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Conserved domains on  [gi|1027696493|ref|WP_063632618|]
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shikimate dehydrogenase [Streptococcus pyogenes]

Protein Classification

shikimate dehydrogenase( domain architecture ID 11478370)

(NADP(+)) dependent shikimate dehydrogenase catalyzes the reversible reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA), part of the chorismate biosynthesis pathway

CATH:  3.40.50.720
Gene Ontology:  GO:0004764|GO:0050661|GO:0009423
PubMed:  17825835
SCOP:  4000101

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
14-307 1.64e-82

shikimate 5-dehydrogenase; Reviewed


:

Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 250.49  E-value: 1.64e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  14 RRMKFMYSALLGNPVEHSISDELFEYLNHNIGvlDEYKHKKILVDSVCLEDKIKYLINDpKCIGLNITLPYKREVMRYID 93
Cdd:PRK00258    1 ITGKTRLYAVIGNPIAHSKSPLIHNAAFKQLG--LDGVYLAILVPPEDLEDAVKGFFAL-GGRGANVTVPFKEAAFALAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  94 NLDRVAEITGSVNNIYKSGNIITGTNTDWKGIYNTLVFFN--ISHITKCCVLGTGGTARAAIFTLQKLQISPTVVY-REP 170
Cdd:PRK00258   78 ELSERARLIGAVNTLVLEDGRLIGDNTDGIGFVRALEERLgvDLKGKRILILGAGGAARAVILPLLDLGVAEITIVnRTV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 171 isENTRSLIKSFPDLKYITYkELADQQILNDMEIIINTTPVGMINyeeSLPINFDHLDNVNyKDKYFMDVVFNPLHTKLH 250
Cdd:PRK00258  158 --ERAEELAKLFGALGKAEL-DLELQEELADFDLIINATSAGMSG---ELPLPPLPLSLLR-PGTIVYDMIYGPLPTPFL 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1027696493 251 EYFGKKGAKIIDGLWVLIFQGIEAFSLWSDKindgkyffsKDDVVLIHTFLEGKIKG 307
Cdd:PRK00258  231 AWAKAQGARTIDGLGMLVHQAAEAFELWTGV---------RPPVEPMLAALRAALAA 278
 
Name Accession Description Interval E-value
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
14-307 1.64e-82

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 250.49  E-value: 1.64e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  14 RRMKFMYSALLGNPVEHSISDELFEYLNHNIGvlDEYKHKKILVDSVCLEDKIKYLINDpKCIGLNITLPYKREVMRYID 93
Cdd:PRK00258    1 ITGKTRLYAVIGNPIAHSKSPLIHNAAFKQLG--LDGVYLAILVPPEDLEDAVKGFFAL-GGRGANVTVPFKEAAFALAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  94 NLDRVAEITGSVNNIYKSGNIITGTNTDWKGIYNTLVFFN--ISHITKCCVLGTGGTARAAIFTLQKLQISPTVVY-REP 170
Cdd:PRK00258   78 ELSERARLIGAVNTLVLEDGRLIGDNTDGIGFVRALEERLgvDLKGKRILILGAGGAARAVILPLLDLGVAEITIVnRTV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 171 isENTRSLIKSFPDLKYITYkELADQQILNDMEIIINTTPVGMINyeeSLPINFDHLDNVNyKDKYFMDVVFNPLHTKLH 250
Cdd:PRK00258  158 --ERAEELAKLFGALGKAEL-DLELQEELADFDLIINATSAGMSG---ELPLPPLPLSLLR-PGTIVYDMIYGPLPTPFL 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1027696493 251 EYFGKKGAKIIDGLWVLIFQGIEAFSLWSDKindgkyffsKDDVVLIHTFLEGKIKG 307
Cdd:PRK00258  231 AWAKAQGARTIDGLGMLVHQAAEAFELWTGV---------RPPVEPMLAALRAALAA 278
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
22-278 3.10e-55

