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Conserved domains on  [gi|1730650594|gb|TYG26181|]
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isochorismatase [Klebsiella grimontii]

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 ...
 6-141 5.56e-33

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: 115.39  E-value: 5.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   6 VVMVVDMQNGVF---ATPRIERERCAAQINRLIDAA----DTVVFIQHSEEGGLEEGSEG-------------FALLPEL 65
Cdd:COG1335     1 ALLVIDVQNDFVppgALAVPGADAVVANIARLLAAAraagVPVIHTRDWHPPDGSEFAEFdlwpphcvpgtpgAELVPEL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730650594  66 HQPAGALFVTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTANRPAAQA 141
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEA 156
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 6-141 5.56e-33

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: 115.39  E-value: 5.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   6 VVMVVDMQNGVF---ATPRIERERCAAQINRLIDAA----DTVVFIQHSEEGGLEEGSEG-------------FALLPEL 65
Cdd:COG1335     1 ALLVIDVQNDFVppgALAVPGADAVVANIARLLAAAraagVPVIHTRDWHPPDGSEFAEFdlwpphcvpgtpgAELVPEL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730650594  66 HQPAGALFVTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTANRPAAQA 141
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEA 156
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 8-148 9.21e-32

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: 111.91  E-value: 9.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   8 MVVDMQNGVFATPRIER--ERCAAQINRLIDAADT----VVFIQHSEEGGLEEGS--EGFALLPELHQPAGALFVTKTAC 79
Cdd:cd01014     3 LVIDVQNGYFDGGLPPLnnEAALENIAALIAAARAagipVIHVRHIDDEGGSFAPgsEGWEIHPELAPLEGETVIEKTVP 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730650594  80 DAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTANRPAAQ----AVTLIAHY 148
Cdd:cd01014    83 NAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGgvlsAEEIHAHY 155
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 9-141 3.77e-24

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 92.85  E-value: 3.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   9 VVDMQNGVFATPRIERERCAA---QINRLIDAADT----VVFIQHSEEGGLEEGSEGF-------------ALLPELHQP 68
Cdd:pfam00857   5 VIDMQNDFVDSGGPKVEGIAAileNINRLLKAARKagipVIFTRQVPEPDDADFALKDrpspafppgttgaELVPELAPL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730650594  69 AGALFVTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTANRPAAQA 141
Cdd:pfam00857  85 PGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
60-129 1.01e-08

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 52.69  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594  60 ALLPELHQPAGALFVTK---TACD---AFY------RTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVA 127
Cdd:PRK11609   94 ALHPLLNQKAIDAVFHKgenPLIDsysAFFdnghrqKTALDDWLREHGITELIVMGLATDYCVKFTVLDALALGYQVNVI 173


                  ..
gi 1730650594 128 ED 129
Cdd:PRK11609  174 TD 175
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 6-141 5.56e-33

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: 115.39  E-value: 5.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   6 VVMVVDMQNGVF---ATPRIERERCAAQINRLIDAA----DTVVFIQHSEEGGLEEGSEG-------------FALLPEL 65
Cdd:COG1335     1 ALLVIDVQNDFVppgALAVPGADAVVANIARLLAAAraagVPVIHTRDWHPPDGSEFAEFdlwpphcvpgtpgAELVPEL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730650594  66 HQPAGALFVTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTANRPAAQA 141
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEA 156
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 8-148 9.21e-32

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: 111.91  E-value: 9.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   8 MVVDMQNGVFATPRIER--ERCAAQINRLIDAADT----VVFIQHSEEGGLEEGS--EGFALLPELHQPAGALFVTKTAC 79
Cdd:cd01014     3 LVIDVQNGYFDGGLPPLnnEAALENIAALIAAARAagipVIHVRHIDDEGGSFAPgsEGWEIHPELAPLEGETVIEKTVP 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730650594  80 DAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTANRPAAQ----AVTLIAHY 148
Cdd:cd01014    83 NAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGgvlsAEEIHAHY 155
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 6-141 5.96e-28

