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Conserved domains on  [gi|1767231942|sp|G2X4M1|]
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RecName: Full=Secreted isochorismatase effector Isc1

Protein Classification

cysteine hydrolase family protein( domain architecture ID 10099067)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 21-172 1.98e-48

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: 154.67  E-value: 1.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  21 VLVIIDAQGEYAEGKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPlFTQGTKLAEIFDELTPKEGEAVVTK 100
Cdd:cd01014     1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGS-FAPGSEGWEIHPELAPLEGETVIEK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767231942 101 HHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPG----VDAAQLVKVA 172
Cdd:cd01014    80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDhggvLSAEEIHAHY 155
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 21-172 1.98e-48

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: 154.67  E-value: 1.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  21 VLVIIDAQGEYAEGKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPlFTQGTKLAEIFDELTPKEGEAVVTK 100
Cdd:cd01014     1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGS-FAPGSEGWEIHPELAPLEGETVIEK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767231942 101 HHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPG----VDAAQLVKVA 172
Cdd:cd01014    80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDhggvLSAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 21-184 1.25e-47

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: 153.14  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  21 VLVIIDAQGEYAE-GKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPLFT----------QGTKLAEIFDEL 89
Cdd:COG1335     1 ALLVIDVQNDFVPpGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTPGAELVPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  90 TPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPGVDAaqlv 169
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEA---- 156

                         170
                  ....*....|....*
gi 1767231942 170 kvALAEIADVFGTLV 184
Cdd:COG1335   157 --ALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 20-186 2.16e-42

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 139.85  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  20 SVLVIIDAQ-GEYAEGKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPLFT----------QGTKLAEIFDE 88
Cdd:pfam00857   1 TALLVIDMQnDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFAlkdrpspafpPGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  89 LTPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPGVDAaql 168
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA--- 157

                         170
                  ....*....|....*...
gi 1767231942 169 vkvALAEIADVFGTLVSS 186
Cdd:pfam00857 158 ---ALERLAQRGAEVTTT 172
PLN02621 PLN02621
nicotinamidase
 20-154 1.15e-16

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 74.05  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  20 SVLVIIDAQGEYAegklkiSNIEASRPNISSLLEKYRAANAPIVHV--VHETPAGAP---------LFTQGTKLAEIFDE 88
Cdd:PLN02621   21 AALLVIDMQNYFS------SMAEPILPALLTTIDLCRRASIPVFFTrhSHKSPSDYGmlgewwdgdLILDGTTEAELMPE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767231942  89 LT-PKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDA 154
Cdd:PLN02621   95 IGrVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDA 161
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 21-172 1.98e-48

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: 154.67  E-value: 1.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  21 VLVIIDAQGEYAEGKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPlFTQGTKLAEIFDELTPKEGEAVVTK 100
Cdd:cd01014     1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGS-FAPGSEGWEIHPELAPLEGETVIEK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767231942 101 HHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPG----VDAAQLVKVA 172
Cdd:cd01014    80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDhggvLSAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 21-184 1.25e-47

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: 153.14  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  21 VLVIIDAQGEYAE-GKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPLFT----------QGTKLAEIFDEL 89
Cdd:COG1335     1 ALLVIDVQNDFVPpGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTPGAELVPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  90 TPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPGVDAaqlv 169
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEA---- 156

                         170
                  ....*....|....*
gi 1767231942 170 kvALAEIADVFGTLV 184
Cdd:COG1335   157 --ALARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 21-166 1.30e-44

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: 145.10  E-value: 1.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  21 VLVIIDAQGEYAEGKLKI-SNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAP---------LFTQGTKLAEIFDELT 90
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLlPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPefaellwppHCVKGTEGAELVPELA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767231942  91 PKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPGVDAA 166
Cdd:cd00431    81 PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAA 156
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 20-186 2.16e-42

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 139.85  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  20 SVLVIIDAQ-GEYAEGKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPLFT----------QGTKLAEIFDE 88
Cdd:pfam00857   1 TALLVIDMQnDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFAlkdrpspafpPGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  89 LTPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPGVDAaql 168
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA--- 157

                         170
                  ....*....|....*...
gi 1767231942 169 vkvALAEIADVFGTLVSS 186
Cdd:pfam00857 158 ---ALERLAQRGAEVTTT 172
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
20-189 3.63e-24

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 94.15  E-value: 3.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  20 SVLVIIDAQ----GEYAEGKlkiSNIEASRPNISSLLEKYRAANAPIVHVVH---ETPAGAPLF--------TQGTKLAE 84
Cdd:COG1535    20 AALLIHDMQnyflRPYDPDE---PPIRELVANIARLRDACRAAGIPVVYTAQpgdQTPEDRGLLndfwgpglTAGPEGQE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  85 IFDELTPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDipgvd 164
Cdd:COG1535    97 IVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFS----- 171

