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Conserved domains on  [gi|504290734|ref|WP_014477836|]
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MULTISPECIES: cysteine hydrolase family protein [Bacillus]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 10003554)

cysteine hydrolase family protein related to isochorismatase and nicotinamidase; catalyzes the hydrolysis of a chemical bond using an active site cysteinyl residue

CATH:  3.40.50.850
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 4-182 1.80e-54

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: 170.47  E-value: 1.80e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   4 ALICIDYTNDFVAsDGKLTCgEPGRMIEEAIVNLTEEFITNGDYVVLAVDSHDEGDQYHPETRLFPPHNIKGTEGKDLYG 83
Cdd:COG1335    1 ALLVIDVQNDFVP-PGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  84 KLLPLyqkhehePNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQ 163
Cdd:COG1335   79 ELAPL-------PGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP 151

                        170
                 ....*....|....*....
gi 504290734 164 EGHAWALSHFANsIGAQVA 182
Cdd:COG1335  152 EAHEAALARLRA-AGATVV 169
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 4-182 1.80e-54

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: 170.47  E-value: 1.80e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   4 ALICIDYTNDFVAsDGKLTCgEPGRMIEEAIVNLTEEFITNGDYVVLAVDSHDEGDQYHPETRLFPPHNIKGTEGKDLYG 83
Cdd:COG1335    1 ALLVIDVQNDFVP-PGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  84 KLLPLyqkhehePNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQ 163
Cdd:COG1335   79 ELAPL-------PGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP 151

                        170
                 ....*....|....*....
gi 504290734 164 EGHAWALSHFANsIGAQVA 182
Cdd:COG1335  152 EAHEAALARLRA-AGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 4-174 9.71e-51

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: 9.71e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   4 ALICIDYTNDFVASDGKLTcgEPGRMIEEAIVNLTEEFITNGDYVVLAVDSHDEGDQYHPETrLFPPHNIKGTEGKDLYG 83
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLL--PGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGTEGAELVP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  84 KLLPlyqkhehEPNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQ 163
Cdd:cd00431   78 ELAP-------LPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDE 150

                        170
                 ....*....|.
gi 504290734 164 EGHAWALSHFA 174
Cdd:cd00431  151 EDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 4-181 3.51e-39

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 131.37  E-value: 3.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734    4 ALICIDYTNDFVASDGKLTcgEPGRMIEEAIVNLTEEFITNGDYVVLAVDSHDEGDQYHPETRLFPPHNIKGTEGKDLYG 83
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKV--EGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   84 KLLPLyqkhehePNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQ 163
Cdd:pfam00857  80 ELAPL-------PGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSP 152

                         170
                  ....*....|....*...
gi 504290734  164 EGHAWALSHFANSiGAQV 181
Cdd:pfam00857 153 EAHDAALERLAQR-GAEV 169
PLN02621 PLN02621
nicotinamidase
 102-174 3.72e-14

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 67.11  E-value: 3.72e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504290734 102 EKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQEGHAWALSHFA 174
Cdd:PLN02621 106 EKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEATLKNLA 178
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 4-182 1.80e-54

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: 170.47  E-value: 1.80e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   4 ALICIDYTNDFVAsDGKLTCgEPGRMIEEAIVNLTEEFITNGDYVVLAVDSHDEGDQYHPETRLFPPHNIKGTEGKDLYG 83
Cdd:COG1335    1 ALLVIDVQNDFVP-PGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  84 KLLPLyqkhehePNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQ 163
Cdd:COG1335   79 ELAPL-------PGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP 151

                        170
                 ....*....|....*....
gi 504290734 164 EGHAWALSHFANsIGAQVA 182
Cdd:COG1335  152 EAHEAALARLRA-AGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 4-174 9.71e-51

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: 9.71e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   4 ALICIDYTNDFVASDGKLTcgEPGRMIEEAIVNLTEEFITNGDYVVLAVDSHDEGDQYHPETrLFPPHNIKGTEGKDLYG 83
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLL--PGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGTEGAELVP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  84 KLLPlyqkhehEPNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQ 163
Cdd:cd00431   78 ELAP-------LPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDE 150