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 180.34  E-value: 3.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  22 ALLGNPVEHSISDEL----FEYLNHNIgvldEYKhkKILVDSVCLEDKIKyLINDPKCIGLNITLPYKREVMRYIDNLDR 97
Cdd:COG0169     8 GVIGDPIAHSLSPAIhnaaFAALGLDA----VYV--AFDVPPEDLAAAVA-GLRALGIRGLNVTIPHKEAAIPLLDELDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  98 VAEITGSVNNIYKSGNIITGTNTDWKGIYNTLVFFNIS-HITKCCVLGTGGTARAAIFTLQKLQISP-TVVYREPisENT 175
Cdd:COG0169    81 RARLIGAVNTVVFEDGRLIGDNTDGIGFVRALREAGVDlAGKRVLVLGAGGAARAVAAALAEAGAAEiTIVNRTP--ERA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 176 RSLIKSFPdLKYITYKELADqqILNDMEIIINTTPVGMINyEESLPINFDHLDnvnyKDKYFMDVVFNPLHTKLHEYFGK 255
Cdd:COG0169   159 EALAARLG-VRAVPLDDLAA--ALAGADLVINATPLGMAG-GDALPLPASLLA----PGAVVYDLVYNPLETPLLRAARA 230
                         250       260
                  ....*....|....*....|...
gi 1027696493 256 KGAKIIDGLWVLIFQGIEAFSLW 278
Cdd:COG0169   231 RGARVIDGLGMLVHQAAEAFELW 253
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
120-278 8.07e-43

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 144.34  E-value: 8.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 120 TDWKGIYNTLVFFNIS-HITKCCVLGTGGTARAAIFTLQKLQISP-TVVYREPisENTRSLIKSFPDLKYItYKELADQQ 197
Cdd:cd01065     1 TDGLGFVRALEEAGIElKGKKVLILGAGGAARAVAYALAELGAAKiVIVNRTL--EKAKALAERFGELGIA-IAYLDLEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 198 ILNDMEIIINTTPVGMiNYEESLPINFDHLDnvnyKDKYFMDVVFNPLHTKLHEYFGKKGAKIIDGLWVLIFQGIEAFSL 277
Cdd:cd01065    78 LLAEADLIINTTPVGM-KPGDELPLPPSLLK----PGGVVYDVVYNPLETPLLKEARALGAKTIDGLEMLVYQAAEAFEL 152

                  .
gi 1027696493 278 W 278
Cdd:cd01065   153 W 153
aroE TIGR00507
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ...
22-279 2.66e-34

shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally equivalent domains from larger, multifunctional proteins of fungi and plants. Below the trusted cutoff of 180, but above the noise cutoff of 20, are the putative shikimate dehydrogenases of Thermotoga maritima and Mycobacterium tuberculosis, and uncharacterized paralogs of shikimate dehydrogenase from E. coli and H. influenzae. The related enzyme quinate 5-dehydrogenase scores below the noise cutoff. A neighbor-joining tree, constructed with quinate 5-dehydrogenases as the outgroup, shows the Clamydial homolog as clustering among the shikimate dehydrogenases, although the sequence is unusual in the degree of sequence divergence and the presence of an additional N-terminal domain. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161904 [Multi-domain]  Cd Length: 270  Bit Score: 125.99  E-value: 2.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  22 ALLGNPVEHSISdelfeYLNHNIGVLD---EYKHKKILVDSVCLEDKIKYLINDPkCIGLNITLPYKREVMRYIDNLDRV 98
Cdd:TIGR00507   4 GVIGNPIAHSKS-----PLIHNAFFKQlglEGPYIAFLVPPDDLEDALSGFFALG-FKGANVTSPFKERAFQFLDEIDGR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  99 AEITGSVNNIYKSGNIITGTNTDWKGIYNTLVFFN-ISHITKCCVLGTGGTARAAIFTLQKLQISPTVVYREpiSENTRS 177
Cdd:TIGR00507  78 AKLAGAVNTLVLEDGKLVGYNTDGIGLVSDLEQLIpLRPNQNVLIIGAGGAAKAVALELLKADCNVIIANRT--VSKAEE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 178 LIKSFPDLKYITYKELADQQiLNDMEIIINTTPVGMINYEESLPINFDHLDnvnyKDKYFMDVVFNPLHTKLHEYFGKKG 257
Cdd:TIGR00507 156 LAERFQRYGEIQAFSMDELP-LHRVDLIINATSAGMSGNIDEPPVPAEYLK----EGKLVYDLVYNPLETPFLAEAKSLG 230
                         250       260
                  ....*....|....*....|..
gi 1027696493 258 AKIIDGLWVLIFQGIEAFSLWS 279
Cdd:TIGR00507 231 TKTIDGLGMLVYQAALSFELWT 252
Shikimate_dh_N pfam08501
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ...
23-108 1.70e-10

Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain of shikimate dehydrogenase.


Pssm-ID: 400688 [Multi-domain]  Cd Length: 83  Bit Score: 56.45  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  23 LLGNPVEHSIS----DELFEYLNHNigvlDEYKHKKILVDSvcLEDKIKYLInDPKCIGLNITLPYKREVMRYIDNLDRV 98
Cdd:pfam08501   1 VIGNPISHSLSpaihNAAFKALGLN----GVYVAFEVPPDN--LPDFVEGLR-ALGFRGLNVTIPHKEAAIPLLDELSPE 73
                          90
                  ....*....|
gi 1027696493  99 AEITGSVNNI 108
Cdd:pfam08501  74 AKAIGAVNTI 83
 
Name Accession Description Interval E-value
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
14-307 1.64e-82

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 250.49  E-value: 1.64e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  14 RRMKFMYSALLGNPVEHSISDELFEYLNHNIGvlDEYKHKKILVDSVCLEDKIKYLINDpKCIGLNITLPYKREVMRYID 93
Cdd:PRK00258    1 ITGKTRLYAVIGNPIAHSKSPLIHNAAFKQLG--LDGVYLAILVPPEDLEDAVKGFFAL-GGRGANVTVPFKEAAFALAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  94 NLDRVAEITGSVNNIYKSGNIITGTNTDWKGIYNTLVFFN--ISHITKCCVLGTGGTARAAIFTLQKLQISPTVVY-REP 170
Cdd:PRK00258   78 ELSERARLIGAVNTLVLEDGRLIGDNTDGIGFVRALEERLgvDLKGKRILILGAGGAARAVILPLLDLGVAEITIVnRTV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 171 isENTRSLIKSFPDLKYITYkELADQQILNDMEIIINTTPVGMINyeeSLPINFDHLDNVNyKDKYFMDVVFNPLHTKLH 250
Cdd:PRK00258  158 --ERAEELAKLFGALGKAEL-DLELQEELADFDLIINATSAGMSG---ELPLPPLPLSLLR-PGTIVYDMIYGPLPTPFL 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1027696493 251 EYFGKKGAKIIDGLWVLIFQGIEAFSLWSDKindgkyffsKDDVVLIHTFLEGKIKG 307
Cdd:PRK00258  231 AWAKAQGARTIDGLGMLVHQAAEAFELWTGV---------RPPVEPMLAALRAALAA 278
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
22-278 3.10e-55

