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Conserved domains on  [gi|142000763|gb|ECU73706|]
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hypothetical protein GOS_3202964, partial [marine metagenome]

Protein Classification

shikimate dehydrogenase( domain architecture ID 10099435)

(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
EC:  1.1.1.25
Gene Ontology:  GO:0004764|GO:0070403
PubMed:  25704928|30945211

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 1-156 8.00e-46

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: 147.42  E-value: 8.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LRENKWSSQNKKILILGAGGVTSSILSSFIKAnGVLKIYLCNRTREKAEELKTLWDKavdssgmKKDTIEIVDWGKKIEL 80
Cdd:cd01065   10 LEEAGIELKGKKVLILGAGGAARAVAYALAEL-GAAKIVIVNRTLEKAKALAERFGE-------LGIAIAYLDLEELLAE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 142000763  81 CDLVINTTSVGLTKNENIKLNFSnyENKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTG 156
Cdd:cd01065   82 ADLIINTTPVGMKPGDELPLPPS--LLKPGGVVYDVVYNPLETPLLKEARALGAKTIDGLEMLVYQAAEAFELWTG 155
 
Name Accession Description Interval E-value
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 1-156 8.00e-46

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: 147.42  E-value: 8.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LRENKWSSQNKKILILGAGGVTSSILSSFIKAnGVLKIYLCNRTREKAEELKTLWDKavdssgmKKDTIEIVDWGKKIEL 80
Cdd:cd01065   10 LEEAGIELKGKKVLILGAGGAARAVAYALAEL-GAAKIVIVNRTLEKAKALAERFGE-------LGIAIAYLDLEELLAE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 142000763  81 CDLVINTTSVGLTKNENIKLNFSnyENKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTG 156
Cdd:cd01065   82 ADLIINTTPVGMKPGDELPLPPS--LLKPGGVVYDVVYNPLETPLLKEARALGAKTIDGLEMLVYQAAEAFELWTG 155
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 1-169 1.37e-42

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: 142.59  E-value: 1.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LRENKWSSQNKKILILGAGGVTSSILSSFIKAnGVLKIYLCNRTREKAEELKTLWDKAVdssgmkkdtIEIVDWGKKIEL 80
Cdd:COG0169  112 LREAGVDLAGKRVLVLGAGGAARAVAAALAEA-GAAEITIVNRTPERAEALAARLGVRA---------VPLDDLAAALAG 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  81 CDLVINTTSVGLTKNENIKLNFSNYenKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTGVSPK 160
Cdd:COG0169  182 ADLVINATPLGMAGGDALPLPASLL--APGAVVYDLVYNPLETPLLRAARARGARVIDGLGMLVHQAAEAFELWTGVRPP 259


                 ....*....
gi 142000763 161 InDEVINLL 169
Cdd:COG0169  260 V-EAMRAAL 267
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
 1-169 2.79e-41

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 139.55  E-value: 2.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LREN-KWSSQNKKILILGAGGVTSSILSSFIKAnGVLKIYLCNRTREKAEELKTLWDKAVDSSGmkkdtieIVDWGKKIE 79
Cdd:PRK00258 113 LEERlGVDLKGKRILILGAGGAARAVILPLLDL-GVAEITIVNRTVERAEELAKLFGALGKAEL-------DLELQEELA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  80 LCDLVINTTSVGLTKNENI-KLNFSNYenKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTGVS 158
Cdd:PRK00258 185 DFDLIINATSAGMSGELPLpPLPLSLL--RPGTIVYDMIYGPLPTPFLAWAKAQGARTIDGLGMLVHQAAEAFELWTGVR 262

                        170
                 ....*....|.
gi 142000763 159 PKInDEVINLL 169
Cdd:PRK00258 263 PPV-EPMLAAL 272
aroE TIGR00507
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ...
 1-161 1.39e-32

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: 116.75  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763    1 LRENKWSSQNKKILILGAGGVTSSILSSFIKANgvLKIYLCNRTREKAEELKTLWDKAVDSSGMKKDTIEIvdwgkkiEL 80
Cdd:TIGR00507 108 LEQLIPLRPNQNVLIIGAGGAAKAVALELLKAD--CNVIIANRTVSKAEELAERFQRYGEIQAFSMDELPL-------HR 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   81 CDLVINTTSVGLTKNENIKLNFSNYEnKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTGVSPK 160
Cdd:TIGR00507 179 VDLIINATSAGMSGNIDEPPVPAEYL-KEGKLVYDLVYNPLETPFLAEAKSLGTKTIDGLGMLVYQAALSFELWTGVEPD 257


                  .
gi 142000763  161 I 161
Cdd:TIGR00507 258 I 258
SDH_C pfam18317
Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of ...
 142-159 1.18e-03

Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of Shikimate 5'-dehydrogenase (SDH) present in Methanocaldococcus jannaschii. SDH catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate in the shikimate pathway. The domain is found just after the C-terminal domain (pfam01488) which is responsible for NADP binding.