                        170
                 ....*....|.
gi 504290734 164 EGHAWALSHFA 174
Cdd:cd00431  151 EDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 4-181 3.51e-39

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 131.37  E-value: 3.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734    4 ALICIDYTNDFVASDGKLTcgEPGRMIEEAIVNLTEEFITNGDYVVLAVDSHDEGDQYHPETRLFPPHNIKGTEGKDLYG 83
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKV--EGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   84 KLLPLyqkhehePNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQ 163
Cdd:pfam00857  80 ELAPL-------PGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSP 152

                         170
                  ....*....|....*...
gi 504290734  164 EGHAWALSHFANSiGAQV 181
Cdd:pfam00857 153 EAHDAALERLAQR-GAEV 169
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 4-171 2.39e-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: 79.94  E-value: 2.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   4 ALICIDYTNDFVASdgkltcGEPGRMIEEAIVN---LTEEFITNGDYVVLAVdsHDEgdqyhPETRLFPPhnikGTEGKD 80
Cdd:cd01014    1 ALLVIDVQNGYFDG------GLPPLNNEAALENiaaLIAAARAAGIPVIHVR--HID-----DEGGSFAP----GSEGWE 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  81 LYGKLLPLyqkhEHEPNVyymEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVAS 160
Cdd:cd01014   64 IHPELAPL----EGETVI---EKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACAT 136

                        170
                 ....*....|.
gi 504290734 161 FNQEGHAWALS 171
Cdd:cd01014  137 FDLPDHGGVLS 147
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
4-178 5.40e-19

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 80.28  E-value: 5.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   4 ALICIDYTNDFVASDGKltCGEPGRMIEEAIVNLTEEFITNGDYVVLAVDSHDEgdqyHPETR-----LFPPHNIKGTEG 78
Cdd:COG1535   21 ALLIHDMQNYFLRPYDP--DEPPIRELVANIARLRDACRAAGIPVVYTAQPGDQ----TPEDRgllndFWGPGLTAGPEG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  79 KDLYGKLLPlyqkhehEPNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAV 158
Cdd:COG1535   95 QEIVDELAP-------APGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAV 167

                        170       180
                 ....*....|....*....|
gi 504290734 159 ASFNQEGHAWALSHFANSIG 178
Cdd:COG1535  168 ADFSREEHRMALEYVAGRCG 187
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 2-169 3.33e-18

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: 78.07  E-value: 3.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   2 KKALICIDYTNDFVaSDGKLTCGEpGRMIEEAIVNLTEEFitNGDYVVLAVDSHDE---------------GDQYHPETR 66
Cdd:cd01011    1 TDALLVVDVQNDFC-PGGALAVPG-GDAIVPLINALLSLF--QYDLVVATQDWHPAnhasfasnhpgqmpfITLPPGPQV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  67 LFPPHNIKGTEGKDLYGKL-LPLYQKHEH---EPNVYYmektrYSAF------AGTDLELKLRERQIGELHLAGVCTDIC 136
Cdd:cd01011   77 LWPDHCVQGTPGAELHPGLpVPDIDLIVRkgtNPDIDS-----YSAFfdndrrSSTGLAEYLRERGIDRVDVVGLATDYC 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 504290734 137 VLHTAVDAYNKGFRIVVHKQAVASFNQEG--HAWA 169
Cdd:cd01011  152 VKATALDALKAGFEVRVLEDACRAVDPETieRAIE 186
PLN02621 PLN02621
nicotinamidase
 102-174 3.72e-14

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 67.11  E-value: 3.72e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504290734 102 EKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQEGHAWALSHFA 174
Cdd:PLN02621 106 EKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEATLKNLA 178
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 101-183 6.40e-14

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: 66.27  E-value: 6.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734 101 MEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQEGHAWALSHFANSIGAQ 180
Cdd:cd01015   92 LVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAPHEANLFDIDNKYGDV 171


