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Conserved domains on  [gi|507015254|ref|WP_016088756|]
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cysteine hydrolase family protein [Bacillus sp. dmp10]

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 ...
 6-163 1.26e-54

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: 170.85  E-value: 1.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAFQLPYWGERNNLFAEENMRMLLAEWRKRKRPVFHIQHVNKENaqSMFYEGAETVNFKEELKPLPGEVIIQ 85
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEG--GSFAPGSEGWEIHPELAPLEGETVIE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507015254  86 KSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNRKGlDGKEYNAEDIHNMT 163
Cdd:cd01014   79 KTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPD-HGGVLSAEEIHAHY 155
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 6-163 1.26e-54

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: 170.85  E-value: 1.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAFQLPYWGERNNLFAEENMRMLLAEWRKRKRPVFHIQHVNKENaqSMFYEGAETVNFKEELKPLPGEVIIQ 85
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEG--GSFAPGSEGWEIHPELAPLEGETVIE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507015254  86 KSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNRKGlDGKEYNAEDIHNMT 163
Cdd:cd01014   79 KTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPD-HGGVLSAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 6-175 3.50e-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: 159.68  E-value: 3.50e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAF-QLPYWGERNNLFAEENMRMLLAEWRKRKRPVFHIQHVNKENAQSM---------FYEGAETVNFKEEL 75
Cdd:COG1335    1 ALLVIDVQNDFvPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFaefdlwpphCVPGTPGAELVPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  76 KPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNrkgldgkeyn 155
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRD---------- 150

                        170       180
                 ....*....|....*....|
gi 507015254 156 aEDIHNMTLVNLHEEFATIV 175
Cdd:COG1335  151 -PEAHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 6-177 6.30e-37

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 126.36  E-value: 6.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254    6 ALIIIDVQKAFqLPYWGERNNLFAE--ENMRMLLAEWRKRKRPVFHIQHVNKENAQSM---------FYEGAETVNFKEE 74
Cdd:pfam00857   2 ALLVIDMQNDF-VDSGGPKVEGIAAilENINRLLKAARKAGIPVIFTRQVPEPDDADFalkdrpspaFPPGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   75 LKPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNrkgldgkey 154
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLS--------- 151

                         170       180
                  ....*....|....*....|...
gi 507015254  155 naEDIHNMTLVNLHEEFATIVTT 177
Cdd:pfam00857 152 --PEAHDAALERLAQRGAEVTTT 172
PLN02621 PLN02621
nicotinamidase
 6-175 5.00e-20

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 83.29  E-value: 5.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAFQ------LPywgernnlfaeeNMRMLLAEWRKRKRPVFHIQHVNKENAQ-SMFYE----------GAET 68
Cdd:PLN02621  22 ALLVIDMQNYFSsmaepiLP------------ALLTTIDLCRRASIPVFFTRHSHKSPSDyGMLGEwwdgdlildgTTEA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  69 VNFKEELKPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNrkg 148
Cdd:PLN02621  90 ELMPEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN--- 166

                        170       180
                 ....*....|....*....|....*..
gi 507015254 149 ldgkeynaEDIHNMTLVNLHEEFATIV 175
Cdd:PLN02621 167 --------EELHEATLKNLAYGFAYLV 185
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 6-163 1.26e-54

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: 170.85  E-value: 1.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAFQLPYWGERNNLFAEENMRMLLAEWRKRKRPVFHIQHVNKENaqSMFYEGAETVNFKEELKPLPGEVIIQ 85
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEG--GSFAPGSEGWEIHPELAPLEGETVIE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507015254  86 KSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNRKGlDGKEYNAEDIHNMT 163
Cdd:cd01014   79 KTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPD-HGGVLSAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 6-175 3.50e-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: 159.68  E-value: 3.50e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAF-QLPYWGERNNLFAEENMRMLLAEWRKRKRPVFHIQHVNKENAQSM---------FYEGAETVNFKEEL 75
Cdd:COG1335    1 ALLVIDVQNDFvPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFaefdlwpphCVPGTPGAELVPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  76 KPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNrkgldgkeyn 155
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRD---------- 150

