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Conserved domains on  [gi|489339957|ref|WP_003247139|]
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MULTISPECIES: isochorismatase family cysteine hydrolase [Bacillus]

Protein Classification

isochorismatase family cysteine hydrolase( domain architecture ID 10087237)

cysteine hydrolase family protein such as 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
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 7-165 2.77e-45

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: 146.64  E-value: 2.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFEFDMGETLAKKtEKIVPHILSLKEHARQNEWPIIYINDHYGLWQADIK---NIQQECTNERSKDIITKI 83
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGA-DELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAellWPPHCVKGTEGAELVPEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  84 APVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDEDNEFALTM 163
Cdd:cd00431   80 APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALER 159


                 ..
gi 489339957 164 ME 165
Cdd:cd00431  160 LA 161
 
Name Accession Description Interval E-value
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 7-165 2.77e-45

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: 146.64  E-value: 2.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFEFDMGETLAKKtEKIVPHILSLKEHARQNEWPIIYINDHYGLWQADIK---NIQQECTNERSKDIITKI 83
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGA-DELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAellWPPHCVKGTEGAELVPEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  84 APVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDEDNEFALTM 163
Cdd:cd00431   80 APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALER 159


                 ..
gi 489339957 164 ME 165
Cdd:cd00431  160 LA 161
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 7-173 2.86e-45

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: 146.97  E-value: 2.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFeFDMGETLAKKTEKIVPHILSLKEHARQNEWPIIYINDHY---GLWQADIKNIQQECT-NERSKDIITK 82
Cdd:COG1335    1 ALLVIDVQNDF-VPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHppdGSEFAEFDLWPPHCVpGTPGAELVPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  83 IAPVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDEDNEFALT 162
Cdd:COG1335   80 LAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAALA 159

                        170
                 ....*....|.
gi 489339957 163 MMENvLFAEIT 173
Cdd:COG1335  160 RLRA-AGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 7-176 6.60e-37

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 125.59  E-value: 6.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957    7 ALLIVDMINNFeFDMGETLAKKTEKIVPHILSLKEHARQNEWPIIYINDHYGLWQADIKNIQQECT----NERSKDIITK 82
Cdd:pfam00857   2 ALLVIDMQNDF-VDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPafppGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   83 IAPVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDEDNEFALT 162
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAALE 160

                         170
                  ....*....|....
gi 489339957  163 MMENvLFAEITTEE 176
Cdd:pfam00857 161 RLAQ-RGAEVTTTE 173
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 7-155 4.38e-11

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 59.31  E-value: 4.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFEFDmGETLAKKTEKIVP------------------------HILSLKEHAR---------QNEWPIIYI 53
Cdd:PTZ00331  14 ALIIVDVQNDFCKG-GSLAVPDAEEVIPvinqvrqshhfdlvvatqdwhppnHISFASNHGKpkilpdgttQGLWPPHCV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  54 NDHYGlwqADI-KNIQQECTNErskdIITKIAPVDADYFlikpkhSAFYE-----TALHTLLTELQVRHIIITGIAGNIC 127
Cdd:PTZ00331  93 QGTKG---AQLhKDLVVERIDI----IIRKGTNRDVDSY------SAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFC 159

                        170       180
                 ....*....|....*....|....*...
gi 489339957 128 VLFTANDAYMREYSITIPKDCIASNSDE 155
Cdd:PTZ00331 160 VLFTALDAVKLGFKVVVLEDATRAVDPD 187
 
Name Accession Description Interval E-value
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 7-165 2.77e-45

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: 146.64  E-value: 2.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFEFDMGETLAKKtEKIVPHILSLKEHARQNEWPIIYINDHYGLWQADIK---NIQQECTNERSKDIITKI 83
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGA-DELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAellWPPHCVKGTEGAELVPEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  84 APVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDEDNEFALTM 163
Cdd:cd00431   80 APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALER 159


                 ..
gi 489339957 164 ME 165
Cdd:cd00431  160 LA 161
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 7-173 2.86e-45