                         170       180
                  ....*....|....*....|....*
gi 1767231942 165 aAQLVKVALAEIADVFGTLVSSKDI 189
Cdd:COG1535   172 -REEHRMALEYVAGRCGVVVTTDEV 195
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 22-188 3.78e-19

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: 80.14  E-value: 3.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  22 LVIIDAQGEYAE-GKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAP-------------LFTQGTKLAEIFD 87
Cdd:cd01015     2 LLVIDLVEGYTQpGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTVVYDPDGAdgglwarkvpamsDLVEGSPLAAICD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  88 ELTPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRdipgvdAAQ 167
Cdd:cd01015    82 ELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDR------APA 155

                         170       180
                  ....*....|....*....|.
gi 1767231942 168 LVKVALAEIADVFGTLVSSKD 188
Cdd:cd01015   156 PHEANLFDIDNKYGDVVSTDD 176
PLN02621 PLN02621
nicotinamidase
 20-154 1.15e-16

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 74.05  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  20 SVLVIIDAQGEYAegklkiSNIEASRPNISSLLEKYRAANAPIVHV--VHETPAGAP---------LFTQGTKLAEIFDE 88
Cdd:PLN02621   21 AALLVIDMQNYFS------SMAEPILPALLTTIDLCRRASIPVFFTrhSHKSPSDYGmlgewwdgdLILDGTTEAELMPE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767231942  89 LT-PKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDA 154
Cdd:PLN02621   95 IGrVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDA 161
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 21-158 1.29e-14

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: 67.62  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  21 VLVIIDAQGEYAEGklkISNIEASRPNISSLLEKYRAANAPIVHVVHETpagaplftqgTKLAEIFDELTPKEGEA-VVT 99
Cdd:cd01012     1 ALLLVDVQEKLAPA---IKSFDELINNTVKLAKAAKLLDVPVILTEQYP----------KGLGPTVPELREVFPDApVIE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1767231942 100 KHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDR 158
Cdd:cd01012    68 KTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSR 126
PRK11440 PRK11440
putative hydrolase; Provisional
 7-154 2.54e-10

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 57.05  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942   7 MLGVPPSTastqdSVLVIIDAQG---EYAEGKLKISNIEASRpniSSLLEKYRAANAPIVHV----------VHETPAGA 73
Cdd:PRK11440    1 MLELNAKT-----TALVVIDLQEgilPFAGGPHTADEVVARA---ARLAAKFRASGSPVVLVrvgwsadyaeALKQPVDA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  74 PlfTQGTKLAEIF----DELTPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVI 149
Cdd:PRK11440   73 P--SPAKVLPENWwqhpAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLV 150


                  ....*
gi 1767231942 150 VAEDA 154
Cdd:PRK11440  151 IAEDA 155
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 47-157 5.59e-10

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: 56.19  E-value: 5.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  47 NISSLLEKYRAANAPIVHVV---HETPAG--------APLFTQGTKLAEIFDELTPKEGEAVVTKHHPGSFADTNLQEIL 115
Cdd:cd01013    58 NIARLRDWCRQAGIPVVYTAqpgNQTPEQrallndfwGPGLTASPEETKIVTELAPQPDDTVLTKWRYSAFKRSPLLERL 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1767231942 116 EKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGD 157
Cdd:cd01013   138 KESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIAD 179
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 11-189 1.60e-08

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 52.38  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  11 PPSTASTQDSVLVIIDAQGEYAE-GKLKISNIEASRPNISSLlekyRAANA-----------PIVHVVHETPAGAPLFT- 77
Cdd:PTZ00331    4 SCITVSSTNDALIIVDVQNDFCKgGSLAVPDAEEVIPVINQV----RQSHHfdlvvatqdwhPPNHISFASNHGKPKILp 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  78 -------------QGTKLAEIFDELTPKEGEAVVTKhhpG---------SFAD-----TNLQEILEKSGKKKIVLVGYMA 130
Cdd:PTZ00331   80 dgttqglwpphcvQGTKGAQLHKDLVVERIDIIIRK---GtnrdvdsysAFDNdkgskTGLAQILKAHGVRRVFICGLAF 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1767231942 131 HVCVSTTARQGAQRGWDVIVAEDAVGdrdipGVDAAQlVKVALAEIADVFGTLVSSKDI 189
Cdd:PTZ00331  157 DFCVLFTALDAVKLGFKVVVLEDATR-----AVDPDA-ISKQRAELLEAGVILLTSSDL 209
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 78-166 7.58e-07

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: 47.26  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231942  78 QGTKLAEIFDELTPKEGEAVVTK------------HHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRG 145
Cdd:cd01011    84 QGTPGAELHPGLPVPDIDLIVRKgtnpdidsysafFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALDALKAG 163

                          90       100
                  ....*....|....*....|.
gi 1767231942 146 WDVIVAEDAVGDRDIPGVDAA 166
Cdd:cd01011   164 FEVRVLEDACRAVDPETIERA 184
 
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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