                        170       180
                 ....*....|....*....|
gi 507015254 156 aEDIHNMTLVNLHEEFATIV 175
Cdd:COG1335  151 -PEAHEAALARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 6-160 6.56e-43

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: 141.25  E-value: 6.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAFQLPY-WGERNNLFAEENMRMLLAEWRKRKRPVFHIQHVNKENAQSMFY-----------EGAETVnfkE 73
Cdd:cd00431    1 ALLVVDMQNDFVPGGgLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEllwpphcvkgtEGAELV---P 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  74 ELKPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNrkgLDGKE 153
Cdd:cd00431   78 ELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRD---EEDHE 154


                 ....*..
gi 507015254 154 YNAEDIH 160
Cdd:cd00431  155 AALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 6-177 6.30e-37

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 126.36  E-value: 6.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254    6 ALIIIDVQKAFqLPYWGERNNLFAE--ENMRMLLAEWRKRKRPVFHIQHVNKENAQSM---------FYEGAETVNFKEE 74
Cdd:pfam00857   2 ALLVIDMQNDF-VDSGGPKVEGIAAilENINRLLKAARKAGIPVIFTRQVPEPDDADFalkdrpspaFPPGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   75 LKPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNrkgldgkey 154
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLS--------- 151

                         170       180
                  ....*....|....*....|...
gi 507015254  155 naEDIHNMTLVNLHEEFATIVTT 177
Cdd:pfam00857 152 --PEAHDAALERLAQRGAEVTTT 172
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
6-181 1.63e-27

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 103.01  E-value: 1.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAFQLPYwGERNNLFAE--ENMRMLLAEWRKRKRPVFHIQHVNKENAQS--MFYE--------GAETVNFKE 73
Cdd:COG1535   21 ALLIHDMQNYFLRPY-DPDEPPIRElvANIARLRDACRAAGIPVVYTAQPGDQTPEDrgLLNDfwgpgltaGPEGQEIVD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  74 ELKPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNRkgldgke 153
Cdd:COG1535  100 ELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSR------- 172

                        170       180
                 ....*....|....*....|....*...
gi 507015254 154 ynaeDIHNMTLVNLHEEFATIVTTKEVL 181
Cdd:COG1535  173 ----EEHRMALEYVAGRCGVVVTTDEVL 196
PLN02621 PLN02621
nicotinamidase
 6-175 5.00e-20

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 83.29  E-value: 5.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAFQ------LPywgernnlfaeeNMRMLLAEWRKRKRPVFHIQHVNKENAQ-SMFYE----------GAET 68
Cdd:PLN02621  22 ALLVIDMQNYFSsmaepiLP------------ALLTTIDLCRRASIPVFFTRHSHKSPSDyGMLGEwwdgdlildgTTEA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  69 VNFKEELKPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNrkg 148
Cdd:PLN02621  90 ELMPEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN--- 166

                        170       180
                 ....*....|....*....|....*..
gi 507015254 149 ldgkeynaEDIHNMTLVNLHEEFATIV 175
Cdd:PLN02621 167 --------EELHEATLKNLAYGFAYLV 185
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 6-181 2.12e-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: 80.91  E-value: 2.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAFQLP--YWGErNNLFAEENMRMLLAEWRKRKRPVFHIQHV------------NKENAQSMFYEGAETVNF 71
Cdd:cd01015    1 ALLVIDLVEGYTQPgsYLAP-GIAAALENVQRLLAAARAAGVPVIHTTVVydpdgadgglwaRKVPAMSDLVEGSPLAAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  72 KEELKPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATAtfnrkglDG 151
Cdd:cd01015   80 CDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVG-------DR 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 507015254 152 keynAEDIHNMTLVNLHEEFATIVTTKEVL 181
Cdd:cd01015  153 ----APAPHEANLFDIDNKYGDVVSTDDAL 178
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 5-150 4.01e-12

