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Conserved domains on  [gi|1865329584|gb|QLD08099|]
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isochorismatase family protein [Citrobacter freundii]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 726)

cysteine hydrolase family protein, such as isochorismatase and nicotinamidase, catalyzes the hydrolysis of a chemical bond using an active site cysteinyl residue

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cysteine_hydrolases super family cl00220
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
20-180 1.10e-54

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.


The actual alignment was detected with superfamily member cd01012:

Pssm-ID: 444760 [Multi-domain]  Cd Length: 157  Bit Score: 172.01  E-value: 1.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  20 VMLLIDHQSGLFQTVGDMPmpELRARAAALAKMATLAKIPVITTASVPqGPNGPLIPEIHANAPHAQYVARKGeINAWDN 99
Cdd:cd01012     1 ALLLVDVQEKLAPAIKSFD--ELINNTVKLAKAAKLLDVPVILTEQYP-KGLGPTVPELREVFPDAPVIEKTS-FSCWED 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584 100 EDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEITLARVVQAGVVPMDTAAVASEIQ 179
Cdd:cd01012    77 EAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQ 156

                  .
gi 1865329584 180 G 180
Cdd:cd01012   157 R 157
 
Name Accession Description Interval E-value
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
20-180 1.10e-54

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: 172.01  E-value: 1.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  20 VMLLIDHQSGLFQTVGDMPmpELRARAAALAKMATLAKIPVITTASVPqGPNGPLIPEIHANAPHAQYVARKGeINAWDN 99
Cdd:cd01012     1 ALLLVDVQEKLAPAIKSFD--ELINNTVKLAKAAKLLDVPVILTEQYP-KGLGPTVPELREVFPDAPVIEKTS-FSCWED 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584 100 EDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEITLARVVQAGVVPMDTAAVASEIQ 179
Cdd:cd01012    77 EAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQ 156

                  .
gi 1865329584 180 G 180
Cdd:cd01012   157 R 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
20-169 3.34e-22

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: 88.81  E-value: 3.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  20 VMLLIDHQSGLFQTvGDMPMPELRARAAALAKMATLAK---IPVITT-------------------ASVPQGPNGPLIPE 77
Cdd:COG1335     1 ALLVIDVQNDFVPP-GALAVPGADAVVANIARLLAAARaagVPVIHTrdwhppdgsefaefdlwppHCVPGTPGAELVPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  78 IHANAphAQYVARKGEINAWDNEDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEIT 157
Cdd:COG1335    80 LAPLP--GDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAA 157
                         170
                  ....*....|..
gi 1865329584 158 LARVVQAGVVPM 169
Cdd:COG1335   158 LARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
19-172 5.78e-17

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 75.13  E-value: 5.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  19 SVMLLIDHQSGLFQTVGDmPMPELRARAAALAKMATLAK---IPVITT------------------ASVPQGPNGP-LIP 76
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGP-KVEGIAAILENINRLLKAARkagIPVIFTrqvpepddadfalkdrpsPAFPPGTTGAeLVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  77 EIHANAPHaqYVARKGEINAWDNEDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEI 156
Cdd:pfam00857  80 ELAPLPGD--LVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157
                         170
                  ....*....|....*.
gi 1865329584 157 TLARVVQAGVVPMDTA 172
Cdd:pfam00857 158 ALERLAQRGAEVTTTE 173
PLN02621 PLN02621
nicotinamidase
19-159 2.33e-06

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 46.70  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  19 SVMLLIDHQsGLFQTVGDMPMPELRARAAalakMATLAKIPVITTASVPQGP----------NGPLI----------PEI 78
Cdd:PLN02621   21 AALLVIDMQ-NYFSSMAEPILPALLTTID----LCRRASIPVFFTRHSHKSPsdygmlgewwDGDLIldgtteaelmPEI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  79 HANAPhAQYVARKGEINAWDNEDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEITL 158
Cdd:PLN02621   96 GRVTG-PDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEATL 174

                  .
gi 1865329584 159 A 159
Cdd:PLN02621  175 K 175
 
Name Accession Description Interval E-value
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
20-180 1.10e-54

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: 172.01  E-value: 1.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  20 VMLLIDHQSGLFQTVGDMPmpELRARAAALAKMATLAKIPVITTASVPqGPNGPLIPEIHANAPHAQYVARKGeINAWDN 99
Cdd:cd01012     1 ALLLVDVQEKLAPAIKSFD--ELINNTVKLAKAAKLLDVPVILTEQYP-KGLGPTVPELREVFPDAPVIEKTS-FSCWED 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584 100 EDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEITLARVVQAGVVPMDTAAVASEIQ 179
Cdd:cd01012    77 EAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQ 156

                  .
gi 1865329584 180 G 180
Cdd:cd01012   157 R 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
20-169 3.34e-22

