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Conserved domains on  [gi|502109203|ref|WP_012711767|]
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type I 3-dehydroquinate dehydratase [Sulfolobus islandicus]

Protein Classification

triose-phosphate isomerase; tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like( domain architecture ID 10014283)

triose-phosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate| tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like (DUS1L) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13576 PRK13576
type I 3-dehydroquinate dehydratase;
1-220 2.07e-120

type I 3-dehydroquinate dehydratase;


:

Pssm-ID: 237433  Cd Length: 216  Bit Score: 340.58  E-value: 2.07e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   1 MRPLIVASLPIKKIEDLKLIGNFLDADLIELRLDYLKDREVSVisdyFEFLDKYKNKLIITLRDKAEGGINELADELKIS 80
Cdd:PRK13576   1 MRPLIVASLPIKKIEDLKLIGNFLDADLIELRLDYLKDREVSV----IEFLDKYKDKLIVTLRDKAEGGINELDDELKIS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203  81 LLKELYDKQFLYDVEVSFLQKHNVPYDNAIVSIHYFNYLPTSEKVKEIVSKFYEKAFSVKIAVLGLKGYKEVILPLLEYE 160
Cdd:PRK13576  77 LLKELYDKQFLYDVEASFLQKYNVPYDNKIVSIHYFDYLPTSEEVKEIVSKFYEKAFSVKIAVLGLKGYKEVLLPLLEYE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203 161 NVTVIPMSNNPLERIAVGLLGSKLVYSYAIEPLAQGQLYYKKVIQIFDYINNIITSSSVT 220
Cdd:PRK13576 157 NVTVMPMSVNPLERIAFSLLGSKLIYSYAIEPTAQGQLHYKKVKQILNYLNNIITSSSVT 216
 
Name Accession Description Interval E-value
PRK13576 PRK13576
type I 3-dehydroquinate dehydratase;
1-220 2.07e-120

type I 3-dehydroquinate dehydratase;


Pssm-ID: 237433  Cd Length: 216  Bit Score: 340.58  E-value: 2.07e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   1 MRPLIVASLPIKKIEDLKLIGNFLDADLIELRLDYLKDREVSVisdyFEFLDKYKNKLIITLRDKAEGGINELADELKIS 80
Cdd:PRK13576   1 MRPLIVASLPIKKIEDLKLIGNFLDADLIELRLDYLKDREVSV----IEFLDKYKDKLIVTLRDKAEGGINELDDELKIS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203  81 LLKELYDKQFLYDVEVSFLQKHNVPYDNAIVSIHYFNYLPTSEKVKEIVSKFYEKAFSVKIAVLGLKGYKEVILPLLEYE 160
Cdd:PRK13576  77 LLKELYDKQFLYDVEASFLQKYNVPYDNKIVSIHYFDYLPTSEEVKEIVSKFYEKAFSVKIAVLGLKGYKEVLLPLLEYE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203 161 NVTVIPMSNNPLERIAVGLLGSKLVYSYAIEPLAQGQLYYKKVIQIFDYINNIITSSSVT 220
Cdd:PRK13576 157 NVTVMPMSVNPLERIAFSLLGSKLIYSYAIEPTAQGQLHYKKVKQILNYLNNIITSSSVT 216
AroD COG0710
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-212 1.16e-42

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: 143.89  E-value: 1.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   1 MRPLIVASLPIKKIEDLKL---IGNFLDADLIELRLDYLKDREVSVISDYFEFLDKYKNK-LIITLRDKAEGGINELADE 76
Cdd:COG0710    2 GRPKICVPLVGATPEDLLAeaeAAARAGADLVELRLDYLEDPDLEELKELLEALREYGGLpLIFTFRTAEEGGEFEGSEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203  77 LKISLLKELYDKQ--FLYDVEVSFL-----------QKHNVPydnAIVSIHYFNYLPTSEKVKEIVSKFYEKAFSV-KIA 142
Cdd:COG0710   82 ERLELLRAAADSAgvDLVDVELDTLeddvddlieaaREAGVK---VIVSYHDFEKTPSAEELVEILEKMQELGADIvKIA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203 143 VLGlKGYKEViLPLL-------EYENVTVIPMSN---NPLERIAVGLLGSKLVYSYAIEPLAQGQLYYKKVIQIFDYINN 212
Cdd:COG0710  159 VMA-KSPEDV-LRLLeatleakEELDRPVITMAMgelGKISRILGPLFGSALTYASVGEASAPGQIDVEELRELLELLEA 236
DHQase_I cd00502
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ...
4-209 7.45e-32

