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Conserved domains on  [gi|933608745|ref|WP_054317795|]
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isochorismatase family protein [Burkholderia multivorans]

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 ...
 29-200 1.84e-77

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 cd01015:

Pssm-ID: 444760 [Multi-domain]  Cd Length: 179  Bit Score: 230.75  E-value: 1.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDDNVFSLKVPGMATLTEHHPNSAIV 108
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTVVYDPDGADGGLWARKVPAMSDLVEGSPLAAIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 109 PELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIAPHEAN 188
Cdd:cd01015   81 DELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAPHEAN 160

                        170
                 ....*....|..
gi 933608745 189 LFDMQQKYAAVM 200
Cdd:cd01015  161 LFDIDNKYGDVV 172
 
Name Accession Description Interval E-value
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 29-200 1.84e-77

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: 230.75  E-value: 1.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDDNVFSLKVPGMATLTEHHPNSAIV 108
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTVVYDPDGADGGLWARKVPAMSDLVEGSPLAAIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 109 PELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIAPHEAN 188
Cdd:cd01015   81 DELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAPHEAN 160

                        170
                 ....*....|..
gi 933608745 189 LFDMQQKYAAVM 200
Cdd:cd01015  161 LFDIDNKYGDVV 172
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 29-200 8.07e-50

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: 160.07  E-value: 8.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDDNVFSLKVPGmatLTEHHPNSAIV 108
Cdd:COG1335    1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPH---CVPGTPGAELV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 109 PELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIAPHEAN 188
Cdd:COG1335   78 PELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAA 157

                        170
                 ....*....|..
gi 933608745 189 LFDMQQKYAAVM 200
Cdd:COG1335  158 LARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 29-200 3.44e-41

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 138.31  E-value: 3.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745   29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDdnvFSLKVPGMATLTEHHPNSAIV 108
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDAD---FALKDRPSPAFPPGTTGAELV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  109 PELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIAPHEAN 188
Cdd:pfam00857  79 PELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAA 158

                         170
                  ....*....|..
gi 933608745  189 LFDMQQKYAAVM 200
Cdd:pfam00857 159 LERLAQRGAEVT 170
PLN02621 PLN02621
nicotinamidase
 13-197 2.07e-10

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 57.87  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  13 YREQGFGTPLPPQGNLALLIVD---FVVGFADPatfgggnIAPAIARTtqaLAIARQRGWPVAHSRIVYADDgSDDNVFS 89
Cdd:PLN02621   6 YKKYETRKRDPDPKQAALLVIDmqnYFSSMAEP-------ILPALLTT---IDLCRRASIPVFFTRHSHKSP-SDYGMLG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  90 LKVPGMATLtEHHPNSAIVPELTPARG-ELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGF 168
Cdd:PLN02621  75 EWWDGDLIL-DGTTEAELMPEIGRVTGpDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGF 153

                        170       180
                 ....*....|....*....|....*....
gi 933608745 169 RPLVLADCVGDRAIAPHEANLFDMQQKYA 197
Cdd:PLN02621 154 RVFFSTDATATANEELHEATLKNLAYGFA 182
 
Name Accession Description Interval E-value
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 29-200 1.84e-77

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: 230.75  E-value: 1.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDDNVFSLKVPGMATLTEHHPNSAIV 108
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTVVYDPDGADGGLWARKVPAMSDLVEGSPLAAIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 109 PELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIAPHEAN 188
Cdd:cd01015   81 DELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAPHEAN 160

                        170
                 ....*....|..
gi 933608745 189 LFDMQQKYAAVM 200
Cdd:cd01015  161 LFDIDNKYGDVV 172
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 29-200 8.07e-50

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: 160.07  E-value: 8.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDDNVFSLKVPGmatLTEHHPNSAIV 108
Cdd:COG1335    1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPH---CVPGTPGAELV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 109 PELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIAPHEAN 188
Cdd:COG1335   78 PELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAA 157

                        170
                 ....*....|..
gi 933608745 189 LFDMQQKYAAVM 200
Cdd:COG1335  158 LARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 29-200 3.44e-41

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 138.31  E-value: 3.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745   29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDdnvFSLKVPGMATLTEHHPNSAIV 108
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDAD---FALKDRPSPAFPPGTTGAELV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  109 PELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIAPHEAN 188
Cdd:pfam00857  79 PELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAA 158

