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Conserved domains on  [gi|493017028|ref|WP_006094122|]
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MULTISPECIES: cysteine hydrolase family protein [Bacillus]

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 6.68e-55

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: 171.23  E-value: 6.68e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   6 ALIIIDVQKAFNLPYWGERNNPFAEENMKSLLEEWRRRDLPLFHIQHVNKEniESMFHPNAETSQFKEEVQPLQGEIVIQ 85
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDE--GGSFAPGSEGWEIHPELAPLEGETVIE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493017028  86 KCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNRKGPDGLQyCAEEIHNMT 163
Cdd:cd01014   79 KTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVL-SAEEIHAHY 155
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 6-163 6.68e-55

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: 171.23  E-value: 6.68e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   6 ALIIIDVQKAFNLPYWGERNNPFAEENMKSLLEEWRRRDLPLFHIQHVNKEniESMFHPNAETSQFKEEVQPLQGEIVIQ 85
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDE--GGSFAPGSEGWEIHPELAPLEGETVIE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493017028  86 KCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNRKGPDGLQyCAEEIHNMT 163
Cdd:cd01014   79 KTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVL-SAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 6-175 2.07e-48

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: 155.06  E-value: 2.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   6 ALIIIDVQKAF-NLPYWGERNNPFAEENMKSLLEEWRRRDLPLFHIQHVNKENIESM---------FHPNAETSQFKEEV 75
Cdd:COG1335    1 ALLVIDVQNDFvPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFaefdlwpphCVPGTPGAELVPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  76 QPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNrkgpdglqyc 155
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRD---------- 150

                        170       180
                 ....*....|....*....|
gi 493017028 156 aEEIHNMTLVNLHEEFATIV 175
Cdd:COG1335  151 -PEAHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 5-177 1.53e-32

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 114.81  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028    5 SALIIIDVQKAFnLPYWGERNNPFAE--ENMKSLLEEWRRRDLPLFHIQHVNKENIESM---------FHPNAETSQFKE 73
Cdd:pfam00857   1 TALLVIDMQNDF-VDSGGPKVEGIAAilENINRLLKAARKAGIPVIFTRQVPEPDDADFalkdrpspaFPPGTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   74 EVQPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNrkgpdglq 153
Cdd:pfam00857  80 ELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLS-------- 151

                         170       180
                  ....*....|....*....|....
gi 493017028  154 ycaEEIHNMTLVNLHEEFATIVTT 177
Cdd:pfam00857 152 ---PEAHDAALERLAQRGAEVTTT 172
PLN02621 PLN02621
nicotinamidase
 3-175 3.35e-20

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 83.29  E-value: 3.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   3 KQSALIIIDVQKAFNlpywgernnPFAEENMKSLLEE---WRRRDLPLFHIQHVNKE-----------NIESMFHPNAET 68
Cdd:PLN02621  19 KQAALLVIDMQNYFS---------SMAEPILPALLTTidlCRRASIPVFFTRHSHKSpsdygmlgewwDGDLILDGTTEA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  69 SQFKEEVQPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNrkg 148
Cdd:PLN02621  90 ELMPEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN--- 166

                        170       180
                 ....*....|....*....|....*..
gi 493017028 149 pdglqycaEEIHNMTLVNLHEEFATIV 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 6.68e-55

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: 171.23  E-value: 6.68e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   6 ALIIIDVQKAFNLPYWGERNNPFAEENMKSLLEEWRRRDLPLFHIQHVNKEniESMFHPNAETSQFKEEVQPLQGEIVIQ 85
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDE--GGSFAPGSEGWEIHPELAPLEGETVIE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493017028  86 KCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNRKGPDGLQyCAEEIHNMT 163
Cdd:cd01014   79 KTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVL-SAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 6-175 2.07e-48

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: 155.06  E-value: 2.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   6 ALIIIDVQKAF-NLPYWGERNNPFAEENMKSLLEEWRRRDLPLFHIQHVNKENIESM---------FHPNAETSQFKEEV 75
Cdd:COG1335    1 ALLVIDVQNDFvPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFaefdlwpphCVPGTPGAELVPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  76 QPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNrkgpdglqyc 155
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRD---------- 150

                        170       180
                 ....*....|....*....|
gi 493017028 156 aEEIHNMTLVNLHEEFATIV 175
Cdd:COG1335  151 -PEAHEAALARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 6-160 6.81e-40

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: 133.16  E-value: 6.81e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   6 ALIIIDVQKAF-NLPYWGERNNPFAEENMKSLLEEWRRRDLPLFHIQHVNKENIES--------MFHPNAETSQFKEEVQ 76
Cdd:cd00431    1 ALLVVDMQNDFvPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEfaellwppHCVKGTEGAELVPELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  77 PLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNrkgPDGLQYCA 156
Cdd:cd00431   81 PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRD---EEDHEAAL 157


                 ....
gi 493017028 157 EEIH 160
Cdd:cd00431  158 ERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 5-177 1.53e-32

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 114.81  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028    5 SALIIIDVQKAFnLPYWGERNNPFAE--ENMKSLLEEWRRRDLPLFHIQHVNKENIESM---------FHPNAETSQFKE 73
Cdd:pfam00857   1 TALLVIDMQNDF-VDSGGPKVEGIAAilENINRLLKAARKAGIPVIFTRQVPEPDDADFalkdrpspaFPPGTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   74 EVQPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNrkgpdglq 153
Cdd:pfam00857  80 ELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLS-------- 151

                         170       180
                  ....*....|....*....|....
gi 493017028  154 ycaEEIHNMTLVNLHEEFATIVTT 177
Cdd:pfam00857 152 ---PEAHDAALERLAQRGAEVTTT 172
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
5-182 5.71e-26