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: 115.51  E-value: 7.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   4 LIVASLPIKKI--EDLKLIGNFLDADLIELRLDYLKDREVSVISDYFEFLDKYKN-KLIITLRDKAEGGINELADELKIS 80
Cdd:cd00502    1 KICVPLTGPDLleEALSLLELLLGADAVELRVDLLEDPSIDDVAEQLSLLRELTPlPIIFTVRTKSEGGNFEGSEEEYLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203  81 LLKELYDKQF-LYDVEVSF------LQKHNVPYDNAIVSIHYFNYLPTSEKVKEIVSKFY-EKAFSVKIAVLG--LKGYK 150
Cdd:cd00502   81 LLEEALKLGPdYVDIELDSalleelINSRKKGNTKIIGSYHDFSGTPSDEELVSRLEKMAaLGADIVKIAVMAnsIEDNL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502109203 151 EVILPLLEYEN-----VTVIPM-SNNPLERIAVGLLGSKLVYSYAIEPLAQGQLYYKKVIQIFDY 209
Cdd:cd00502  161 RLLKFTRQVKNlydipLIAINMgELGKLSRILSPVFGSPLTYASLPEPSAPGQLSVEELKQALSL 225
aroD TIGR01093
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ...
24-198 1.18e-09

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: 56.24  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   24 LDADLIELRLDYLKD----REVSVISDYFEFLDKYKnKLIITLRDKAEGGINELADELKISLLKELYDKQF--LYDVEVS 97
Cdd:TIGR01093  24 KGADIVELRVDLLKDvssnNDVDALSEQLSELRVDK-PLIFTIRTQSEGGKFPGNEEEYFEELKRAAESLGpdFVDIELF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   98 F-----------LQKHNVpydNAIVSIHYFNYLPTSEKVKEIVSKFYE-KAFSVKIAVLGLKgyKEVILPLLEYEN---- 161
Cdd:TIGR01093 103 LpddavkeliniAKKGGT---KIIMSNHDFQKTPSWEEIVERLRKALSyGADIVKIAVMANS--KEDVLTLLSATNkvdt 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 502109203  162 ---VTVIPMS---NNPLERIAVGLLGSKLVYSYAIEPLAQGQL 198
Cdd:TIGR01093 178 hydVPLITMSmgdRGKISRVLGAVFGSVLTFGSLGKASAPGQI 220
DHquinase_I pfam01487
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ...
14-143 2.51e-09

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: 55.25  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   14 IEDLKLIGNflDADLIELRLDYLKD--REVSVISDYFEFLDKYKNK-LIITLRDKAEGGINELADELKISLLKELYDKQF 90
Cdd:pfam01487  13 LEELESGKE--GADLVELRVDLLEEpvEDAEDVSEQLALLRRVGDLpLIFTFRTKSEGGEPDGSEEEYLELLRLALRLGV 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   91 LY-DVE-----------VSFLQKHNVPYdnaIVSIHYFNYLPTSEkvkEIVSKfYEKAFS-----VKIAV 143
Cdd:pfam01487  91 DYvDVElflpeeilkelIEAKHEGGTKV---IGSYHDFEGTPSWE---ELISR-YEKMQAlgadiVKIAV 153
 
Name Accession Description Interval E-value
PRK13576 PRK13576
type I 3-dehydroquinate dehydratase;
1-220 2.07e-120

type I 3-dehydroquinate dehydratase;