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 180.34  E-value: 3.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  22 ALLGNPVEHSISDEL----FEYLNHNIgvldEYKhkKILVDSVCLEDKIKyLINDPKCIGLNITLPYKREVMRYIDNLDR 97
Cdd:COG0169     8 GVIGDPIAHSLSPAIhnaaFAALGLDA----VYV--AFDVPPEDLAAAVA-GLRALGIRGLNVTIPHKEAAIPLLDELDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  98 VAEITGSVNNIYKSGNIITGTNTDWKGIYNTLVFFNIS-HITKCCVLGTGGTARAAIFTLQKLQISP-TVVYREPisENT 175
Cdd:COG0169    81 RARLIGAVNTVVFEDGRLIGDNTDGIGFVRALREAGVDlAGKRVLVLGAGGAARAVAAALAEAGAAEiTIVNRTP--ERA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 176 RSLIKSFPdLKYITYKELADqqILNDMEIIINTTPVGMINyEESLPINFDHLDnvnyKDKYFMDVVFNPLHTKLHEYFGK 255
Cdd:COG0169   159 EALAARLG-VRAVPLDDLAA--ALAGADLVINATPLGMAG-GDALPLPASLLA----PGAVVYDLVYNPLETPLLRAARA 230
                         250       260
                  ....*....|....*....|...
gi 1027696493 256 KGAKIIDGLWVLIFQGIEAFSLW 278
Cdd:COG0169   231 RGARVIDGLGMLVHQAAEAFELW 253
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
120-278 8.07e-43

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 144.34  E-value: 8.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 120 TDWKGIYNTLVFFNIS-HITKCCVLGTGGTARAAIFTLQKLQISP-TVVYREPisENTRSLIKSFPDLKYItYKELADQQ 197
Cdd:cd01065     1 TDGLGFVRALEEAGIElKGKKVLILGAGGAARAVAYALAELGAAKiVIVNRTL--EKAKALAERFGELGIA-IAYLDLEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 198 ILNDMEIIINTTPVGMiNYEESLPINFDHLDnvnyKDKYFMDVVFNPLHTKLHEYFGKKGAKIIDGLWVLIFQGIEAFSL 277
Cdd:cd01065    78 LLAEADLIINTTPVGM-KPGDELPLPPSLLK----PGGVVYDVVYNPLETPLLKEARALGAKTIDGLEMLVYQAAEAFEL 152

                  .
gi 1027696493 278 W 278
Cdd:cd01065   153 W 153
aroE TIGR00507
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ...
22-279 2.66e-34

shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally equivalent domains from larger, multifunctional proteins of fungi and plants. Below the trusted cutoff of 180, but above the noise cutoff of 20, are the putative shikimate dehydrogenases of Thermotoga maritima and Mycobacterium tuberculosis, and uncharacterized paralogs of shikimate dehydrogenase from E. coli and H. influenzae. The related enzyme quinate 5-dehydrogenase scores below the noise cutoff. A neighbor-joining tree, constructed with quinate 5-dehydrogenases as the outgroup, shows the Clamydial homolog as clustering among the shikimate dehydrogenases, although the sequence is unusual in the degree of sequence divergence and the presence of an additional N-terminal domain. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161904 [Multi-domain]  Cd Length: 270  Bit Score: 125.99  E-value: 2.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  22 ALLGNPVEHSISdelfeYLNHNIGVLD---EYKHKKILVDSVCLEDKIKYLINDPkCIGLNITLPYKREVMRYIDNLDRV 98
Cdd:TIGR00507   4 GVIGNPIAHSKS-----PLIHNAFFKQlglEGPYIAFLVPPDDLEDALSGFFALG-FKGANVTSPFKERAFQFLDEIDGR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  99 AEITGSVNNIYKSGNIITGTNTDWKGIYNTLVFFN-ISHITKCCVLGTGGTARAAIFTLQKLQISPTVVYREpiSENTRS 177
Cdd:TIGR00507  78 AKLAGAVNTLVLEDGKLVGYNTDGIGLVSDLEQLIpLRPNQNVLIIGAGGAAKAVALELLKADCNVIIANRT--VSKAEE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 178 LIKSFPDLKYITYKELADQQiLNDMEIIINTTPVGMINYEESLPINFDHLDnvnyKDKYFMDVVFNPLHTKLHEYFGKKG 257
Cdd:TIGR00507 156 LAERFQRYGEIQAFSMDELP-LHRVDLIINATSAGMSGNIDEPPVPAEYLK----EGKLVYDLVYNPLETPFLAEAKSLG 230
                         250       260
                  ....*....|....*....|..
gi 1027696493 258 AKIIDGLWVLIFQGIEAFSLWS 279
Cdd:TIGR00507 231 TKTIDGLGMLVYQAALSFELWT 252
PRK12548 PRK12548
shikimate dehydrogenase;
22-281 1.83e-24

shikimate dehydrogenase;


