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Conserved domains on  [gi|613174455|gb|EZX81700|]
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3-dehydroquinate dehydratase [Staphylococcus aureus DICM09/01587-13HST]

Protein Classification

type I 3-dehydroquinate dehydratase( domain architecture ID 10786388)

Type I 3-dehydroquinase (DHQase), the third enzyme in the shikimate pathway.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AroD COG0710
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-232 1.67e-76

3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


:

Pssm-ID: 440474  Cd Length: 236  Bit Score: 230.95  E-value: 1.67e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   1 MTHVEVVATIAPQlyIEETLIQKINH-RIDAIDVLELRIDQIENVTVDQVAEMITKLKVMQDsFKLLVTYRTKLQGGYGQ 79
Cdd:COG0710    1 EGRPKICVPLVGA--TPEDLLAEAEAaARAGADLVELRLDYLEDPDLEELKELLEALREYGG-LPLIFTFRTAEEGGEFE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  80 FTNDSYLNLISDLANINGIDMIDIEWqaDIDIEKHQRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYV 159
Cdd:COG0710   78 GSEEERLELLRAAADSAGVDLVDVEL--DTLEDDVDDLIEAAREAGVKVIVSYHDFEKTPSAEELVEILEKMQELGADIV 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613174455 160 KLAVMPHNKNDVLNLLQSMSTFSDTMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGEPQAPGQIDVTDLK 232
Cdd:COG0710  156 KIAVMAKSPEDVLRLLEATLEAKEELDRPVITMAMGELGKISRILGPLFGSALTYASVGEASAPGQIDVEELR 228
 
Name Accession Description Interval E-value
AroD COG0710
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-232 1.67e-76

3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440474  Cd Length: 236  Bit Score: 230.95  E-value: 1.67e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   1 MTHVEVVATIAPQlyIEETLIQKINH-RIDAIDVLELRIDQIENVTVDQVAEMITKLKVMQDsFKLLVTYRTKLQGGYGQ 79
Cdd:COG0710    1 EGRPKICVPLVGA--TPEDLLAEAEAaARAGADLVELRLDYLEDPDLEELKELLEALREYGG-LPLIFTFRTAEEGGEFE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  80 FTNDSYLNLISDLANINGIDMIDIEWqaDIDIEKHQRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYV 159
Cdd:COG0710   78 GSEEERLELLRAAADSAGVDLVDVEL--DTLEDDVDDLIEAAREAGVKVIVSYHDFEKTPSAEELVEILEKMQELGADIV 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613174455 160 KLAVMPHNKNDVLNLLQSMSTFSDTMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGEPQAPGQIDVTDLK 232
Cdd:COG0710  156 KIAVMAKSPEDVLRLLEATLEAKEELDRPVITMAMGELGKISRILGPLFGSALTYASVGEASAPGQIDVEELR 228
DHQase_I cd00502
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ...
6-233 9.35e-68

Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase). Catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate to produce dehydroshikimate. Dehydroquinase is the third enzyme in the shikimate pathway, which is involved in the biosynthesis of aromatic amino acids. Type I DHQase exists as a homodimer. Type II 3-dehydroquinase also catalyzes the same overall reaction, but is unrelated in terms of sequence and structure, and utilizes a completely different reaction mechanism.


Pssm-ID: 188633  Cd Length: 225  Bit Score: 208.35  E-value: 9.35e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   6 VVATI-APQLYIEETLIQKINHRIDAIdvlELRIDQIENVTVDQVAEMITKLKVMqDSFKLLVTYRTKLQGGYGQFTNDS 84
Cdd:cd00502    2 ICVPLtGPDLLEEALSLLELLLGADAV---ELRVDLLEDPSIDDVAEQLSLLREL-TPLPIIFTVRTKSEGGNFEGSEEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  85 YLNLISDLANInGIDMIDIEWqadiDIEKHQRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYVKLAVM 164
Cdd:cd00502   78 YLELLEEALKL-GPDYVDIEL----DSALLEELINSRKKGNTKIIGSYHDFSGTPSDEELVSRLEKMAALGADIVKIAVM 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613174455 165 PHNKNDVLNLLQSMSTFSDTMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGEPQAPGQIDVTDLKA 233
Cdd:cd00502  153 ANSIEDNLRLLKFTRQVKNLYDIPLIAINMGELGKLSRILSPVFGSPLTYASLPEPSAPGQLSVEELKQ 221
DHquinase_I pfam01487
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ...
18-232 9.16e-54

Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate giving dehydroshikimate. Dehydroquinase functions in the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Type II 3-dehydroquinase catalyzes the trans-dehydration of 3-dehydroshikimate see pfam01220.


Pssm-ID: 426287  Cd Length: 227  Bit Score: 172.74  E-value: 9.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   18 ETLIQKINHRIDAIDVLELRIDQIENV--TVDQVAEMITKLKVMQDsFKLLVTYRTKLQGGYGQFTNDSYLNLISDLANi 95
Cdd:pfam01487  10 EEILEELESGKEGADLVELRVDLLEEPveDAEDVSEQLALLRRVGD-LPLIFTFRTKSEGGEPDGSEEEYLELLRLALR- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   96 NGIDMIDIEWQADIDIEKhqRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYVKLAVMPHNKNDVLNLL 175
Cdd:pfam01487  88 LGVDYVDVELFLPEEILK--ELIEAKHEGGTKVIGSYHDFEGTPSWEELISRYEKMQALGADIVKIAVMAKSIEDVLALL 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 613174455  176 QSMSTFSDTMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGEPQ--APGQIDVTDLK 232
Cdd:pfam01487 166 RFTSEMKSLADKPLIAMSMGELGRISRVLGPIFGSPVTFAALGLAEksAPGQLTAKELR 224
aroD PRK02412
type I 3-dehydroquinate dehydratase;
4-232 3.80e-51

type I 3-dehydroquinate dehydratase;


Pssm-ID: 235036  Cd Length: 253  Bit Score: 166.61  E-value: 3.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   4 VEVVATIAPQLYIEETLIQKINhridaIDVLELRIDQIENVT-VDQVAEMITKLKVMQDSFKLLVTYRTKLQGGYGQFTN 82
Cdd:PRK02412  20 VPIMGKTLEEVLAEALAISKYD-----ADIIEWRADFLEKISdVESVLAAAPAIREKFAGKPLLFTFRTAKEGGEIALSD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  83 DSYLNLISDLANINGIDMIDIEWQADIDIEKhqRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYVKLA 162
Cdd:PRK02412  95 EEYLALIKAVIKSGLPDYIDVELFSGKDVVK--EMVAFAHEHGVKVVLSYHDFEKTPPKEEIVERLRKMESLGADIVKIA 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613174455 163 VMPHNKNDVLNLLQSMSTFSD-TMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGEPQAPGQIDVTDLK 232
Cdd:PRK02412 173 VMPQSEQDVLTLLNATREMKElYADQPLITMSMGKLGRISRLAGEVFGSSWTFASLDKASAPGQISVEDLR 243
aroD TIGR01093
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ...
32-233 1.88e-49

