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Conserved domains on  [gi|90111348|ref|NP_416381|]
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isochorismatase family protein YecD [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

YecD family hydrolase( domain architecture ID 10793573)

YecD family hydrolase similar to Escherichia coli isochorismatase family protein YecD

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11440 PRK11440
putative hydrolase; Provisional
 1-188 2.30e-139

putative hydrolase; Provisional


:

Pssm-ID: 183137  Cd Length: 188  Bit Score: 386.01  E-value: 2.30e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348    1 MLELNAKTTALVVIDLQEGILPFAGGPHTADEVVNRAGKLAAKFRASGQPVFLVRVGWSADYAEALKQPVDAPSPAKVLP 80
Cdd:PRK11440   1 MLELNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSADYAEALKQPVDAPSPAKVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348   81 ENWWQHPAALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAAS 160
Cdd:PRK11440  81 ENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAAS 160

                        170       180
                 ....*....|....*....|....*...
gi 90111348  161 AEQHNNSINHIYPRIARVRSVEEILNAL 188
Cdd:PRK11440 161 AEQHQNSMNHIFPRIARVRSVEEILNAL 188
 
Name Accession Description Interval E-value
PRK11440 PRK11440
putative hydrolase; Provisional
 1-188 2.30e-139

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 386.01  E-value: 2.30e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348    1 MLELNAKTTALVVIDLQEGILPFAGGPHTADEVVNRAGKLAAKFRASGQPVFLVRVGWSADYAEALKQPVDAPSPAKVLP 80
Cdd:PRK11440   1 MLELNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSADYAEALKQPVDAPSPAKVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348   81 ENWWQHPAALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAAS 160
Cdd:PRK11440  81 ENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAAS 160

                        170       180
                 ....*....|....*....|....*...
gi 90111348  161 AEQHNNSINHIYPRIARVRSVEEILNAL 188
Cdd:PRK11440 161 AEQHQNSMNHIFPRIARVRSVEEILNAL 188
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 10-172 9.09e-49

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: 155.89  E-value: 9.09e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  10 ALVVIDLQEGILPFAGGPHT-ADEVVNRAGKLAAKFRASGQPVFLVRVGWSADYAEALKQPvdaPSPAKVLPENWWQHPA 88
Cdd:cd00431   1 ALLVVDMQNDFVPGGGLLLPgADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELL---WPPHCVKGTEGAELVP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  89 ALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHNNSI 168
Cdd:cd00431  78 ELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAAL 157


                ....
gi 90111348 169 NHIY 172
Cdd:cd00431 158 ERLA 161
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 10-178 2.54e-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: 154.68  E-value: 2.54e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  10 ALVVIDLQEGILPF-AGGPHTADEVVNRAGKLAAKFRASGQPVFLVRVGWSADYAEALKQpvDAPSPAKVLPENWWQHPA 88
Cdd:COG1335   1 ALLVIDVQNDFVPPgALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEF--DLWPPHCVPGTPGAELVP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  89 ALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHNNSI 168
Cdd:COG1335  79 ELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAAL 158

                       170
                ....*....|
gi 90111348 169 NHIYPRIARV 178
Cdd:COG1335 159 ARLRAAGATV 168
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 9-182 5.83e-44

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 144.08  E-value: 5.83e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348     9 TALVVIDLQEGILPFAG-GPHTADEVVNRAGKLAAKFRASGQPVFLVRVGWSADYAEAlkQPVDAPSPAKVLPENWWQ-H 86
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGpKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADF--ALKDRPSPAFPPGTTGAElV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348    87 PAaLGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHNN 166
Cdd:pfam00857  79 PE-LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157

                         170
                  ....*....|....*.
gi 90111348   167 SINHIYPRIARVRSVE 182
Cdd:pfam00857 158 ALERLAQRGAEVTTTE 173
 
Name Accession Description Interval E-value
PRK11440 PRK11440
putative hydrolase; Provisional
 1-188 2.30e-139