Pssm-ID: 436404 [Multi-domain]  Cd Length: 31  Bit Score: 35.09  E-value: 1.18e-03
                          10
                  ....*....|....*...
gi 142000763  142 MFLWQAQLAFQMWTGVSP 159
Cdd:pfam18317   4 MLVEQGAEQFELWTGREP 21
 
Name Accession Description Interval E-value
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 1-156 8.00e-46

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: 147.42  E-value: 8.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LRENKWSSQNKKILILGAGGVTSSILSSFIKAnGVLKIYLCNRTREKAEELKTLWDKavdssgmKKDTIEIVDWGKKIEL 80
Cdd:cd01065   10 LEEAGIELKGKKVLILGAGGAARAVAYALAEL-GAAKIVIVNRTLEKAKALAERFGE-------LGIAIAYLDLEELLAE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 142000763  81 CDLVINTTSVGLTKNENIKLNFSnyENKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTG 156
Cdd:cd01065   82 ADLIINTTPVGMKPGDELPLPPS--LLKPGGVVYDVVYNPLETPLLKEARALGAKTIDGLEMLVYQAAEAFELWTG 155
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 1-169 1.37e-42

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: 142.59  E-value: 1.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LRENKWSSQNKKILILGAGGVTSSILSSFIKAnGVLKIYLCNRTREKAEELKTLWDKAVdssgmkkdtIEIVDWGKKIEL 80
Cdd:COG0169  112 LREAGVDLAGKRVLVLGAGGAARAVAAALAEA-GAAEITIVNRTPERAEALAARLGVRA---------VPLDDLAAALAG 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  81 CDLVINTTSVGLTKNENIKLNFSNYenKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTGVSPK 160
Cdd:COG0169  182 ADLVINATPLGMAGGDALPLPASLL--APGAVVYDLVYNPLETPLLRAARARGARVIDGLGMLVHQAAEAFELWTGVRPP 259


                 ....*....
gi 142000763 161 InDEVINLL 169
Cdd:COG0169  260 V-EAMRAAL 267
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
 1-169 2.79e-41

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 139.55  E-value: 2.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LREN-KWSSQNKKILILGAGGVTSSILSSFIKAnGVLKIYLCNRTREKAEELKTLWDKAVDSSGmkkdtieIVDWGKKIE 79
Cdd:PRK00258 113 LEERlGVDLKGKRILILGAGGAARAVILPLLDL-GVAEITIVNRTVERAEELAKLFGALGKAEL-------DLELQEELA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  80 LCDLVINTTSVGLTKNENI-KLNFSNYenKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTGVS 158
Cdd:PRK00258 185 DFDLIINATSAGMSGELPLpPLPLSLL--RPGTIVYDMIYGPLPTPFLAWAKAQGARTIDGLGMLVHQAAEAFELWTGVR 262

                        170
                 ....*....|.
gi 142000763 159 PKInDEVINLL 169
Cdd:PRK00258 263 PPV-EPMLAAL 272
aroE TIGR00507
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ...
 1-161 1.39e-32

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: 116.75  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763    1 LRENKWSSQNKKILILGAGGVTSSILSSFIKANgvLKIYLCNRTREKAEELKTLWDKAVDSSGMKKDTIEIvdwgkkiEL 80
Cdd:TIGR00507 108 LEQLIPLRPNQNVLIIGAGGAAKAVALELLKAD--CNVIIANRTVSKAEELAERFQRYGEIQAFSMDELPL-------HR 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   81 CDLVINTTSVGLTKNENIKLNFSNYEnKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTGVSPK 160
Cdd:TIGR00507 179 VDLIINATSAGMSGNIDEPPVPAEYL-KEGKLVYDLVYNPLETPFLAEAKSLGTKTIDGLGMLVYQAALSFELWTGVEPD 257


                  .
gi 142000763  161 I 161
Cdd:TIGR00507 258 I 258
PRK12548 PRK12548
shikimate dehydrogenase;
1-156 2.53e-17

shikimate dehydrogenase;


