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Conserved domains on  [gi|52696934|gb|AAU86216|]
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shikimate dehydrogenase, partial [Shigella boydii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
aroE super family cl31438
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ...
 1-120 2.76e-57

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]


The actual alignment was detected with superfamily member TIGR00507:

Pssm-ID: 161904 [Multi-domain]  Cd Length: 270  Bit Score: 177.99  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934     1 LAGAVNTLKrLEDGRLLGDNTDGIGLLSDLERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCAVTITNRTVSRAEELAK 80
Cdd:TIGR00507  80 LAGAVNTLV-LEDGKLVGYNTDGIGLVSDLEQLIPLRPNQNVLIIGAGGAAKAVALELLKADCNVIIANRTVSKAEELAE 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 52696934    81 LFAHTGSVQALGMDELEGHEFDLIINATSSGISGDIPAIP 120
Cdd:TIGR00507 159 RFQRYGEIQAFSMDELPLHRVDLIINATSAGMSGNIDEPP 198
 
Name Accession Description Interval E-value
aroE TIGR00507
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ...
 1-120 2.76e-57

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: 177.99  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934     1 LAGAVNTLKrLEDGRLLGDNTDGIGLLSDLERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCAVTITNRTVSRAEELAK 80
Cdd:TIGR00507  80 LAGAVNTLV-LEDGKLVGYNTDGIGLVSDLEQLIPLRPNQNVLIIGAGGAAKAVALELLKADCNVIIANRTVSKAEELAE 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 52696934    81 LFAHTGSVQALGMDELEGHEFDLIINATSSGISGDIPAIP 120
Cdd:TIGR00507 159 RFQRYGEIQAFSMDELPLHRVDLIINATSAGMSGNIDEPP 198
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
 1-120 4.38e-47

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 152.26  E-value: 4.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934    1 LAGAVNTLKRlEDGRLLGDNTDGIGLLSDL-ERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEEL 78
Cdd:PRK00258  85 LIGAVNTLVL-EDGRLIGDNTDGIGFVRALeERLGVDLKGKRILILGAGGAARAVILPLLDLGVAeITIVNRTVERAEEL 163

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 52696934   79 AKLFAHTGSVQALGMDELEGHEFDLIINATSSGISGDIPAIP 120
Cdd:PRK00258 164 AKLFGALGKAELDLELQEELADFDLIINATSAGMSGELPLPP 205
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 1-120 4.41e-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: 139.12  E-value: 4.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934   1 LAGAVNTLKRlEDGRLLGDNTDGIGLLSDLERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEELA 79
Cdd:COG0169  84 LIGAVNTVVF-EDGRLIGDNTDGIGFVRALREAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAeITIVNRTPERAEALA 162

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 52696934  80 KLFahtgSVQALGMDELEG--HEFDLIINATSSGISG-DIPAIP 120
Cdd:COG0169 163 ARL----GVRAVPLDDLAAalAGADLVINATPLGMAGgDALPLP 202
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 21-111 9.17e-25

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: 91.56  E-value: 9.17e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934  21 TDGIGLLSDLERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEELAKLFAHTGSVQALGMDELEGH 99
Cdd:cd01065   1 TDGLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAAkIVIVNRTLEKAKALAERFGELGIAIAYLDLEELLA 80

                        90
                ....*....|..
gi 52696934 100 EFDLIINATSSG 111
Cdd:cd01065  81 EADLIINTTPVG 92
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 38-110 1.24e-11

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: 57.20  E-value: 1.24e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52696934    38 SGLRILLIGAGGASRGVLLPLLSLDC-AVTITNRTVSRAEELAKLFahtGSVQALGMDELEGH--EFDLIINATSS 110
Cdd:pfam01488  11 KDKKVLLIGAGEMGELVAKHLLAKGAkEVTIANRTIERAQELAEKF---GGVEALPLDDLKEYlaEADIVISATSS 83
 
Name Accession Description Interval E-value
aroE TIGR00507
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ...
 1-120 2.76e-57