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: 61.90  E-value: 4.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   5 IALIIIDVQKAF----QLPYWG------ERNNLFAEENMRMLLA--EWRKRKRPVFHIQHVNKENAQSMFY--------- 63
Cdd:cd01011    2 DALLVVDVQNDFcpggALAVPGgdaivpLINALLSLFQYDLVVAtqDWHPANHASFASNHPGQMPFITLPPgpqvlwpdh 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  64 -----EGAEtvnFKEELKPLPGEVIIQKSVN------SAFIG------TNLEEQLRENKCNAVVVVGLTTNHCVETTTRM 126
Cdd:cd01011   82 cvqgtPGAE---LHPGLPVPDIDLIVRKGTNpdidsySAFFDndrrssTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158

                        170       180
                 ....*....|....*....|....
gi 507015254 127 AGNLGFTTYLVSDATATFNRKGLD 150
Cdd:cd01011  159 ALKAGFEVRVLEDACRAVDPETIE 182
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 1-142 8.29e-10

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 55.84  E-value: 8.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   1 MMNQIALIIIDVQKAFQLPywGER------------NNLFAEENMRMLLA--EWRkrkrPVFHIQHVNKENAQSMFYEGA 66
Cdd:PTZ00331   9 SSTNDALIIVDVQNDFCKG--GSLavpdaeevipviNQVRQSHHFDLVVAtqDWH----PPNHISFASNHGKPKILPDGT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  67 ETV-------------NFKEELKPLPGEVIIQKSVN------SAFIG-----TNLEEQLRENKCNAVVVVGLTTNHCVET 122
Cdd:PTZ00331  83 TQGlwpphcvqgtkgaQLHKDLVVERIDIIIRKGTNrdvdsySAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVLF 162

                        170       180
                 ....*....|....*....|
gi 507015254 123 TTRMAGNLGFTTYLVSDATA 142
Cdd:PTZ00331 163 TALDAVKLGFKVVVLEDATR 182
PRK11440 PRK11440
putative hydrolase; Provisional
 70-181 2.08e-08

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 51.65  E-value: 2.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  70 NFKEELKPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATfnrkgl 149
Cdd:PRK11440  85 QHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSA------ 158

                         90       100       110
                 ....*....|....*....|....*....|..
gi 507015254 150 dgkeyNAEDIHNMTLVNLHEEFATIVTTKEVL 181
Cdd:PRK11440 159 -----ASAEQHQNSMNHIFPRIARVRSVEEIL 185
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 6-145 8.55e-06

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: 43.74  E-value: 8.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254   6 ALIIIDVQKAFqLPYWGERNNLFaeENMRMLLAEWRKRKRPVFHIQHVNKENAQSMfyegaetvnfkEELKPL-PGEVII 84
Cdd:cd01012    1 ALLLVDVQEKL-APAIKSFDELI--NNTVKLAKAAKLLDVPVILTEQYPKGLGPTV-----------PELREVfPDAPVI 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507015254  85 QKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFN 145
Cdd:cd01012   67 EKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRS 127
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 73-177 2.61e-05

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: 43.10  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507015254  73 EELKPLPGEVIIQKSVNSAFIGTNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSDATATFNRKGldgk 152
Cdd:cd01013  109 TELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADFSLEE---- 184

                         90       100
                 ....*....|....*....|....*
gi 507015254 153 eynaediHNMTLVNLHEEFATIVTT 177
Cdd:cd01013  185 -------HRMALKYAATRCAMVVST 202
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
83-139 2.58e-03

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 37.28  E-value: 2.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507015254  83 IIQKSVN------SAFIG------TNLEEQLRENKCNAVVVVGLTTNHCVETTTRMAGNLGFTTYLVSD 139
Cdd:PRK11609 107 VFHKGENplidsySAFFDnghrqkTALDDWLREHGITELIVMGLATDYCVKFTVLDALALGYQVNVITD 175
 
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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