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 386.01  E-value: 2.30e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348    1 MLELNAKTTALVVIDLQEGILPFAGGPHTADEVVNRAGKLAAKFRASGQPVFLVRVGWSADYAEALKQPVDAPSPAKVLP 80
Cdd:PRK11440   1 MLELNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSADYAEALKQPVDAPSPAKVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348   81 ENWWQHPAALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAAS 160
Cdd:PRK11440  81 ENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAAS 160

                        170       180
                 ....*....|....*....|....*...
gi 90111348  161 AEQHNNSINHIYPRIARVRSVEEILNAL 188
Cdd:PRK11440 161 AEQHQNSMNHIFPRIARVRSVEEILNAL 188
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 10-172 9.09e-49

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: 155.89  E-value: 9.09e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  10 ALVVIDLQEGILPFAGGPHT-ADEVVNRAGKLAAKFRASGQPVFLVRVGWSADYAEALKQPvdaPSPAKVLPENWWQHPA 88
Cdd:cd00431   1 ALLVVDMQNDFVPGGGLLLPgADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELL---WPPHCVKGTEGAELVP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  89 ALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHNNSI 168
Cdd:cd00431  78 ELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAAL 157


                ....
gi 90111348 169 NHIY 172
Cdd:cd00431 158 ERLA 161
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 10-178 2.54e-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: 154.68  E-value: 2.54e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  10 ALVVIDLQEGILPF-AGGPHTADEVVNRAGKLAAKFRASGQPVFLVRVGWSADYAEALKQpvDAPSPAKVLPENWWQHPA 88
Cdd:COG1335   1 ALLVIDVQNDFVPPgALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEF--DLWPPHCVPGTPGAELVP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  89 ALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHNNSI 168
Cdd:COG1335  79 ELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAAL 158

                       170
                ....*....|
gi 90111348 169 NHIYPRIARV 178
Cdd:COG1335 159 ARLRAAGATV 168
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 9-182 5.83e-44

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 144.08  E-value: 5.83e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348     9 TALVVIDLQEGILPFAG-GPHTADEVVNRAGKLAAKFRASGQPVFLVRVGWSADYAEAlkQPVDAPSPAKVLPENWWQ-H 86
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGpKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADF--ALKDRPSPAFPPGTTGAElV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348    87 PAaLGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHNN 166
Cdd:pfam00857  79 PE-LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157

                         170
                  ....*....|....*.
gi 90111348   167 SINHIYPRIARVRSVE 182
Cdd:pfam00857 158 ALERLAQRGAEVTTTE 173
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-188 6.99e-35

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 121.50  E-value: 6.99e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348   3 ELNAKTTALVVIDLQEGIL-PFAGGPHTADEVVNRAGKLAAKFRASGQPVFlvrvgWSAdyaealkQPVDAPSPAKVLPE 81
Cdd:COG1535  14 TLDPARAALLIHDMQNYFLrPYDPDEPPIRELVANIARLRDACRAAGIPVV-----YTA-------QPGDQTPEDRGLLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  82 NWWQH-----------PAALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLV 150
Cdd:COG1535  82 DFWGPgltagpegqeiVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPF 161

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 90111348 151 IAEDACSAASAEQHNNSINHIYPRIARVRSVEEILNAL 188
Cdd:COG1535 162 VVADAVADFSREEHRMALEYVAGRCGVVVTTDEVLEAL 199
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 10-163 5.23e-31

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: 110.37  E-value: 5.23e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  10 ALVVIDLQEGILPFAGGPHTADEVVNRAGKLAAKFRASGQPVFLVRVgwsadyaealkqpvDAPSPAKVLP--ENWWQHP 87
Cdd:cd01014   1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRH--------------IDDEGGSFAPgsEGWEIHP 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  88 AALgATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACS---------A 158
Cdd:cd01014  67 ELA-PLEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACAtfdlpdhggV 145


                ....*
gi 90111348 159 ASAEQ 163
Cdd:cd01014 146 LSAEE 150
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 10-185 6.67e-20