Pssm-ID: 183585 [Multi-domain]  Cd Length: 289  Bit Score: 100.20  E-value: 1.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  22 ALLGNPVEHSISDELFEYLNHNIGVLDEYKHKKILVDSVclEDKIKyLINDPKCIGLNITLPYKREVMRYIDNLDRVAEI 101
Cdd:PRK12548   13 GLIGSPVGHSGSPAMYNYSFQKAGLDYAYLAFDIPVDKV--PDAIK-AIKTFNMRGANVTMPCKSEAAKYMDELSPAARI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 102 TGSVNNIYKSGNIITGTNTDWKGIYNTL----VFFNISHITkccVLGTGGTARA-------------AIFTLQKlqispt 164
Cdd:PRK12548   90 IGAVNTIVNDDGKLTGHITDGLGFVRNLrehgVDVKGKKLT---VIGAGGAATAiqvqcaldgakeiTIFNIKD------ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 165 vVYREPISENTRSLIKSFPDLKYITYkELADQQILN----DMEIIINTTPVGMINYEESLPINfdhlD-NVNYKDKYFMD 239
Cdd:PRK12548  161 -DFYERAEQTAEKIKQEVPECIVNVY-DLNDTEKLKaeiaSSDILVNATLVGMKPNDGETNIK----DtSVFRKDLVVAD 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1027696493 240 VVFNPLHTKLHEYFGKKGAKIIDGLWVLIFQGIEAFSLWSDK 281
Cdd:PRK12548  235 TVYNPKKTKLLEDAEAAGCKTVGGLGMLLWQGAEAYKLYTGK 276
PRK12749 PRK12749
quinate/shikimate dehydrogenase; Reviewed
17-281 4.54e-20

quinate/shikimate dehydrogenase; Reviewed


Pssm-ID: 183721 [Multi-domain]  Cd Length: 288  Bit Score: 88.14  E-value: 4.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  17 KFMYSALLGNPVEHSISDELFEYLNHNIGVldEYKHKKILVDSVCLEDKIKYLiNDPKCIGLNITLPYKREVMRYIDNLD 96
Cdd:PRK12749    6 KYELIGLMAYPIRHSLSPEMQNKALEKAGL--PFTYMAFEVDNDSFPGAIEGL-KALKMRGTGVSMPNKQLACEYVDELT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  97 RVAEITGSVNNIYKSGNIITGTNTDWKGIYNTL--VFFNISHITKCcVLGTGGT-----ARAAIFTLQKLQI-------- 161
Cdd:PRK12749   83 PAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIkeSGFDIKGKTMV-LLGAGGAstaigAQGAIEGLKEIKLfnrrdeff 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 162 SPTVVYREPISENTRSLIksfpdlkyiTYKELADQQILNDM----EIIINTTPVGMINYEESLPINfdhldnvnykDKYF 237
Cdd:PRK12749  162 DKALAFAQRVNENTDCVV---------TVTDLADQQAFAEAlasaDILTNGTKVGMKPLENESLVN----------DISL 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1027696493 238 M-------DVVFNPLHTKLHEYFGKKGAKIIDGLWVLIFQGIEAFSLWSDK 281
Cdd:PRK12749  223 LhpgllvtECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGK 273
aroDE PRK09310
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;
22-278 5.20e-17

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;