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: 177.99  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934     1 LAGAVNTLKrLEDGRLLGDNTDGIGLLSDLERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCAVTITNRTVSRAEELAK 80
Cdd:TIGR00507  80 LAGAVNTLV-LEDGKLVGYNTDGIGLVSDLEQLIPLRPNQNVLIIGAGGAAKAVALELLKADCNVIIANRTVSKAEELAE 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 52696934    81 LFAHTGSVQALGMDELEGHEFDLIINATSSGISGDIPAIP 120
Cdd:TIGR00507 159 RFQRYGEIQAFSMDELPLHRVDLIINATSAGMSGNIDEPP 198
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
 1-120 4.38e-47

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 152.26  E-value: 4.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934    1 LAGAVNTLKRlEDGRLLGDNTDGIGLLSDL-ERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEEL 78
Cdd:PRK00258  85 LIGAVNTLVL-EDGRLIGDNTDGIGFVRALeERLGVDLKGKRILILGAGGAARAVILPLLDLGVAeITIVNRTVERAEEL 163

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 52696934   79 AKLFAHTGSVQALGMDELEGHEFDLIINATSSGISGDIPAIP 120
Cdd:PRK00258 164 AKLFGALGKAELDLELQEELADFDLIINATSAGMSGELPLPP 205
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 1-120 4.41e-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: 139.12  E-value: 4.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934   1 LAGAVNTLKRlEDGRLLGDNTDGIGLLSDLERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEELA 79
Cdd:COG0169  84 LIGAVNTVVF-EDGRLIGDNTDGIGFVRALREAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAeITIVNRTPERAEALA 162

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 52696934  80 KLFahtgSVQALGMDELEG--HEFDLIINATSSGISG-DIPAIP 120
Cdd:COG0169 163 ARL----GVRAVPLDDLAAalAGADLVINATPLGMAGgDALPLP 202
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 21-111 9.17e-25

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: 91.56  E-value: 9.17e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934  21 TDGIGLLSDLERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEELAKLFAHTGSVQALGMDELEGH 99
Cdd:cd01065   1 TDGLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAAkIVIVNRTLEKAKALAERFGELGIAIAYLDLEELLA 80

                        90
                ....*....|..
gi 52696934 100 EFDLIINATSSG 111
Cdd:cd01065  81 EADLIINTTPVG 92
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 38-110 3.07e-13

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 64.43  E-value: 3.07e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52696934   38 SGLRILLIGAGGASRGVLLPLLSLDC-AVTITNRTVSRAEELAKLFahtgSVQALGMDELEG--HEFDLIINATSS 110
Cdd:PRK00045 181 SGKKVLVIGAGEMGELVAKHLAEKGVrKITVANRTLERAEELAEEF----GGEAIPLDELPEalAEADIVISSTGA 252
Shik-DH-AROM TIGR01809
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ...
 1-120 4.93e-13

shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of shikimate-5-dehydrogenases found in Corynebacterium, Mycobacteria and fungi. The fungal sequences are pentafunctional proteins known as AroM which contain the central five seven steps in the chorismate biosynthesis pathway. The Corynebacterium and Mycobacterial sequences represent the sole shikimate-5-dehydrogenases in species which otherwise have every enzyme of the chorismate biosynthesis pathway. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273813 [Multi-domain]  Cd Length: 282  Bit Score: 63.40  E-value: 4.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934     1 LAGAVNTLKRLEDGRLLGDNTDGIGLLSDLERLSFIR--SGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEE 77
Cdd:TIGR01809  85 LIGSVNTLLRTQNGIWKGDNTDWDGIAGALANIGKFEplAGFRGLVIGAGGTSRAAVYALASLGVTdITVINRNPDKLSR 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 52696934    78 LAKLFAHTGSVQAL-GMDELEGHEFDliINATSSGISGDIPAIP 120
Cdd:TIGR01809 165 LVDLGVQVGVITRLeGDSGGLAIEKA--AEVLVSTVPADVPADY 206
aroDE PRK09310
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;
1-119 6.28e-13

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;