Pssm-ID: 183585 [Multi-domain]  Cd Length: 289  Bit Score: 77.09  E-value: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LRENKWSSQNKKILILGAGGVTSSILSSfIKANGVLKIYLCNRTR---EKAEELKTLWDKAV--------DSSGMKKDTI 69
Cdd:PRK12548 117 LREHGVDVKGKKLTVIGAGGAATAIQVQ-CALDGAKEITIFNIKDdfyERAEQTAEKIKQEVpecivnvyDLNDTEKLKA 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  70 EIVDwgkkielCDLVINTTSVGLTKNENIKLNFSNYENKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQL 149
Cdd:PRK12548 196 EIAS-------SDILVNATLVGMKPNDGETNIKDTSVFRKDLVVADTVYNPKKTKLLEDAEAAGCKTVGGLGMLLWQGAE 268


                 ....*..
gi 142000763 150 AFQMWTG 156
Cdd:PRK12548 269 AYKLYTG 275
PRK12749 PRK12749
quinate/shikimate dehydrogenase; Reviewed
 1-156 9.23e-13

quinate/shikimate dehydrogenase; Reviewed


Pssm-ID: 183721 [Multi-domain]  Cd Length: 288  Bit Score: 64.25  E-value: 9.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LRENKWSSQNKKILILGAGGVTSSIlSSFIKANGVLKIYLCNRTREkaeelktLWDKAVDSSGMKKD----TIEIVDWGK 76
Cdd:PRK12749 115 IKESGFDIKGKTMVLLGAGGASTAI-GAQGAIEGLKEIKLFNRRDE-------FFDKALAFAQRVNEntdcVVTVTDLAD 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  77 K------IELCDLVINTTSVGLTKNENIKLNFSNYENKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLA 150
Cdd:PRK12749 187 QqafaeaLASADILTNGTKVGMKPLENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQ 266


                 ....*.
gi 142000763 151 FQMWTG 156
Cdd:PRK12749 267 FTLWTG 272
PLN02520 PLN02520
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
 11-160 8.22e-11

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase


Pssm-ID: 178135 [Multi-domain]  Cd Length: 529  Bit Score: 59.39  E-value: 8.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  11 KKILILGAGGVTSSiLSSFIKANGVlKIYLCNRTREKAEELktlwdkaVDSSGmkkdtieivdwGKKIELCDL------- 83
Cdd:PLN02520 380 KLFVVIGAGGAGKA-LAYGAKEKGA-RVVIANRTYERAKEL-------ADAVG-----------GQALTLADLenfhpee 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  84 ---VINTTSVGLTKNEN----IKLNFSNYenkkdALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTG 156
Cdd:PLN02520 440 gmiLANTTSVGMQPNVDetpiSKHALKHY-----SLVFDAVYTPKITRLLREAEESGAIIVSGTEMFIRQAYEQFERFTG 514


                 ....*
gi 142000763 157 V-SPK 160
Cdd:PLN02520 515 LpAPK 519
PRK14027 PRK14027
quinate/shikimate dehydrogenase (NAD+);
13-162 2.81e-10

quinate/shikimate dehydrogenase (NAD+);


Pssm-ID: 172521 [Multi-domain]  Cd Length: 283  Bit Score: 57.36  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  13 ILILGAGGVTSSILSSFIkANGVLKIYLCNRTREKAEELKTLWDKAVDSS---GMKKDTIEIVdwgkkIELCDLVINTTS 89
Cdd:PRK14027 130 VVQVGAGGVGNAVAYALV-THGVQKLQVADLDTSRAQALADVINNAVGREavvGVDARGIEDV-----IAAADGVVNATP 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 142000763  90 VGLTKNENIKLNFSNYenKKDALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTGVSPKIN 162
Cdd:PRK14027 204 MGMPAHPGTAFDVSCL--TKDHWVGDVVYMPIETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGLEPDVS 274
aroDE PRK09310
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;
1-154 3.25e-10

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;


Pssm-ID: 137204 [Multi-domain]  Cd Length: 477  Bit Score: 57.50  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   1 LRENKWSSQNKKILILGAGGVTSSILSSFIKANGVLKIYlcNRTREKAEELKTLWD-KAVD-SSGMKKDTIeivdwgkki 78
Cdd:PRK09310 323 LKQKNIPLNNQHVAIVGAGGAAKAIATTLARAGAELLIF--NRTKAHAEALASRCQgKAFPlESLPELHRI--------- 391