                 ...
gi 504290734 181 VAE 183
Cdd:cd01015  172 VST 174
PLN02743 PLN02743
nicotinamidase
 5-162 3.93e-13

nicotinamidase


Pssm-ID: 215396  Cd Length: 239  Bit Score: 65.15  E-value: 3.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   5 LICIDYTNDF-VASDGKLTCGEPG----RMIEEAiVNLTEEFITNGDYVVLAVDSHDEGDQYHPetrlFPPHNIKGTEGK 79
Cdd:PLN02743  30 LVLVDEVNGFcTVGAGNLAPREPDkqisKMVDES-ARLAREFCERKWPVLAFLDSHHPDKPEHP----YPPHCIVGTGEE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  80 dlygKLLPLYQKHEHEPNVYYMEKTRYSAFAGTdLELK--------LRERQIGELHLAGVCTDICVLH---TAVDAYNKG 148
Cdd:PLN02743 105 ----NLVPALQWLENDPNVTLRRKDCIDGFVGA-IEKDgsnvfvdwVNNNKIKVILVVGICTDICVLDfvaSALSARNHG 179

                        170
                 ....*....|....*....
gi 504290734 149 F-----RIVVHKQAVASFN 162
Cdd:PLN02743 180 IlppleDVVVYSRGCATYD 198
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 2-173 5.11e-12

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 61.62  E-value: 5.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   2 KKALICIDYTNDFVaSDGKLTCgEPGRMIEEAIVNLTEEfiTNGDYVVLAVDSHDEG-------------DQYHPETRLF 68
Cdd:PTZ00331  12 NDALIIVDVQNDFC-KGGSLAV-PDAEEVIPVINQVRQS--HHFDLVVATQDWHPPNhisfasnhgkpkiLPDGTTQGLW 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  69 PPHNIKGTEGKDLYGKLlplyqkHEHEPNVYYMEKTR-----YSAFAG-----TDLELKLRERQIGELHLAGVCTDICVL 138
Cdd:PTZ00331  88 PPHCVQGTKGAQLHKDL------VVERIDIIIRKGTNrdvdsYSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVL 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 504290734 139 HTAVDAYNKGFRIVVHKQAVASFNQEGHAWALSHF 173
Cdd:PTZ00331 162 FTALDAVKLGFKVVVLEDATRAVDPDAISKQRAEL 196
PRK11440 PRK11440
putative hydrolase; Provisional
 103-178 5.42e-11

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 58.59  E-value: 5.42e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504290734 103 KTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQEGHAWALSHFANSIG 178
Cdd:PRK11440 101 KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHQNSMNHIFPRIA 176
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
1-153 1.59e-09

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 55.00  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734   1 MKKALICIDYTNDFVASdGKLTCGEPGRMIeeAIVN-LTEEFITNGDYVVLAVDSH--DEGD-----QYHPETR------ 66
Cdd:PRK11609   1 MKRALLLVDLQNDFCAG-GALAVPEGDSTI--DVANrLIDWCQSRGIPVIASQDWHpaNHGSfasnhGAEPGTQgeldgl 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  67 ---LFPPHNIKGTEGKDLYgkllPLYQKHEHEPNVYYMEKTR---YSAF------AGTDLELKLRERQIGELHLAGVCTD 134
Cdd:PRK11609  78 pqtWWPDHCVQNSEGAALH----PLLNQKAIDAVFHKGENPLidsYSAFfdnghrQKTALDDWLREHGITELIVMGLATD 153

                        170
                 ....*....|....*....
gi 504290734 135 ICVLHTAVDAYNKGFRIVV 153
Cdd:PRK11609 154 YCVKFTVLDALALGYQVNV 172
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 83-170 1.94e-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: 1.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  83 GKLLPLYQK-HEHEPNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASF 161
Cdd:cd01012   47 KGLGPTVPElREVFPDAPVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSR 126


                 ....*....
gi 504290734 162 NQEGHAWAL 170
Cdd:cd01012  127 SKEDHELAL 135
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 95-174 2.69e-09

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: 54.27  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504290734  95 EPNVYYMEKTRYSAFAGTDLELKLRERQIGELHLAGVCTDICVLHTAVDAYNKGFRIVVHKQAVASFNQEGHAWALSHFA 174
Cdd:cd01013  114 QPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADFSLEEHRMALKYAA 193
 
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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