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: 146.97  E-value: 2.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFeFDMGETLAKKTEKIVPHILSLKEHARQNEWPIIYINDHY---GLWQADIKNIQQECT-NERSKDIITK 82
Cdd:COG1335    1 ALLVIDVQNDF-VPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHppdGSEFAEFDLWPPHCVpGTPGAELVPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  83 IAPVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDEDNEFALT 162
Cdd:COG1335   80 LAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAALA 159

                        170
                 ....*....|.
gi 489339957 163 MMENvLFAEIT 173
Cdd:COG1335  160 RLRA-AGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 7-176 6.60e-37

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 125.59  E-value: 6.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957    7 ALLIVDMINNFeFDMGETLAKKTEKIVPHILSLKEHARQNEWPIIYINDHYGLWQADIKNIQQECT----NERSKDIITK 82
Cdd:pfam00857   2 ALLVIDMQNDF-VDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPafppGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   83 IAPVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDEDNEFALT 162
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAALE 160

                         170
                  ....*....|....
gi 489339957  163 MMENvLFAEITTEE 176
Cdd:pfam00857 161 RLAQ-RGAEVTTTE 173
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
7-180 8.63e-33

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 116.10  E-value: 8.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNF--EFDMGETLAkktEKIVPHILSLKEHARQNEWPIIY--------------INDhygLWQADIKniqqe 70
Cdd:COG1535   21 ALLIHDMQNYFlrPYDPDEPPI---RELVANIARLRDACRAAGIPVVYtaqpgdqtpedrglLND---FWGPGLT----- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  71 CTNERSKdIITKIAPVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIA 150
Cdd:COG1535   90 AGPEGQE-IVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVA 168

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489339957 151 SNSDEDNEFALtmmENV--LFAEITTEEQIIE 180
Cdd:COG1535  169 DFSREEHRMAL---EYVagRCGVVVTTDEVLE 197
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 7-162 5.12e-18

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: 77.76  E-value: 5.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFEFDMGETLAKKTEkIVPHILSLKEHARQNEWPIIY--------------INDHYGLWQADIKNIQQect 72
Cdd:cd01013   31 VLLVHDMQRYFLDFYDESAEPVPQ-LIANIARLRDWCRQAGIPVVYtaqpgnqtpeqralLNDFWGPGLTASPEETK--- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  73 nerskdIITKIAPVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASN 152
Cdd:cd01013  107 ------IVTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADF 180

                        170
                 ....*....|
gi 489339957 153 SDEDNEFALT 162
Cdd:cd01013  181 SLEEHRMALK 190
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 7-164 3.63e-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: 74.16  E-value: 3.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINnfEFDMGETLAKKTEKIVPHILSLKEHARQNEWPIIYINDH----YGLWQadikniqqectNERSKDIITK 82
Cdd:cd01014    1 ALLVIDVQN--GYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIddegGSFAP-----------GSEGWEIHPE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  83 IAPVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASnsdEDNEFALT 162
Cdd:cd01014   68 LAPLEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACAT---FDLPDHGG 144


                 ..
gi 489339957 163 MM 164
Cdd:cd01014  145 VL 146
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 7-176 1.79e-15

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: 70.51  E-value: 1.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFEfDMGETLAKKTEKIVPHILSLKEHARQNEWPIIYINDHY-------GLWQADIKNIQQECTNERSKDI 79
Cdd:cd01015    1 ALLVIDLVEGYT-QPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTVVYdpdgadgGLWARKVPAMSDLVEGSPLAAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  80 ITKIAPVDADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDEDNEF 159
Cdd:cd01015   80 CDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAPHEA 159

                        170
                 ....*....|....*..
gi 489339957 160 ALTMMENVLFAEITTEE 176
Cdd:cd01015  160 NLFDIDNKYGDVVSTDD 176
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 7-155 4.38e-11

