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Conserved domains on  [gi|269914641|pdb|3KL2|G]
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Chain G, Putative isochorismatase

Protein Classification

cysteine hydrolase( domain architecture ID 10467615)

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
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 26-212 5.71e-48

Isochorismatase family; This family are hydrolase enzymes.


:

Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 155.64  E-value: 5.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G         26 TAIVLIEYQNEFTSDGGVLHGAVADvmqhtgMLANTVAVVDAARQAGVPIMHAPITFAEGYGELTRhpygilkGVVDGKA 105
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGIAA------ILENINRLLKAARKAGIPVIFTRQVPEPDDADFAL-------KDRPSPA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        106 FVKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDC 185
Cdd:pfam00857  68 FPPGTTGAELVPELAPLPGDLVVD-KTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDA 146

                         170       180
                  ....*....|....*....|....*..
3KL2_G        186 VAATSQEEHNNAISYDFPMFSVPMTSA 212
Cdd:pfam00857 147 CASLSPEAHDAALERLAQRGAEVTTTE 173
 
Name Accession Description Interval E-value
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 26-212 5.71e-48

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 155.64  E-value: 5.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G         26 TAIVLIEYQNEFTSDGGVLHGAVADvmqhtgMLANTVAVVDAARQAGVPIMHAPITFAEGYGELTRhpygilkGVVDGKA 105
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGIAA------ILENINRLLKAARKAGIPVIFTRQVPEPDDADFAL-------KDRPSPA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        106 FVKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDC 185
Cdd:pfam00857  68 FPPGTTGAELVPELAPLPGDLVVD-KTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDA 146

                         170       180
                  ....*....|....*....|....*..
3KL2_G        186 VAATSQEEHNNAISYDFPMFSVPMTSA 212
Cdd:pfam00857 147 CASLSPEAHDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 27-198 8.70e-48

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: 154.73  E-value: 8.70e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       27 AIVLIEYQNEFTSDGGVLHGAVADVmqhtgmLANTVAVVDAARQAGVPIMHAPITFAEGYGELTRHPYGilkgvvdgKAF 106
Cdd:cd00431   1 ALLVVDMQNDFVPGGGLLLPGADEL------VPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELLWP--------PHC 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G      107 VKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDCV 186
Cdd:cd00431  67 VKGTEGAELVPELAPLPDDLVIE-KTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDAC 145

                       170
                ....*....|..
3KL2_G      187 AATSQEEHNNAI 198
Cdd:cd00431 146 ATRDEEDHEAAL 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 27-198 1.18e-45

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: 149.67  E-value: 1.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       27 AIVLIEYQNEFTsDGGVLHGAVADvmqhtGMLANTVAVVDAARQAGVPIMHAPITFAEGYGELTrhpygilKGVVDGKAF 106
Cdd:COG1335   1 ALLVIDVQNDFV-PPGALAVPGAD-----AVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFA-------EFDLWPPHC 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G      107 VKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDCV 186
Cdd:COG1335  68 VPGTPGAELVPELAPLPGDPVVD-KTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDAC 146

                       170
                ....*....|..
3KL2_G      187 AATSQEEHNNAI 198
Cdd:COG1335 147 ASRDPEAHEAAL 158
PRK11440 PRK11440
putative hydrolase; Provisional
 19-218 3.88e-27

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 102.50  E-value: 3.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        19 LELDPARTAIVLIEYQNEFTSDGGVLHGAvADVMQHTGMLAntvavvDAARQAGVPIMHAPITFAEGYGELTRHPygilk 98
Cdd:PRK11440   2 LELNAKTTALVVIDLQEGILPFAGGPHTA-DEVVARAARLA------AKFRASGSPVVLVRVGWSADYAEALKQP----- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        99 gvVDGKAFVKG------TWGAAivdeLAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTG 172
Cdd:PRK11440  70 --VDAPSPAKVlpenwwQHPAA----LGKTDSDIEVT-KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNA 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
3KL2_G       173 YERGFRVITLTDCVAATSQEEHNNAISYDFPMFSVPMTSADVIAAL 218
Cdd:PRK11440 143 WELGFNLVIAEDACSAASAEQHQNSMNHIFPRIARVRSVEEILNAL 188
 
Name Accession Description Interval E-value
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 26-212 5.71e-48

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 155.64  E-value: 5.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G         26 TAIVLIEYQNEFTSDGGVLHGAVADvmqhtgMLANTVAVVDAARQAGVPIMHAPITFAEGYGELTRhpygilkGVVDGKA 105
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGIAA------ILENINRLLKAARKAGIPVIFTRQVPEPDDADFAL-------KDRPSPA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        106 FVKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDC 185
Cdd:pfam00857  68 FPPGTTGAELVPELAPLPGDLVVD-KTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDA 146