Pssm-ID: 137204 [Multi-domain]  Cd Length: 477  Bit Score: 81.00  E-value: 5.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  22 ALLGNPVEHSISdelfeYLNHN-----IGVLDEYKhkKILVDSVCLEDKIKyLINDPKCIGLNITLPYKREVMRYIDNLD 96
Cdd:PRK09310  219 GLIGDPVDRSIS-----HLSHNplfsqLSLNCPYI--KLPLTPQELPKFFS-TIRDLPFLGLSVTMPLKTAVLDFLDKLD 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  97 RVAEITGSVNNIYKSGNIITGTNTDWKGIYNTLVFFNIS-HITKCCVLGTGGTAR--AAIFTLQKLQIS---PTVVYREP 170
Cdd:PRK09310  291 PSVKLCGSCNTLVFRNGKIEGYNTDGEGLFSLLKQKNIPlNNQHVAIVGAGGAAKaiATTLARAGAELLifnRTKAHAEA 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 171 ISenTRSLIKSFPdlkyitykeLADQQILNDMEIIINTTPVGMINYEESLPInfdhldnvnykdkyFMDVVFNPLHTKLH 250
Cdd:PRK09310  371 LA--SRCQGKAFP---------LESLPELHRIDIIINCLPPSVTIPKAFPPC--------------VVDINTLPKHSPYT 425
                         250       260
                  ....*....|....*....|....*...
gi 1027696493 251 EYFGKKGAKIIDGLWVLIFQGIEAFSLW 278
Cdd:PRK09310  426 QYARSQGSSIIYGYEMFAEQALLQFRLW 453
PRK12550 PRK12550
shikimate 5-dehydrogenase; Reviewed
77-278 1.11e-14

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 183587 [Multi-domain]  Cd Length: 272  Bit Score: 72.68  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  77 GLNITLPYKREVMRYIDNLDRVAEITGSVNNIYKSGNIITGTNTDWKGIYNTLVFFNISHITKCCVLGTGGTARAAIFTL 156
Cdd:PRK12550   62 GCAVSMPFKEAVIPLVDELDPSAQAIESVNTIVNTDGHLKAYNTDYIAIAKLLASYQVPPDLVVALRGSGGMAKAVAAAL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 157 QKLQISP-TVVYREPisentrsliksfpdlkyITYKELADQ---QILNDME-----IIINTTPVGMINYEESLPINFDhL 227
Cdd:PRK12550  142 RDAGFTDgTIVARNE-----------------KTGKALAELygyEWRPDLGgieadILVNVTPIGMAGGPEADKLAFP-E 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1027696493 228 DNVNYKDKYFmDVVFNPLHTKLHEYFGKKGAKIIDGLWVLIFQGIEAFSLW 278
Cdd:PRK12550  204 AEIDAASVVF-DVVALPAETPLIRYARARGKTVITGAEVIALQAVEQFVLY 253
PRK12549 PRK12549
shikimate 5-dehydrogenase; Reviewed
77-279 1.39e-11

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 183586 [Multi-domain]  Cd Length: 284  Bit Score: 63.76  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  77 GLNITLPYKREVMRYIDNLDRVAEITGSVNNI-YKSGNIItGTNTDWKGIY----NTLVFFNISHITKccvLGTGGTARA 151
Cdd:PRK12549   66 GLNITHPCKQAVIPHLDELSDDARALGAVNTVvFRDGRRI-GHNTDWSGFAesfrRGLPDASLERVVQ---LGAGGAGAA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 152 AIFTLQKLQI-SPTVVYREPisenTRS------LIKSFPDLKYITYKELAdqQILNDMEIIINTTPVGMINYeESLPINF 224
Cdd:PRK12549  142 VAHALLTLGVeRLTIFDVDP----ARAaaladeLNARFPAARATAGSDLA--AALAAADGLVHATPTGMAKH-PGLPLPA 214
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1027696493 225 DHLDnvnyKDKYFMDVVFNPLHTKLHEYFGKKGAKIIDGLWVLIFQGIEAFSLWS 279
Cdd:PRK12549  215 ELLR----PGLWVADIVYFPLETELLRAARALGCRTLDGGGMAVFQAVDAFELFT 265
Shikimate_dh_N pfam08501
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ...
23-108 1.70e-10

Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain of shikimate dehydrogenase.