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 98.77  E-value: 5.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   5 SALIIIDVQKAFNLPYwGERNNPFAE--ENMKSLLEEWRRRDLPLFHIQHVNKENIES------MFHP----NAETSQFK 72
Cdd:COG1535   20 AALLIHDMQNYFLRPY-DPDEPPIRElvANIARLRDACRAAGIPVVYTAQPGDQTPEDrgllndFWGPgltaGPEGQEIV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  73 EEVQPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNRkgpdgl 152
Cdd:COG1535   99 DELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSR------ 172

                        170       180       190
                 ....*....|....*....|....*....|
gi 493017028 153 qycaeEIHNMTLVNLHEEFATIVTTSEILE 182
Cdd:COG1535  173 -----EEHRMALEYVAGRCGVVVTTDEVLE 197
PLN02621 PLN02621
nicotinamidase
 3-175 3.35e-20

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 83.29  E-value: 3.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   3 KQSALIIIDVQKAFNlpywgernnPFAEENMKSLLEE---WRRRDLPLFHIQHVNKE-----------NIESMFHPNAET 68
Cdd:PLN02621  19 KQAALLVIDMQNYFS---------SMAEPILPALLTTidlCRRASIPVFFTRHSHKSpsdygmlgewwDGDLILDGTTEA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  69 SQFKEEVQPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNrkg 148
Cdd:PLN02621  90 ELMPEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN--- 166

                        170       180
                 ....*....|....*....|....*..
gi 493017028 149 pdglqycaEEIHNMTLVNLHEEFATIV 175
Cdd:PLN02621 167 --------EELHEATLKNLAYGFAYLV 185
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 6-181 4.14e-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: 4.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   6 ALIIIDVQKAFNLP--YWGErNNPFAEENMKSLLEEWRRRDLPLFHIQHV------------NKENIESMFHPNAETSQF 71
Cdd:cd01015    1 ALLVIDLVEGYTQPgsYLAP-GIAAALENVQRLLAAARAAGVPVIHTTVVydpdgadgglwaRKVPAMSDLVEGSPLAAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  72 KEEVQPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATAtfnrkgpDG 151
Cdd:cd01015   80 CDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVG-------DR 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 493017028 152 lqycAEEIHNMTLVNLHEEFATIVTTSEIL 181
Cdd:cd01015  153 ----APAPHEANLFDIDNKYGDVVSTDDAL 178
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 5-142 7.31e-09

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 53.15  E-value: 7.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   5 SALIIIDVQKAFNLPywGERNNPFAEE--------------NMKSLLEEWRRRDLPLFHIQHVN----KENIESMFHP-- 64
Cdd:PTZ00331  13 DALIIVDVQNDFCKG--GSLAVPDAEEvipvinqvrqshhfDLVVATQDWHPPNHISFASNHGKpkilPDGTTQGLWPph 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  65 ---NAETSQFKEEVQPLQGEIVIQKCVN------SAFMG-----TNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNL 130
Cdd:PTZ00331  91 cvqGTKGAQLHKDLVVERIDIIIRKGTNrdvdsySAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTALDAVKL 170

                        170
                 ....*....|..
gi 493017028 131 GFSTYLVSDATA 142
Cdd:PTZ00331 171 GFKVVVLEDATR 182
PRK11440 PRK11440
putative hydrolase; Provisional
 3-181 9.93e-09

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 52.42  E-value: 9.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   3 KQSALIIIDVQKAFnLPYWGernNPFAEENMKS----LLEEWRRRDLPLFHIQhV--NKENIESMFHP-NAETS------ 69
Cdd:PRK11440   7 KTTALVVIDLQEGI-LPFAG---GPHTADEVVAraarLAAKFRASGSPVVLVR-VgwSADYAEALKQPvDAPSPakvlpe 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  70 ---QFKEEVQPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATfnr 146
Cdd:PRK11440  82 nwwQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSA--- 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 493017028 147 kgpdglqyCAEEIHNMTLVNLHEEFATIVTTSEIL 181
Cdd:PRK11440 159 --------ASAEQHQNSMNHIFPRIARVRSVEEIL 185
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 64-158 1.64e-08

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: 51.88  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  64 PNAETSQFKEEVQPLQGEIVIQKCVN------SAFMG------TNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLG 131
Cdd:cd01011   84 QGTPGAELHPGLPVPDIDLIVRKGTNpdidsySAFFDndrrssTGLAEYLRERGIDRVDVVGLATDYCVKATALDALKAG 163

                         90       100
                 ....*....|....*....|....*..
gi 493017028 132 FSTYLVSDATATFNrkgPDGLQYCAEE 158
Cdd:cd01011  164 FEVRVLEDACRAVD---PETIERAIEE 187
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 6-145 2.81e-04

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: 39.50  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028   6 ALIIIDVQK--AFNLPYwgernnpFAE--ENMKSLLEEWRRRDLPLFHIQHVNKeniesmfhPNAETSQfkeEVQPLQGE 81
Cdd:cd01012    1 ALLLVDVQEklAPAIKS-------FDEliNNTVKLAKAAKLLDVPVILTEQYPK--------GLGPTVP---ELREVFPD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493017028  82 I-VIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFN 145
Cdd:cd01012   63 ApVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRS 127
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 73-156 2.85e-04

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: 40.01  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493017028  73 EEVQPLQGEIVIQKCVNSAFMGTNLEKQLKEKNCNSVIIVGLTTNHCVETTTRMAGNLGFSTYLVSDATATFNRKGPD-G 151
Cdd:cd01013  109 TELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADFSLEEHRmA 188


                 ....*
gi 493017028 152 LQYCA 156
Cdd:cd01013  189 LKYAA 193
 
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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