Pssm-ID: 237433  Cd Length: 216  Bit Score: 340.58  E-value: 2.07e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   1 MRPLIVASLPIKKIEDLKLIGNFLDADLIELRLDYLKDREVSVisdyFEFLDKYKNKLIITLRDKAEGGINELADELKIS 80
Cdd:PRK13576   1 MRPLIVASLPIKKIEDLKLIGNFLDADLIELRLDYLKDREVSV----IEFLDKYKDKLIVTLRDKAEGGINELDDELKIS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203  81 LLKELYDKQFLYDVEVSFLQKHNVPYDNAIVSIHYFNYLPTSEKVKEIVSKFYEKAFSVKIAVLGLKGYKEVILPLLEYE 160
Cdd:PRK13576  77 LLKELYDKQFLYDVEASFLQKYNVPYDNKIVSIHYFDYLPTSEEVKEIVSKFYEKAFSVKIAVLGLKGYKEVLLPLLEYE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203 161 NVTVIPMSNNPLERIAVGLLGSKLVYSYAIEPLAQGQLYYKKVIQIFDYINNIITSSSVT 220
Cdd:PRK13576 157 NVTVMPMSVNPLERIAFSLLGSKLIYSYAIEPTAQGQLHYKKVKQILNYLNNIITSSSVT 216
AroD COG0710
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-212 1.16e-42

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: 143.89  E-value: 1.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   1 MRPLIVASLPIKKIEDLKL---IGNFLDADLIELRLDYLKDREVSVISDYFEFLDKYKNK-LIITLRDKAEGGINELADE 76
Cdd:COG0710    2 GRPKICVPLVGATPEDLLAeaeAAARAGADLVELRLDYLEDPDLEELKELLEALREYGGLpLIFTFRTAEEGGEFEGSEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203  77 LKISLLKELYDKQ--FLYDVEVSFL-----------QKHNVPydnAIVSIHYFNYLPTSEKVKEIVSKFYEKAFSV-KIA 142
Cdd:COG0710   82 ERLELLRAAADSAgvDLVDVELDTLeddvddlieaaREAGVK---VIVSYHDFEKTPSAEELVEILEKMQELGADIvKIA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203 143 VLGlKGYKEViLPLL-------EYENVTVIPMSN---NPLERIAVGLLGSKLVYSYAIEPLAQGQLYYKKVIQIFDYINN 212
Cdd:COG0710  159 VMA-KSPEDV-LRLLeatleakEELDRPVITMAMgelGKISRILGPLFGSALTYASVGEASAPGQIDVEELRELLELLEA 236
DHQase_I cd00502
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ...
4-209 7.45e-32

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: 115.51  E-value: 7.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   4 LIVASLPIKKI--EDLKLIGNFLDADLIELRLDYLKDREVSVISDYFEFLDKYKN-KLIITLRDKAEGGINELADELKIS 80
Cdd:cd00502    1 KICVPLTGPDLleEALSLLELLLGADAVELRVDLLEDPSIDDVAEQLSLLRELTPlPIIFTVRTKSEGGNFEGSEEEYLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203  81 LLKELYDKQF-LYDVEVSF------LQKHNVPYDNAIVSIHYFNYLPTSEKVKEIVSKFY-EKAFSVKIAVLG--LKGYK 150
Cdd:cd00502   81 LLEEALKLGPdYVDIELDSalleelINSRKKGNTKIIGSYHDFSGTPSDEELVSRLEKMAaLGADIVKIAVMAnsIEDNL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502109203 151 EVILPLLEYEN-----VTVIPM-SNNPLERIAVGLLGSKLVYSYAIEPLAQGQLYYKKVIQIFDY 209
Cdd:cd00502  161 RLLKFTRQVKNlydipLIAINMgELGKLSRILSPVFGSPLTYASLPEPSAPGQLSVEELKQALSL 225
aroD PRK02412
type I 3-dehydroquinate dehydratase;
2-208 2.44e-13

type I 3-dehydroquinate dehydratase;