                         170       180
                  ....*....|....*....|....*..
3KL2_G        186 VAATSQEEHNNAISYDFPMFSVPMTSA 212
Cdd:pfam00857 147 CASLSPEAHDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 27-198 8.70e-48

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: 154.73  E-value: 8.70e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       27 AIVLIEYQNEFTSDGGVLHGAVADVmqhtgmLANTVAVVDAARQAGVPIMHAPITFAEGYGELTRHPYGilkgvvdgKAF 106
Cdd:cd00431   1 ALLVVDMQNDFVPGGGLLLPGADEL------VPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELLWP--------PHC 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G      107 VKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDCV 186
Cdd:cd00431  67 VKGTEGAELVPELAPLPDDLVIE-KTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDAC 145

                       170
                ....*....|..
3KL2_G      187 AATSQEEHNNAI 198
Cdd:cd00431 146 ATRDEEDHEAAL 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 27-198 1.18e-45

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: 149.67  E-value: 1.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       27 AIVLIEYQNEFTsDGGVLHGAVADvmqhtGMLANTVAVVDAARQAGVPIMHAPITFAEGYGELTrhpygilKGVVDGKAF 106
Cdd:COG1335   1 ALLVIDVQNDFV-PPGALAVPGAD-----AVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFA-------EFDLWPPHC 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G      107 VKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDCV 186
Cdd:COG1335  68 VPGTPGAELVPELAPLPGDPVVD-KTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDAC 146

                       170
                ....*....|..
3KL2_G      187 AATSQEEHNNAI 198
Cdd:COG1335 147 ASRDPEAHEAAL 158
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
20-219 1.13e-29

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 109.55  E-value: 1.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       20 ELDPARTAIVLIEYQNEFTSDGGVLHGAVADVmqhtgmLANTVAVVDAARQAGVPIMHapitfaegygelTRHPY----- 94
Cdd:COG1535  14 TLDPARAALLIHDMQNYFLRPYDPDEPPIREL------VANIARLRDACRAAGIPVVY------------TAQPGdqtpe 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       95 --GILKGVVdGKAFVKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTG 172
Cdd:COG1535  76 drGLLNDFW-GPGLTAGPEGQEIVDELAPAPGDTVLT-KWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDA 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
3KL2_G      173 YERGFRVITLTDCVAATSQEEHNNAISYDFPMFSVPMTSADVIAALE 219
Cdd:COG1535 154 FMRDIQPFVVADAVADFSREEHRMALEYVAGRCGVVVTTDEVLEALR 200
PRK11440 PRK11440
putative hydrolase; Provisional
 19-218 3.88e-27

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 102.50  E-value: 3.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        19 LELDPARTAIVLIEYQNEFTSDGGVLHGAvADVMQHTGMLAntvavvDAARQAGVPIMHAPITFAEGYGELTRHPygilk 98
Cdd:PRK11440   2 LELNAKTTALVVIDLQEGILPFAGGPHTA-DEVVARAARLA------AKFRASGSPVVLVRVGWSADYAEALKQP----- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        99 gvVDGKAFVKG------TWGAAivdeLAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTG 172
Cdd:PRK11440  70 --VDAPSPAKVlpenwwQHPAA----LGKTDSDIEVT-KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNA 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
3KL2_G       173 YERGFRVITLTDCVAATSQEEHNNAISYDFPMFSVPMTSADVIAAL 218
Cdd:PRK11440 143 WELGFNLVIAEDACSAASAEQHQNSMNHIFPRIARVRSVEEILNAL 188
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 27-199 1.10e-26

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: 100.36  E-value: 1.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       27 AIVLIEYQNEFTSDGGVLHGavadvmqHTGMLANTVAVVDAARQAGVPIMHapitfaegygelTRHPygilkgVVDGKAF 106
Cdd:cd01014   1 ALLVIDVQNGYFDGGLPPLN-------NEAALENIAALIAAARAAGIPVIH------------VRHI------DDEGGSF 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G      107 VKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDCV 186
Cdd:cd01014  56 APGSEGWEIHPELAPLEGETVIE-KTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADAC 134

                       170
                ....*....|...
3KL2_G      187 AATSQEEHNNAIS 199
Cdd:cd01014 135 ATFDLPDHGGVLS 147
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 27-194 5.90e-25

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: 96.70  E-value: 5.90e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       27 AIVLIEYQNEFTSDGGVLHGAVADVmqhtgmLANTVAVVDAARQAGVPIMHAPITFAEGygeLTRHPYGILKgVVDGKAF 106
Cdd:cd01015   1 ALLVIDLVEGYTQPGSYLAPGIAAA------LENVQRLLAAARAAGVPVIHTTVVYDPD---GADGGLWARK-VPAMSDL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G      107 VKGTWGAAIVDELAPVNGDIVIEgKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDCV 186
Cdd:cd01015  71 VEGSPLAAICDELAPQEDEMVLV-KKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECV 149