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 142000763  79 elcDLVINTTSVGLTKNENIKlnfsnyenkkdALFYDLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMW 154
Cdd:PRK09310 392 ---DIIINCLPPSVTIPKAFP-----------PCVVDINTLPKHSPYTQYARSQGSSIIYGYEMFAEQALLQFRLW 453
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 9-89 4.47e-07

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (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 DH, 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: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 48.42  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   9 QNKKILILGAGgVTSSILSSFIKANGVLKIYLCNRTREKAEELKtlwdkavdssgmKKDTIEIVDW---GKKIELCDLVI 85
Cdd:cd05213  177 KGKKVLVIGAG-EMGELAAKHLAAKGVAEITIANRTYERAEELA------------KELGGNAVPLdelLELLNEADVVI 243


                 ....
gi 142000763  86 NTTS 89
Cdd:cd05213  244 SATG 247
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 9-89 3.53e-06

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 45.94  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763   9 QNKKILILGAGGvTSSILSSFIKANGVLKIYLCNRTREKAEEL-KTLWDKAVDSSGMKkdtieivdwgKKIELCDLVINT 87
Cdd:PRK00045 181 SGKKVLVIGAGE-MGELVAKHLAEKGVRKITVANRTLERAEELaEEFGGEAIPLDELP----------EALAEADIVISS 249


                 ..
gi 142000763  88 TS 89
Cdd:PRK00045 250 TG 251
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 9-51 8.45e-06

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 44.72  E-value: 8.45e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 142000763   9 QNKKILILGAGGvTSSILSSFIKANGVLKIYLCNRTREKAEEL 51
Cdd:COG0373  181 SGKTVLVIGAGE-MGELAARHLAAKGVKRITVANRTLERAEEL 222
PRK12549 PRK12549
shikimate 5-dehydrogenase; Reviewed
 115-159 1.84e-04

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 183586 [Multi-domain]  Cd Length: 284  Bit Score: 40.65  E-value: 1.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 142000763 115 DLIYNPKETNFLKDAKLRGNKIMNGKMMFLWQAQLAFQMWTGVSP 159
Cdd:PRK12549 225 DIVYFPLETELLRAARALGCRTLDGGGMAVFQAVDAFELFTGREP 269
SDH_C pfam18317
Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of ...
 142-159 1.18e-03

Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of Shikimate 5'-dehydrogenase (SDH) present in Methanocaldococcus jannaschii. SDH catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate in the shikimate pathway. The domain is found just after the C-terminal domain (pfam01488) which is responsible for NADP binding.


Pssm-ID: 436404 [Multi-domain]  Cd Length: 31  Bit Score: 35.09  E-value: 1.18e-03
                          10
                  ....*....|....*...
gi 142000763  142 MFLWQAQLAFQMWTGVSP 159
Cdd:pfam18317   4 MLVEQGAEQFELWTGREP 21
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 9-52 1.26e-03

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 38.12  E-value: 1.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 142000763   9 QNKKILILGAGGVTSSILSSFIKAnGVLK--IYLCNRTREKAEELK 52
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKS-GVPPedIIVSDRSPERLEALA 45
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 11-89 1.88e-03

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 36.78  E-value: 1.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 142000763   11 KKILILGAGgVTSSILSSFIKANGVLKIYLCNRTREKAEELktlwdkAVDSSGMKKDTIEivDWGKKIELCDLVINTTS 89
Cdd:pfam01488  13 KKVLLIGAG-EMGELVAKHLLAKGAKEVTIANRTIERAQEL------AEKFGGVEALPLD--DLKEYLAEADIVISATS 82
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 13-127 2.13e-03

A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240214 [Multi-domain]  Cd Length: 120  Bit Score: 36.40  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142000763  13 ILILGAGGVTSSILSS--FIKANGVLKIYLcnrtrEKAEELKTLWDKAVDS---------SGMKKDTIEIVDWGKKielc 81
Cdd:cd05710    2 VFFVGCGGSLADMYPAkyFLKKESKLPVFV-----YNAAEFLHTGPKRLTEksvvilashSGNTKETVAAAKFAKE---- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 142000763  82 dlvINTTSVGLTKNENIKL-NFSNYenkkdALFYDLIYNPKETNFLK 127
Cdd:cd05710   73 ---KGATVIGLTDDEDSPLaKLADY-----VIVYGFEIDAVEEKYLL 111
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 13-73 5.63e-03

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 34.87  E-value: 5.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 142000763   13 ILILGAGGVTSSILSSFIKANGVLKIYLCNRTREKAeelktlwDKAVDSSGMKKDTIEIVD 73
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFDVDRITVADRTLEKA-------QALAAKLGGVRFIAVAVD 54
 
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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