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: 82.06  E-value: 6.67e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  10 ALVVIDLQEGIL----PFAGGPHTADEVVNRagkLAAKFRASGQPVFLVRVGWSADYAE----ALKQPVDApspAKVLPE 81
Cdd:cd01015   1 ALLVIDLVEGYTqpgsYLAPGIAAALENVQR---LLAAARAAGVPVIHTTVVYDPDGADgglwARKVPAMS---DLVEGS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  82 NWWQHPAALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASA 161
Cdd:cd01015  75 PLAAICDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAP 154

                       170       180
                ....*....|....*....|....
gi 90111348 162 EQHNNSINHIYPRIARVRSVEEIL 185
Cdd:cd01015 155 APHEANLFDIDNKYGDVVSTDDAL 178
PLN02621 PLN02621
nicotinamidase
 5-168 2.18e-16

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 73.28  E-value: 2.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348    5 NAKTTALVVIDLQEGilpFAGgphTADEVVNRAGKLAAKFRASGQPVFLVRvgwsadyaEALKQPVDAPspakVLPEnWW 84
Cdd:PLN02621  17 DPKQAALLVIDMQNY---FSS---MAEPILPALLTTIDLCRRASIPVFFTR--------HSHKSPSDYG----MLGE-WW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348   85 QHPAAL-GATDSDI-----------EII-KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVI 151
Cdd:PLN02621  78 DGDLILdGTTEAELmpeigrvtgpdEVVeKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFF 157

                        170
                 ....*....|....*..
gi 90111348  152 AEDACSAASAEQHNNSI 168
Cdd:PLN02621 158 STDATATANEELHEATL 174
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 8-162 1.36e-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: 63.05  E-value: 1.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348   8 TTALVVIDLQE-----GILPFAGGphtaDEVVNRAGKLAAKFRasGQPVFLVR-------VGWSADYAEalKQPVDAPSP 75
Cdd:cd01011   1 TDALLVVDVQNdfcpgGALAVPGG----DAIVPLINALLSLFQ--YDLVVATQdwhpanhASFASNHPG--QMPFITLPP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  76 AKVLPenWWQH-----PAA-----LGATDSDIEIIKRQ------WGAFYG------TDLELQLRRRGIDTIVLCGISTNI 133
Cdd:cd01011  73 GPQVL--WPDHcvqgtPGAelhpgLPVPDIDLIVRKGTnpdidsYSAFFDndrrssTGLAEYLRERGIDRVDVVGLATDY 150

                       170       180
                ....*....|....*....|....*....
gi 90111348 134 GVESTARNAWELGFNLVIAEDACSAASAE 162
Cdd:cd01011 151 CVKATALDALKAGFEVRVLEDACRAVDPE 179
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 4-182 5.65e-12

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: 61.59  E-value: 5.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348   4 LNAKTTALVVIDLQEGIL-PFAGGPHTADEVVNRAGKLAAKFRASGQPVFlvrvgWSAdyaealkQPVDAPSPAKVLPEN 82
Cdd:cd01013  25 IDPKRAVLLVHDMQRYFLdFYDESAEPVPQLIANIARLRDWCRQAGIPVV-----YTA-------QPGNQTPEQRALLND 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  83 WW---------QHP--AALGATDSDIEIIKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVI 151
Cdd:cd01013  93 FWgpgltaspeETKivTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFV 172

                       170       180       190
                ....*....|....*....|....*....|.
gi 90111348 152 AEDACSAASAEQHNNSINHIYPRIARVRSVE 182
Cdd:cd01013 173 VADAIADFSLEEHRMALKYAATRCAMVVSTD 203
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 10-164 4.01e-10

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: 55.68  E-value: 4.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111348  10 ALVVIDLQEGilpFAGGPHTADEVVNRAGKLAAKFRASGQPVFlvrvgWSADYAEALKQPVdapspakvlpenwwqhpAA 89
Cdd:cd01012   1 ALLLVDVQEK---LAPAIKSFDELINNTVKLAKAAKLLDVPVI-----LTEQYPKGLGPTV-----------------PE 55

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111348  90 LGATDSDIEII-KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQH 164
Cdd:cd01012  56 LREVFPDAPVIeKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDH 131
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 109-171 1.02e-04

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 41.21  E-value: 1.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111348  109 GTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHNNSINHI 171
Cdd:PTZ00331 134 KTGLAQILKAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAEL 196
 
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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