3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, either as a monofunctional protein or as a domain of a larger, multifunctional protein. It is often found fused to shikimate 5-dehydrogenase (EC 1.1.1.25), and sometimes additional domains. Type II 3-dehydroquinate dehydratase, designated AroQ, is described by the model TIGR01088. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273439  Cd Length: 229  Bit Score: 161.78  E-value: 1.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   32 DVLELRIDQIENVT-VDQVAEMITKLKVMQDSFKLLVTYRTKLQGGYGQFTNDSYLNLISDLANINGIDMIDIEWQADID 110
Cdd:TIGR01093  27 DIVELRVDLLKDVSsNNDVDALSEQLSELRVDKPLIFTIRTQSEGGKFPGNEEEYFEELKRAAESLGPDFVDIELFLPDD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  111 IEKhqRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYVKLAVMPHNKNDVLNLLQSMSTFSDTMDCKVV 190
Cdd:TIGR01093 107 AVK--ELINIAKKGGTKIIMSNHDFQKTPSWEEIVERLRKALSYGADIVKIAVMANSKEDVLTLLSATNKVDTHYDVPLI 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 613174455  191 GISMSKLGLISRTAQGVFGGALTYGCIGEPQAPGQIDVTDLKA 233
Cdd:TIGR01093 185 TMSMGDRGKISRVLGAVFGSVLTFGSLGKASAPGQISVDDLRE 227
 
Name Accession Description Interval E-value
AroD COG0710
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-232 1.67e-76

3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440474  Cd Length: 236  Bit Score: 230.95  E-value: 1.67e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   1 MTHVEVVATIAPQlyIEETLIQKINH-RIDAIDVLELRIDQIENVTVDQVAEMITKLKVMQDsFKLLVTYRTKLQGGYGQ 79
Cdd:COG0710    1 EGRPKICVPLVGA--TPEDLLAEAEAaARAGADLVELRLDYLEDPDLEELKELLEALREYGG-LPLIFTFRTAEEGGEFE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  80 FTNDSYLNLISDLANINGIDMIDIEWqaDIDIEKHQRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYV 159
Cdd:COG0710   78 GSEEERLELLRAAADSAGVDLVDVEL--DTLEDDVDDLIEAAREAGVKVIVSYHDFEKTPSAEELVEILEKMQELGADIV 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613174455 160 KLAVMPHNKNDVLNLLQSMSTFSDTMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGEPQAPGQIDVTDLK 232
Cdd:COG0710  156 KIAVMAKSPEDVLRLLEATLEAKEELDRPVITMAMGELGKISRILGPLFGSALTYASVGEASAPGQIDVEELR 228
DHQase_I cd00502
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ...
6-233 9.35e-68

Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase). Catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate to produce dehydroshikimate. Dehydroquinase is the third enzyme in the shikimate pathway, which is involved in the biosynthesis of aromatic amino acids. Type I DHQase exists as a homodimer. Type II 3-dehydroquinase also catalyzes the same overall reaction, but is unrelated in terms of sequence and structure, and utilizes a completely different reaction mechanism.


Pssm-ID: 188633  Cd Length: 225  Bit Score: 208.35  E-value: 9.35e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   6 VVATI-APQLYIEETLIQKINHRIDAIdvlELRIDQIENVTVDQVAEMITKLKVMqDSFKLLVTYRTKLQGGYGQFTNDS 84
Cdd:cd00502    2 ICVPLtGPDLLEEALSLLELLLGADAV---ELRVDLLEDPSIDDVAEQLSLLREL-TPLPIIFTVRTKSEGGNFEGSEEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  85 YLNLISDLANInGIDMIDIEWqadiDIEKHQRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYVKLAVM 164
Cdd:cd00502   78 YLELLEEALKL-GPDYVDIEL----DSALLEELINSRKKGNTKIIGSYHDFSGTPSDEELVSRLEKMAALGADIVKIAVM 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613174455 165 PHNKNDVLNLLQSMSTFSDTMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGEPQAPGQIDVTDLKA 233
Cdd:cd00502  153 ANSIEDNLRLLKFTRQVKNLYDIPLIAINMGELGKLSRILSPVFGSPLTYASLPEPSAPGQLSVEELKQ 221
DHquinase_I pfam01487
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ...
18-232 9.16e-54

Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate giving dehydroshikimate. Dehydroquinase functions in the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Type II 3-dehydroquinase catalyzes the trans-dehydration of 3-dehydroshikimate see pfam01220.


