 239  Bit Score: 44.34  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   6 LLLVDLQNDFCAGGA--LAVAEGDSTID--------IANALIDwcqpRQIPVLASQDWH-PAQHgsfasqhqAEPYsqgk 74
Cdd:PLN02743  30 LVLVDEVNGFCTVGAgnLAPREPDKQISkmvdesarLAREFCE----RKWPVLAFLDSHhPDKP--------EHPY---- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  75 ldglpqtlwPDHCVQHTDGAALHPLLNQHAIDACIYKGENPLIDSYSAFFDNEhrQKTTLDTWLREHDVTELIVMGLATD 154
Cdd:PLN02743  94 ---------PPHCIVGTGEENLVPALQWLENDPNVTLRRKDCIDGFVGAIEKD--GSNVFVDWVNNNKIKVILVVGICTD 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 267993164 155 YCV-KF--TVLDALELGYA-----VNVITDGC-------------RGVNIHPQDSAH 190
Cdd:PLN02743 163 ICVlDFvaSALSARNHGILppledVVVYSRGCatydlplhvaktiKGALAHPQELMH 219
PLN02621 PLN02621
nicotinamidase
5-202 3.46e-05

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 43.23  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   5 ALLLVDLQNDFCAGGALAVAEGDSTIDIanalidwCQPRQIPVLASQDWH--PAQHGSFASqhqaepysqgkldglpqtL 82
Cdd:PLN02621  22 ALLVIDMQNYFSSMAEPILPALLTTIDL-------CRRASIPVFFTRHSHksPSDYGMLGE------------------W 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  83 WP-DHCVQHTDGAALHPLLNQHAidaciykGENPLID--SYSAFFdnehrqKTTLDTWLREHDVTELIVMGLATDYCVKF 159
Cdd:PLN02621  77 WDgDLILDGTTEAELMPEIGRVT-------GPDEVVEksTYSAFY------NTRLEERLRKIGVKEVIVTGVMTNLCCET 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 267993164 160 TVLDALELGYAVNVITDGCRGVNIHPQDSahAFMEMASAGATL 202
Cdd:PLN02621 144 TAREAFVRGFRVFFSTDATATANEELHEA--TLKNLAYGFAYL 184
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
5-178 5.46e-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: 42.39  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164   5 ALLLVDLQNDFCAGGALAVAEGDSTIDIANALIDWCQPRQIPVLASQ---DWHPAQHGSFAsqhqaepysqgklDGLPQT 81
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTvvyDPDGADGGLWA-------------RKVPAM 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 267993164  82 LWPdhcvqhTDGAALHpllnqhAIDACI--YKGENPLIDSY-SAFFdnehrqKTTLDTWLREHDVTELIVMGLATDYCVK 158
Cdd:cd01015   68 SDL------VEGSPLA------AICDELapQEDEMVLVKKYaSAFF------GTSLAATLTARGVDTLIVAGCSTSGCIR 129
                        170       180
                 ....*....|....*....|
gi 267993164 159 FTVLDALELGYAVNVITDGC 178
Cdd:cd01015  130 ATAVDAMQHGFRPIVVRECV 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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