                         170
                  ....*....|..
gi 933608745  189 LFDMQQKYAAVM 200
Cdd:pfam00857 159 LERLAQRGAEVT 170
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 29-192 8.25e-41

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: 137.01  E-value: 8.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDDNVFslkvPGMATLTEHHPNSAIV 108
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL----LWPPHCVKGTEGAELV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 109 PELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIAPHEAN 188
Cdd:cd00431   77 PELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAA 156


                 ....
gi 933608745 189 LFDM 192
Cdd:cd00431  157 LERL 160
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
29-200 2.70e-34

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 121.50  E-value: 2.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDDNVFSLKV-PGMATLTEHHpnsAI 107
Cdd:COG1535   21 ALLIHDMQNYFLRPYDPDEPPIRELVANIARLRDACRAAGIPVVYTAQPGDQTPEDRGLLNDFWgPGLTAGPEGQ---EI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 108 VPELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIAPHEA 187
Cdd:COG1535   98 VDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSREEHRM 177

                        170
                 ....*....|...
gi 933608745 188 NLFDMQQKYAAVM 200
Cdd:COG1535  178 ALEYVAGRCGVVV 190
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 29-176 4.33e-24

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: 93.42  E-value: 4.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADPAtFGGGNIAPAIARTTQALAIARQRGWPVAHSRivyaDDGSDDNVFslkVPGMatltehhPNSAIV 108
Cdd:cd01014    1 ALLVIDVQNGYFDGG-LPPLNNEAALENIAALIAAARAAGIPVIHVR----HIDDEGGSF---APGS-------EGWEIH 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933608745 109 PELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADC 176
Cdd:cd01014   66 PELAPLEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADA 133
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 29-185 1.31e-15

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: 72.30  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADP---ATFGGGNIAPAIARTTQALAIARQ---RGW-PVAHsrIVYADDGSDDNVFSLKVPGMATLTEH 101
Cdd:cd01011    3 ALLVVDVQNDFCPGgalAVPGGDAIVPLINALLSLFQYDLVvatQDWhPANH--ASFASNHPGQMPFITLPPGPQVLWPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 102 H-----PNSAIVPELTPARGELVVRK-TVP-----SAFFG------TQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAM 164
Cdd:cd01011   81 HcvqgtPGAELHPGLPVPDIDLIVRKgTNPdidsySAFFDndrrssTGLAEYLRERGIDRVDVVGLATDYCVKATALDAL 160

                        170       180
                 ....*....|....*....|.
gi 933608745 165 SHGFRPLVLADCVgdRAIAPH 185
Cdd:cd01011  161 KAGFEVRVLEDAC--RAVDPE 179
PLN02621 PLN02621
nicotinamidase
 13-197 2.07e-10

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 57.87  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  13 YREQGFGTPLPPQGNLALLIVD---FVVGFADPatfgggnIAPAIARTtqaLAIARQRGWPVAHSRIVYADDgSDDNVFS 89
Cdd:PLN02621   6 YKKYETRKRDPDPKQAALLVIDmqnYFSSMAEP-------ILPALLTT---IDLCRRASIPVFFTRHSHKSP-SDYGMLG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  90 LKVPGMATLtEHHPNSAIVPELTPARG-ELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGF 168
Cdd:PLN02621  75 EWWDGDLIL-DGTTEAELMPEIGRVTGpDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGF 153

                        170       180
                 ....*....|....*....|....*....
gi 933608745 169 RPLVLADCVGDRAIAPHEANLFDMQQKYA 197
Cdd:PLN02621 154 RVFFSTDATATANEELHEATLKNLAYGFA 182
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 29-198 1.70e-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: 55.42  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFADPATFGGGNIAPAIARTTQALAIARQRGWPVAHSrivyADDGS-DDNVFSLKV----PGMATLTEHHp 103
Cdd:cd01013   31 VLLVHDMQRYFLDFYDESAEPVPQLIANIARLRDWCRQAGIPVVYT----AQPGNqTPEQRALLNdfwgPGLTASPEET- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 104 nsAIVPELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRPLVLADCVGDRAIA 183
Cdd:cd01013  106 --KIVTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADFSLE 183