Pssm-ID: 426287  Cd Length: 227  Bit Score: 172.74  E-value: 9.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   18 ETLIQKINHRIDAIDVLELRIDQIENV--TVDQVAEMITKLKVMQDsFKLLVTYRTKLQGGYGQFTNDSYLNLISDLANi 95
Cdd:pfam01487  10 EEILEELESGKEGADLVELRVDLLEEPveDAEDVSEQLALLRRVGD-LPLIFTFRTKSEGGEPDGSEEEYLELLRLALR- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   96 NGIDMIDIEWQADIDIEKhqRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYVKLAVMPHNKNDVLNLL 175
Cdd:pfam01487  88 LGVDYVDVELFLPEEILK--ELIEAKHEGGTKVIGSYHDFEGTPSWEELISRYEKMQALGADIVKIAVMAKSIEDVLALL 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 613174455  176 QSMSTFSDTMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGEPQ--APGQIDVTDLK 232
Cdd:pfam01487 166 RFTSEMKSLADKPLIAMSMGELGRISRVLGPIFGSPVTFAALGLAEksAPGQLTAKELR 224
aroD PRK02412
type I 3-dehydroquinate dehydratase;
4-232 3.80e-51

type I 3-dehydroquinate dehydratase;


Pssm-ID: 235036  Cd Length: 253  Bit Score: 166.61  E-value: 3.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   4 VEVVATIAPQLYIEETLIQKINhridaIDVLELRIDQIENVT-VDQVAEMITKLKVMQDSFKLLVTYRTKLQGGYGQFTN 82
Cdd:PRK02412  20 VPIMGKTLEEVLAEALAISKYD-----ADIIEWRADFLEKISdVESVLAAAPAIREKFAGKPLLFTFRTAKEGGEIALSD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  83 DSYLNLISDLANINGIDMIDIEWQADIDIEKhqRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYVKLA 162
Cdd:PRK02412  95 EEYLALIKAVIKSGLPDYIDVELFSGKDVVK--EMVAFAHEHGVKVVLSYHDFEKTPPKEEIVERLRKMESLGADIVKIA 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613174455 163 VMPHNKNDVLNLLQSMSTFSD-TMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGEPQAPGQIDVTDLK 232
Cdd:PRK02412 173 VMPQSEQDVLTLLNATREMKElYADQPLITMSMGKLGRISRLAGEVFGSSWTFASLDKASAPGQISVEDLR 243
aroD TIGR01093
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ...
32-233 1.88e-49

3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, either as a monofunctional protein or as a domain of a larger, multifunctional protein. It is often found fused to shikimate 5-dehydrogenase (EC 1.1.1.25), and sometimes additional domains. Type II 3-dehydroquinate dehydratase, designated AroQ, is described by the model TIGR01088. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273439  Cd Length: 229  Bit Score: 161.78  E-value: 1.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455   32 DVLELRIDQIENVT-VDQVAEMITKLKVMQDSFKLLVTYRTKLQGGYGQFTNDSYLNLISDLANINGIDMIDIEWQADID 110
Cdd:TIGR01093  27 DIVELRVDLLKDVSsNNDVDALSEQLSELRVDKPLIFTIRTQSEGGKFPGNEEEYFEELKRAAESLGPDFVDIELFLPDD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  111 IEKhqRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYVKLAVMPHNKNDVLNLLQSMSTFSDTMDCKVV 190
Cdd:TIGR01093 107 AVK--ELINIAKKGGTKIIMSNHDFQKTPSWEEIVERLRKALSYGADIVKIAVMANSKEDVLTLLSATNKVDTHYDVPLI 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 613174455  191 GISMSKLGLISRTAQGVFGGALTYGCIGEPQAPGQIDVTDLKA 233
Cdd:TIGR01093 185 TMSMGDRGKISRVLGAVFGSVLTFGSLGKASAPGQISVDDLRE 227
PLN02520 PLN02520
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
16-231 1.55e-19