Pssm-ID: 400688 [Multi-domain]  Cd Length: 83  Bit Score: 56.45  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  23 LLGNPVEHSIS----DELFEYLNHNigvlDEYKHKKILVDSvcLEDKIKYLInDPKCIGLNITLPYKREVMRYIDNLDRV 98
Cdd:pfam08501   1 VIGNPISHSLSpaihNAAFKALGLN----GVYVAFEVPPDN--LPDFVEGLR-ALGFRGLNVTIPHKEAAIPLLDELSPE 73
                          90
                  ....*....|
gi 1027696493  99 AEITGSVNNI 108
Cdd:pfam08501  74 AKAIGAVNTI 83
PLN02520 PLN02520
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
23-275 9.08e-10

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase


Pssm-ID: 178135 [Multi-domain]  Cd Length: 529  Bit Score: 59.39  E-value: 9.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  23 LLGNPVEHSISDELFEYLNHNIGVLDEYKHkkILVDSVcledkIKYL--INDPKCIGLNITLPYKREVMRYIDNLDRVAE 100
Cdd:PLN02520  257 IIGKPVGHSKSPILHNEAFKSVGFNGVYVH--LLVDDL-----AKFLqtYSSPDFAGFSCTIPHKEDALKCCDEVDPIAK 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 101 ITGSVNNIYK--SGNIITGTNTDWKG----IYNTLVFFNISHITKC-------CVLGTGGTARAAIFTLQklQISPTVVy 167
Cdd:PLN02520  330 SIGAINTIIRrpSDGKLVGYNTDYIGaisaIEDGLRASGSSPASGSplagklfVVIGAGGAGKALAYGAK--EKGARVV- 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 168 repISENTRSLIKSFPDL---KYITYKELADQQILNDMeIIINTTPVGMINYEESLPINFDHLdnvNYKDKYFmDVVFNP 244
Cdd:PLN02520  407 ---IANRTYERAKELADAvggQALTLADLENFHPEEGM-ILANTTSVGMQPNVDETPISKHAL---KHYSLVF-DAVYTP 478
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1027696493 245 LHTKLHEYFGKKGAKIIDGLWVLIFQGIEAF 275
Cdd:PLN02520  479 KITRLLREAEESGAIIVSGTEMFIRQAYEQF 509
PRK14027 PRK14027
quinate/shikimate dehydrogenase (NAD+);
77-279 2.74e-09

quinate/shikimate dehydrogenase (NAD+);


Pssm-ID: 172521 [Multi-domain]  Cd Length: 283  Bit Score: 56.97  E-value: 2.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493  77 GLNITLPYKREVMRYIDNLDRVAEITGSVNNIYKSGN-IITGTNTDWKGIYNTL-VFFNISHITKCCVLGTGGTARAAIF 154
Cdd:PRK14027   65 GLNITHPYKQAVLPLLDEVSEQATQLGAVNTVVIDATgHTTGHNTDVSGFGRGMeEGLPNAKLDSVVQVGAGGVGNAVAY 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027696493 155 TL-----QKLQISPTVVYR-EPISENTRSLIKSFP----DLKYItykeladQQILNDMEIIINTTPVGMINYEESLpinF 224
Cdd:PRK14027  145 ALvthgvQKLQVADLDTSRaQALADVINNAVGREAvvgvDARGI-------EDVIAAADGVVNATPMGMPAHPGTA---F 214
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1027696493 225 DhlDNVNYKDKYFMDVVFNPLHTKLHEYFGKKGAKIIDGLWVLIFQGIEAFSLWS 279
Cdd:PRK14027  215 D--VSCLTKDHWVGDVVYMPIETELLKAARALGCETLDGTRMAIHQAVDAFRLFT 267
 
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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