|
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
|
|
|