                ....*...
3KL2_G      187 AATSQEEH 194
Cdd:cd01015 150 GDRAPAPH 157
PLN02621 PLN02621
nicotinamidase
 16-202 7.06e-17

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 75.59  E-value: 7.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        16 TEKLELDPARTAIVLIEYQNEFTSdggvlhgavadvMQHTgMLANTVAVVDAARQAGVPIMHapitfaegygelTRH--- 92
Cdd:PLN02621  11 TRKRDPDPKQAALLVIDMQNYFSS------------MAEP-ILPALLTTIDLCRRASIPVFF------------TRHshk 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        93 ---PYGILKGVVDGKAFVKGTWGAAIVDELAPVNGDIVIEGKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTM 169
Cdd:PLN02621  66 spsDYGMLGEWWDGDLILDGTTEAELMPEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTA 145

                        170       180       190
                 ....*....|....*....|....*....|....*.
3KL2_G       170 RTGYERGFRVITLTDCVAATSQEEHNNAI---SYDF 202
Cdd:PLN02621 146 REAFVRGFRVFFSTDATATANEELHEATLknlAYGF 181
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 107-192 2.51e-10

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: 57.66  E-value: 2.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G      107 VKGTWGAAIVDELAPVNGDIVIE-----------GKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYER 175
Cdd:cd01011  83 VQGTPGAELHPGLPVPDIDLIVRkgtnpdidsysAFFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALDALKA 162

                        90
                ....*....|....*..
3KL2_G      176 GFRVITLTDCVAATSQE 192
Cdd:cd01011 163 GFEVRVLEDACRAVDPE 179
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 23-192 4.06e-08

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 51.61  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G        23 PARTAIVLIEYQNEFTSDGGVLH---GAVADVMQHTGMLANTVAVVdaARQAGVPIMHapITFAEGYGELTRHPYGILKG 99
Cdd:PTZ00331  10 STNDALIIVDVQNDFCKGGSLAVpdaEEVIPVINQVRQSHHFDLVV--ATQDWHPPNH--ISFASNHGKPKILPDGTTQG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       100 VVDGKAfVKGTWGAAIVDELAPVNGDIVIEG--KRGLDTFAS--------TNLDFILRSKGVDTIVLGGFLTNCCVESTM 169
Cdd:PTZ00331  86 LWPPHC-VQGTKGAQLHKDLVVERIDIIIRKgtNRDVDSYSAfdndkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTA 164

                        170       180
                 ....*....|....*....|...
3KL2_G       170 RTGYERGFRVITLTDCVAATSQE 192
Cdd:PTZ00331 165 LDAVKLGFKVVVLEDATRAVDPD 187
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 27-198 6.28e-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: 50.29  E-value: 6.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       27 AIVLIEYQNEFtsdggvlhgaVADVMQHTGMLANTVAVVDAARQAGVPIMhapitfaegygeLTRHPYGILKgvvdgkaf 106
Cdd:cd01012   1 ALLLVDVQEKL----------APAIKSFDELINNTVKLAKAAKLLDVPVI------------LTEQYPKGLG-------- 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G      107 vkgtwgaAIVDELAPVNGDIVIEGKRGLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRTGYERGFRVITLTDCV 186
Cdd:cd01012  51 -------PTVPELREVFPDAPVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADAC 123

                       170
                ....*....|..
3KL2_G      187 AATSQEEHNNAI 198
Cdd:cd01012 124 GSRSKEDHELAL 135
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 21-200 1.16e-07

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: 50.41  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G       21 LDPARTAIVLIEYQNEFTSdggvLHGAVADVMqhTGMLANTVAVVDAARQAGVPIMHapitfaegygelTRHPYGILKGv 100
Cdd:cd01013  25 IDPKRAVLLVHDMQRYFLD----FYDESAEPV--PQLIANIARLRDWCRQAGIPVVY------------TAQPGNQTPE- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KL2_G      101 vdGKAFVKGTWG---------AAIVDELAPVNGDIVIEGKRgLDTFASTNLDFILRSKGVDTIVLGGFLTNCCVESTMRT 171
Cdd:cd01013  86 --QRALLNDFWGpgltaspeeTKIVTELAPQPDDTVLTKWR-YSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVD 162

                       170       180
                ....*....|....*....|....*....
3KL2_G      172 GYERGFRVITLTDCVAATSQEEHNNAISY 200
Cdd:cd01013 163 AFMRDIQPFVVADAIADFSLEEHRMALKY 191
 
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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