Pssm-ID: 235036  Cd Length: 253  Bit Score: 66.85  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   2 RPLIVASLPIKKIEDLK---LIGNFLDADLIELRLDYLKDREV--SVISDYFEFLDKYKNK-LIITLRDKAEGGINELAD 75
Cdd:PRK02412  15 APKIIVPIMGKTLEEVLaeaLAISKYDADIIEWRADFLEKISDveSVLAAAPAIREKFAGKpLLFTFRTAKEGGEIALSD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203  76 ELKISLLKELYDKQF--LYDVE-----------VSFLQKHNVpydNAIVSIHYFNYLPTSEkvkEIVSKFYEKAFS---- 138
Cdd:PRK02412  95 EEYLALIKAVIKSGLpdYIDVElfsgkdvvkemVAFAHEHGV---KVVLSYHDFEKTPPKE---EIVERLRKMESLgadi 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203 139 VKIAVLGlKGYKEViLPLL--------EYENVTVIPMSNNPL---ERIAVGLLGSKLVYSYAIEPLAQGQLY---YKKVI 204
Cdd:PRK02412 169 VKIAVMP-QSEQDV-LTLLnatremkeLYADQPLITMSMGKLgriSRLAGEVFGSSWTFASLDKASAPGQISvedLRRIL 246

                 ....
gi 502109203 205 QIFD 208
Cdd:PRK02412 247 EILH 250
aroD TIGR01093
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ...
24-198 1.18e-09

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: 56.24  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   24 LDADLIELRLDYLKD----REVSVISDYFEFLDKYKnKLIITLRDKAEGGINELADELKISLLKELYDKQF--LYDVEVS 97
Cdd:TIGR01093  24 KGADIVELRVDLLKDvssnNDVDALSEQLSELRVDK-PLIFTIRTQSEGGKFPGNEEEYFEELKRAAESLGpdFVDIELF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   98 F-----------LQKHNVpydNAIVSIHYFNYLPTSEKVKEIVSKFYE-KAFSVKIAVLGLKgyKEVILPLLEYEN---- 161
Cdd:TIGR01093 103 LpddavkeliniAKKGGT---KIIMSNHDFQKTPSWEEIVERLRKALSyGADIVKIAVMANS--KEDVLTLLSATNkvdt 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 502109203  162 ---VTVIPMS---NNPLERIAVGLLGSKLVYSYAIEPLAQGQL 198
Cdd:TIGR01093 178 hydVPLITMSmgdRGKISRVLGAVFGSVLTFGSLGKASAPGQI 220
DHquinase_I pfam01487
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ...
14-143 2.51e-09

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: 55.25  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   14 IEDLKLIGNflDADLIELRLDYLKD--REVSVISDYFEFLDKYKNK-LIITLRDKAEGGINELADELKISLLKELYDKQF 90
Cdd:pfam01487  13 LEELESGKE--GADLVELRVDLLEEpvEDAEDVSEQLALLRRVGDLpLIFTFRTKSEGGEPDGSEEEYLELLRLALRLGV 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   91 LY-DVE-----------VSFLQKHNVPYdnaIVSIHYFNYLPTSEkvkEIVSKfYEKAFS-----VKIAV 143
Cdd:pfam01487  91 DYvDVElflpeeilkelIEAKHEGGTKV---IGSYHDFEGTPSWE---ELISR-YEKMQAlgadiVKIAV 153
aroD PRK01261
3-dehydroquinate dehydratase; Provisional
1-209 1.68e-04

3-dehydroquinate dehydratase; Provisional


Pssm-ID: 234930  Cd Length: 229  Bit Score: 41.41  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203   1 MRPLIVASLPIKKIEDLK---LIGNFLDADLIELRLDYLKDREVSVISDYFEFLDKYKNKLIITLRDKAEGGINELADEL 77
Cdd:PRK01261  19 MQPIVVESIFFKDIKEMKerfKTKVLSDKNLYEIRFDLFHDHSIESEPEIISALNEMDIDYIFTYRGVDARKYYETAIDK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502109203  78 KISLLkelydkqflyDVEVSFLQKHNVPYDNAIVSIHYfnYLPTSEKVKEIVSKFYEK-AFSVKIAvLGLKGYKEVILPL 156
Cdd:PRK01261  99 MPPAV----------DLDINLIGKLEFRPRNTMLMVSY--HTNNSDNMPAILDIMNEKnPDYVKVA-CNYNDNKKFVDDL 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502109203 157 LE--------YENVTVIPMSNNPLeRIAVGLLGSKLVYSYAIEPLAQGQL---YYKKVIQIFDY 209
Cdd:PRK01261 166 QYilmkkdekYKPIVFIPMGREFL-RIFSGYYVSDIVYARYDNETAPGQPkrdYYESAFIKYGY 228
 
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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