                        170
                 ....*....|....*
gi 933608745 184 PHeanlfDMQQKYAA 198
Cdd:cd01013  184 EH-----RMALKYAA 193
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 90-200 1.61e-08

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: 51.83  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  90 LKVPgmATLTEHHP--NSAIVPELTP-ARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSH 166
Cdd:cd01012   35 LDVP--VILTEQYPkgLGPTVPELREvFPDAPVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEE 112

                         90       100       110
                 ....*....|....*....|....*....|....
gi 933608745 167 GFRPLVLADCVGDRAIAPHEANLFDMQQKYAAVM 200
Cdd:cd01012  113 GYEVFVVADACGSRSKEDHELALARMRQAGAVLT 146
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
100-202 6.85e-06

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 45.37  E-value: 6.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 100 EHHPNSAIVPELTPARGELVVRK-TVP-----SAFFG------TQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHG 167
Cdd:PRK11609  88 QNSEGAALHPLLNQKAIDAVFHKgENPlidsySAFFDnghrqkTALDDWLREHGITELIVMGLATDYCVKFTVLDALALG 167

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 933608745 168 FRPLVLAD-CVGDRaIAPHEAN--LFDMQQKYAAVMPL 202
Cdd:PRK11609 168 YQVNVITDgCRGVN-LQPQDSAhaFMEMSAAGATLYTL 204
PRK11440 PRK11440
putative hydrolase; Provisional
 29-175 2.91e-05

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 43.18  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  29 ALLIVDFVVGFAdPATFGGGNIAPAIARTTQALAIARQRGWPVAHSRIVYADDGSDdnvfSLKVP-----GMATLTE--- 100
Cdd:PRK11440  10 ALVVIDLQEGIL-PFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSADYAE----ALKQPvdapsPAKVLPEnww 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933608745 101 HHPnsaivPELTPARGELVVRKTVPSAFFGTQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDAMSHGFRpLVLAD 175
Cdd:PRK11440  85 QHP-----AALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFN-LVIAE 153
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 27-184 7.18e-05

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 42.36  E-value: 7.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  27 NLALLIVDFVVGFADPATF---GGGNIAPAIARTTQALA---IARQRGW-PVAHsrIVYADDGSDDNVFSLKVPGMatLT 99
Cdd:PTZ00331  12 NDALIIVDVQNDFCKGGSLavpDAEEVIPVINQVRQSHHfdlVVATQDWhPPNH--ISFASNHGKPKILPDGTTQG--LW 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745 100 EHH-----PNSAIVPELTPARGELVVRKTVP------SAFFG-----TQLAPWLAQRAVQTLLVAGAVTSGCVRASVVDA 163
Cdd:PTZ00331  88 PPHcvqgtKGAQLHKDLVVERIDIIIRKGTNrdvdsySAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTALDA 167

                        170       180
                 ....*....|....*....|.
gi 933608745 164 MSHGFRPLVLADCVgdRAIAP 184
Cdd:PTZ00331 168 VKLGFKVVVLEDAT--RAVDP 186
PLN02743 PLN02743
nicotinamidase
 21-170 4.03e-04

nicotinamidase


Pssm-ID: 215396  Cd Length: 239  Bit Score: 40.49  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  21 PLPPQGNLALLIVDFVVGFAdpaTFGGGNIAP-----AIARTT-QALAIARQ---RGWPVahsrivyaddgsddnvfslk 91
Cdd:PLN02743  21 VLNGDVRTGLVLVDEVNGFC---TVGAGNLAPrepdkQISKMVdESARLAREfceRKWPV-------------------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933608745  92 vpgMATLTEHHPN----------------SAIVPELTPARGE---LVVRKTVPSAFFGT-------QLAPWLAQRAVQTL 145
Cdd:PLN02743  78 ---LAFLDSHHPDkpehpypphcivgtgeENLVPALQWLENDpnvTLRRKDCIDGFVGAiekdgsnVFVDWVNNNKIKVI 154

                        170       180
                 ....*....|....*....|....*...
gi 933608745 146 LVAGAVTSGCVRASVVDAMS---HGFRP 170
Cdd:PLN02743 155 LVVGICTDICVLDFVASALSarnHGILP 182
 
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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