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 59.31  E-value: 4.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFEFDmGETLAKKTEKIVP------------------------HILSLKEHAR---------QNEWPIIYI 53
Cdd:PTZ00331  14 ALIIVDVQNDFCKG-GSLAVPDAEEVIPvinqvrqshhfdlvvatqdwhppnHISFASNHGKpkilpdgttQGLWPPHCV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  54 NDHYGlwqADI-KNIQQECTNErskdIITKIAPVDADYFlikpkhSAFYE-----TALHTLLTELQVRHIIITGIAGNIC 127
Cdd:PTZ00331  93 QGTKG---AQLhKDLVVERIDI----IIRKGTNRDVDSY------SAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFC 159

                        170       180
                 ....*....|....*....|....*...
gi 489339957 128 VLFTANDAYMREYSITIPKDCIASNSDE 155
Cdd:PTZ00331 160 VLFTALDAVKLGFKVVVLEDATRAVDPD 187
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 74-179 5.19e-11

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: 57.99  E-value: 5.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  74 ERSKDIITKIAPVDADYFLI-KPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASN 152
Cdd:cd01012   47 KGLGPTVPELREVFPDAPVIeKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSR 126

                         90       100
                 ....*....|....*....|....*..
gi 489339957 153 SDEDNEFALTMMENvLFAEITTEEQII 179
Cdd:cd01012  127 SKEDHELALARMRQ-AGAVLTTSESVL 152
PLN02621 PLN02621
nicotinamidase
 7-164 2.24e-08

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 51.32  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   7 ALLIVDMINNFefdmgetlAKKTEKIVPHILSLKEHARQNEWPIIYI-NDH-----YGL----WQADIknIQQECTNers 76
Cdd:PLN02621  22 ALLVIDMQNYF--------SSMAEPILPALLTTIDLCRRASIPVFFTrHSHkspsdYGMlgewWDGDL--ILDGTTE--- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  77 KDIITKIAPV-DADYFLIKPKHSAFYETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDE 155
Cdd:PLN02621  89 AELMPEIGRVtGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEE 168


                 ....*....
gi 489339957 156 DNEFALTMM 164
Cdd:PLN02621 169 LHEATLKNL 177
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
97-164 9.73e-07

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 46.91  E-value: 9.73e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489339957  97 HSAFY------ETALHTLLTELQVRHIIITGIAGNICVLFTANDAYMREYSITIPKD-CIASN-SDEDNEFALTMM 164
Cdd:PRK11609 119 YSAFFdnghrqKTALDDWLREHGITELIVMGLATDYCVKFTVLDALALGYQVNVITDgCRGVNlQPQDSAHAFMEM 194
PRK11440 PRK11440
putative hydrolase; Provisional
 83-162 1.61e-06

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 46.26  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  83 IAPVDADYFLIKPKHSAFYETALhtlltELQVRH-----IIITGIAGNICVLFTANDAYMREYSITIPKDCIASNSDEDN 157
Cdd:PRK11440  90 LGKTDSDIEVTKRQWGAFYGTDL-----ELQLRRrgidtIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQH 164


                 ....*
gi 489339957 158 EFALT 162
Cdd:PRK11440 165 QNSMN 169
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 6-164 4.90e-06

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: 44.95  E-value: 4.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957   6 KALLIVDMINNFefdM-GETLA-KKTEKIVPHILslkEHARQNEW-PIIYIND-HY---GLWQADIKNIQQECT------ 72
Cdd:cd01011    2 DALLVVDVQNDF---CpGGALAvPGGDAIVPLIN---ALLSLFQYdLVVATQDwHPanhASFASNHPGQMPFITlppgpq 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489339957  73 ---------NERSKDIITKIAPVDADYFLIK------PKHSAFYE------TALHTLLTELQVRHIIITGIAGNICVLFT 131
Cdd:cd01011   76 vlwpdhcvqGTPGAELHPGLPVPDIDLIVRKgtnpdiDSYSAFFDndrrssTGLAEYLRERGIDRVDVVGLATDYCVKAT 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489339957 132 ANDAYMREYSITIPKDCIASNSDEDNEFALTMM 164
Cdd:cd01011  156 ALDALKAGFEVRVLEDACRAVDPETIERAIEEM 188
 
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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