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase


Pssm-ID: 178135 [Multi-domain]  Cd Length: 529  Bit Score: 86.74  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  16 IEETLIQKINHRIDAIDVLELRIDQIENVTVDQVAEMITKlkvmQDSFKLLVTYRTKLQGGygQFTNDS-----YLNLIS 90
Cdd:PLN02520  34 VDKMLIEMAKAKELGADLVEIRLDFLKNFNPREDLKTLIK----QSPLPTLVTYRPKWEGG--QYEGDEnkrqdALRLAM 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  91 DLaninGIDMIDIEWQAdidIEKHQRIITHLQQYNKEVIISHHNFESTPPLDELQFIFFKMQKFNPEYVKLAVMPHNKND 170
Cdd:PLN02520 108 EL----GADYVDVELKV---AHEFINSISGKKPEKCKVIVSSHNYENTPSVEELGNLVARIQATGADIVKIATTALDITD 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613174455 171 VLNLLQSMStfsdtmDCKV--VGISMSKLGLISRTAQGVFGGALTYGCI--GEPQAPGQIDVTDL 231
Cdd:PLN02520 181 VARMFQITV------HSQVptIGLVMGERGLISRILCPKFGGYLTFGTLeaGKVSAPGQPTIKDL 239
PRK13576 PRK13576
type I 3-dehydroquinate dehydratase;
21-232 5.02e-11

type I 3-dehydroquinate dehydratase;


Pssm-ID: 237433  Cd Length: 216  Bit Score: 60.15  E-value: 5.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  21 IQKINHRIDAiDVLELRIDQIENVTVDqVAEMITKLKVmqdsfKLLVTYRTKLQGGYGQFTNDSYLNLISDLANINgiDM 100
Cdd:PRK13576  17 LKLIGNFLDA-DLIELRLDYLKDREVS-VIEFLDKYKD-----KLIVTLRDKAEGGINELDDELKISLLKELYDKQ--FL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455 101 IDIEwqadidiekhqriITHLQQYN---KEVIISHHNFESTPPLDELQFIFfkmQKFNPE--YVKLAVMPhnKNDVLNLL 175
Cdd:PRK13576  88 YDVE-------------ASFLQKYNvpyDNKIVSIHYFDYLPTSEEVKEIV---SKFYEKafSVKIAVLG--LKGYKEVL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 613174455 176 QSMSTFSdtmdcKVVGISMSKLGLiSRTAQGVFGGALTYGCIGEPQAPGQIDVTDLK 232
Cdd:PRK13576 150 LPLLEYE-----NVTVMPMSVNPL-ERIAFSLLGSKLIYSYAIEPTAQGQLHYKKVK 200
aroD PRK01261
3-dehydroquinate dehydratase; Provisional
32-227 2.55e-04

3-dehydroquinate dehydratase; Provisional


Pssm-ID: 234930  Cd Length: 229  Bit Score: 41.03  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455  32 DVLELRIDQIENVTVDQVAEMITKLKVMqdSFKLLVTYRTKLQGGYGQfTNDSYLnlisdlaningidmidiEWQADIDI 111
Cdd:PRK01261  48 NLYEIRFDLFHDHSIESEPEIISALNEM--DIDYIFTYRGVDARKYYE-TAIDKM-----------------PPAVDLDI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613174455 112 EKHQRIitHLQQYNKEVIISHHNFEStpplDELQFIFFKMQKFNPEYVKLAVMPHNKNDVLNLLQSMSTFSDTMDCKVVG 191
Cdd:PRK01261 108 NLIGKL--EFRPRNTMLMVSYHTNNS----DNMPAILDIMNEKNPDYVKVACNYNDNKKFVDDLQYILMKKDEKYKPIVF 181
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 613174455 192 ISMSKLGLisRTAQGVFGGALTYGCIGEPQAPGQID 227
Cdd:PRK01261 182 IPMGREFL--RIFSGYYVSDIVYARYDNETAPGQPK 215
 
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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