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: 88.81  E-value: 3.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  20 VMLLIDHQSGLFQTvGDMPMPELRARAAALAKMATLAK---IPVITT-------------------ASVPQGPNGPLIPE 77
Cdd:COG1335     1 ALLVIDVQNDFVPP-GALAVPGADAVVANIARLLAAARaagVPVIHTrdwhppdgsefaefdlwppHCVPGTPGAELVPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  78 IHANAphAQYVARKGEINAWDNEDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEIT 157
Cdd:COG1335    80 LAPLP--GDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAA 157
                         170
                  ....*....|..
gi 1865329584 158 LARVVQAGVVPM 169
Cdd:COG1335   158 LARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
20-161 1.72e-21

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: 86.94  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  20 VMLLIDHQSGLFQTVGDM--PMPELRARAAALAKMATLAKIPVITT------------------ASVPQGPNGPLIPEIh 79
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLlpGADELVPNINRLLAAARAAGIPVIFTrdwhppddpefaellwppHCVKGTEGAELVPEL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  80 ANAPHAQYVaRKGEINAWDNEDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEITLA 159
Cdd:cd00431    80 APLPDDLVI-EKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALE 158

                  ..
gi 1865329584 160 RV 161
Cdd:cd00431   159 RL 160
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
19-172 5.78e-17

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 75.13  E-value: 5.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  19 SVMLLIDHQSGLFQTVGDmPMPELRARAAALAKMATLAK---IPVITT------------------ASVPQGPNGP-LIP 76
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGP-KVEGIAAILENINRLLKAARkagIPVIFTrqvpepddadfalkdrpsPAFPPGTTGAeLVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  77 EIHANAPHaqYVARKGEINAWDNEDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEI 156
Cdd:pfam00857  80 ELAPLPGD--LVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157
                         170
                  ....*....|....*.
gi 1865329584 157 TLARVVQAGVVPMDTA 172
Cdd:pfam00857 158 ALERLAQRGAEVTTTE 173
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
22-158 5.40e-10

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: 56.06  E-value: 5.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  22 LLIDHQSGLFqTVGDMP--MPELRARAAALAKMATLAKIPVI--------TTASVPQGPNGPLIPEIHAnaPHAQYVARK 91
Cdd:cd01014     3 LVIDVQNGYF-DGGLPPlnNEAALENIAALIAAARAAGIPVIhvrhiddeGGSFAPGSEGWEIHPELAP--LEGETVIEK 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1865329584  92 GEINAWDNEDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEITL 158
Cdd:cd01014    80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVL 146
PLN02621 PLN02621
nicotinamidase
19-159 2.33e-06

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 46.70  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  19 SVMLLIDHQsGLFQTVGDMPMPELRARAAalakMATLAKIPVITTASVPQGP----------NGPLI----------PEI 78
Cdd:PLN02621   21 AALLVIDMQ-NYFSSMAEPILPALLTTID----LCRRASIPVFFTRHSHKSPsdygmlgewwDGDLIldgtteaelmPEI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  79 HANAPhAQYVARKGEINAWDNEDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEITL 158
Cdd:PLN02621   96 GRVTG-PDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEATL 174

                  .
gi 1865329584 159 A 159
Cdd:PLN02621  175 K 175
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
107-177 3.96e-06

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 46.21  E-value: 3.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865329584 107 KATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEITLARVVQAGVVPMDTAAVASE 177
Cdd:PTZ00331  142 KAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELLEAGVILLTSSDLVAS 212
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
66-167 3.83e-05

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: 43.02  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  66 VPQGPNGPLIPEIHAnaPHAQYVARKG---EINA----WDNEDFVK-----AVKATGRKTLIIAGTITSVCMAFPAISAV 133
Cdd:cd01011    83 VQGTPGAELHPGLPV--PDIDLIVRKGtnpDIDSysafFDNDRRSStglaeYLRERGIDRVDVVGLATDYCVKATALDAL 160
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1865329584 134 AEGYKVFAVIDASGTYSKMAQEITLARVVQAGVV 167
Cdd:cd01011   161 KAGFEVRVLEDACRAVDPETIERAIEEMKEAGVV 194
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
107-174 1.88e-04

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 40.99  E-value: 1.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1865329584 107 KATGRKTLIIAGTITSVCMAFPAISAVAEGYKVFAVIDASGTYSKMAQEITLARVVQ-AGVVpMDTAAV 174
Cdd:COG1535   128 RELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSREEHRMALEYVAGrCGVV-VTTDEV 195
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
57-147 3.19e-03

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: 37.38  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865329584  57 KIPVITTASVPQgpngPLIPEIHANAPHA-QYVARKGEINAWDNEDFVKAVKATGRKTLIIAGTITSVCMAFPAISAVAE 135
Cdd:cd01015    63 KVPAMSDLVEGS----PLAAICDELAPQEdEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQH 138
                          90
                  ....*....|..
gi 1865329584 136 GYKVFAVIDASG 147
Cdd:cd01015   139 GFRPIVVRECVG 150
 
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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