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: 101.96  E-value: 5.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   6 VVMVVDMQNGVF---ATPRIERERCAAQINRLIDAADT----VVFIQHSEEGGLEEGSEGF------------ALLPELH 66
Cdd:cd00431     1 ALLVVDMQNDFVpggGLLLPGADELVPNINRLLAAARAagipVIFTRDWHPPDDPEFAELLwpphcvkgtegaELVPELA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730650594  67 QPAGALFVTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTANRPAAQA 141
Cdd:cd00431    81 PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEA 155
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 9-141 3.77e-24

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 92.85  E-value: 3.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   9 VVDMQNGVFATPRIERERCAA---QINRLIDAADT----VVFIQHSEEGGLEEGSEGF-------------ALLPELHQP 68
Cdd:pfam00857   5 VIDMQNDFVDSGGPKVEGIAAileNINRLLKAARKagipVIFTRQVPEPDDADFALKDrpspafppgttgaELVPELAPL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730650594  69 AGALFVTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTANRPAAQA 141
Cdd:pfam00857  85 PGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 4-130 2.48e-11

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: 59.58  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   4 KRVVMVVDMQN-----GVFATPriERERCAAQINRLIDAA--DTVVFIQ-------------HSEEGGLEEGSEGF---- 59
Cdd:cd01011     1 TDALLVVDVQNdfcpgGALAVP--GGDAIVPLINALLSLFqyDLVVATQdwhpanhasfasnHPGQMPFITLPPGPqvlw 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594  60 -----------ALLPELHQPAGALFVTK---------TAC---DAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKN 116
Cdd:cd01011    79 pdhcvqgtpgaELHPGLPVPDIDLIVRKgtnpdidsySAFfdnDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158

                         170
                  ....*....|....
gi 1730650594 117 GASRGYAITVAEDA 130
Cdd:cd01011   159 ALKAGFEVRVLEDA 172
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
60-129 1.01e-08

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 52.69  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594  60 ALLPELHQPAGALFVTK---TACD---AFY------RTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVA 127
Cdd:PRK11609   94 ALHPLLNQKAIDAVFHKgenPLIDsysAFFdnghrqKTALDDWLREHGITELIVMGLATDYCVKFTVLDALALGYQVNVI 173


                  ..
gi 1730650594 128 ED 129
Cdd:PRK11609  174 TD 175
PRK11440 PRK11440
putative hydrolase; Provisional
 74-136 2.97e-08

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 50.88  E-value: 2.97e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730650594  74 VTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTANR 136
Cdd:PRK11440   99 VTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASA 161
PLN02621 PLN02621
nicotinamidase
 61-135 9.66e-08

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 49.78  E-value: 9.66e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730650594  61 LLPELHQPAGA-LFVTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDAHTTAN 135
Cdd:PLN02621   91 LMPEIGRVTGPdEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN 166
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 85-130 4.56e-07

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 47.75  E-value: 4.56e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1730650594  85 TRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDA 130
Cdd:PTZ00331  135 TGLAQILKAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDA 180
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 60-130 4.41e-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: 42.00  E-value: 4.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730650594  60 ALLPELHQPAGALFVTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDA 130
Cdd:cd01015    78 AICDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVREC 148
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-130 1.57e-04

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 40.60  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594   3 AKRVVMVVDMQNgVFATPRIERERCAAQ----INRLIDAADT----VVFIQHSEEGGLE--------------EGSEGFA 60
Cdd:COG1535    18 ARAALLIHDMQN-YFLRPYDPDEPPIRElvanIARLRDACRAagipVVYTAQPGDQTPEdrgllndfwgpgltAGPEGQE 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730650594  61 LLPELHQPAGALFVTKTACDAFYRTRLEAVLREHHITEFVICGCATDYCVDTTIKNGASRGYAITVAEDA 130
Cdd:COG1535    97 IVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADA 166
 
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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