Pssm-ID: 137204 [Multi-domain]  Cd Length: 477  Bit Score: 63.66  E-value: 6.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934    1 LAGAVNTLKrLEDGRLLGDNTDGIGLLSDLERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCAVTITNRTVSRAEELAK 80
Cdd:PRK09310 295 LCGSCNTLV-FRNGKIEGYNTDGEGLFSLLKQKNIPLNNQHVAIVGAGGAAKAIATTLARAGAELLIFNRTKAHAEALAS 373

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 52696934   81 LFahtgSVQALGMDEL-EGHEFDLIINATSSGIsgDIPAI 119
Cdd:PRK09310 374 RC----QGKAFPLESLpELHRIDIIINCLPPSV--TIPKA 407
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 38-110 4.17e-12

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: 61.28  E-value: 4.17e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52696934  38 SGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEELAKLFahtgSVQALGMDELEGH--EFDLIINATSS 110
Cdd:COG0373 181 SGKTVLVIGAGEMGELAARHLAAKGVKrITVANRTLERAEELAEEF----GGEAVPLEELPEAlaEADIVISSTGA 252
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 30-110 8.03e-12

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: 59.97  E-value: 8.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934  30 LERLSFIRSGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEELAKLFahtgSVQALGMDELEG--HEFDLIIN 106
Cdd:cd05213 169 AEKIFGNLKGKKVLVIGAGEMGELAAKHLAAKGVAeITIANRTYERAEELAKEL----GGNAVPLDELLEllNEADVVIS 244


                ....
gi 52696934 107 ATSS 110
Cdd:cd05213 245 ATGA 248
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 38-110 1.24e-11

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: 57.20  E-value: 1.24e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52696934    38 SGLRILLIGAGGASRGVLLPLLSLDC-AVTITNRTVSRAEELAKLFahtGSVQALGMDELEGH--EFDLIINATSS 110
Cdd:pfam01488  11 KDKKVLLIGAGEMGELVAKHLLAKGAkEVTIANRTIERAQELAEKF---GGVEALPLDDLKEYlaEADIVISATSS 83
PLN02520 PLN02520
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
 3-120 1.37e-09

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase


Pssm-ID: 178135 [Multi-domain]  Cd Length: 529  Bit Score: 54.00  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934    3 GAVNT-LKRLEDGRLLGDNTDGIGLLSDLE---RLSFIRS-------GLRILLIGAGGASRGVLLPLLSLDCAVTITNRT 71
Cdd:PLN02520 332 GAINTiIRRPSDGKLVGYNTDYIGAISAIEdglRASGSSPasgsplaGKLFVVIGAGGAGKALAYGAKEKGARVVIANRT 411

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 52696934   72 VSRAEELAKLFAHtgsvQALGMDELEG-HEFDLII--NATSSGISGDIPAIP 120
Cdd:PLN02520 412 YERAKELADAVGG----QALTLADLENfHPEEGMIlaNTTSVGMQPNVDETP 459
PRK12549 PRK12549
shikimate 5-dehydrogenase; Reviewed
 3-114 2.54e-09

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 183586 [Multi-domain]  Cd Length: 284  Bit Score: 52.98  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934    3 GAVNTLkRLEDGRLLGDNTDGIGLLSDLERlsfirsGL------RILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRA 75
Cdd:PRK12549  92 GAVNTV-VFRDGRRIGHNTDWSGFAESFRR------GLpdasleRVVQLGAGGAGAAVAHALLTLGVErLTIFDVDPARA 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 52696934   76 EELA-KLFAHTGSVQALGMDELEG--HEFDLIINATSSGISG 114
Cdd:PRK12549 165 AALAdELNARFPAARATAGSDLAAalAAADGLVHATPTGMAK 206
PRK12548 PRK12548
shikimate dehydrogenase;
3-80 1.21e-07

shikimate dehydrogenase;


Pssm-ID: 183585 [Multi-domain]  Cd Length: 289  Bit Score: 48.20  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934    3 GAVNTLKRlEDGRLLGDNTDGIGLLSDLERLSFIRSGLRILLIGAGGASRGVLLPlLSLDCA--VTITNRT---VSRAEE 77
Cdd:PRK12548  91 GAVNTIVN-DDGKLTGHITDGLGFVRNLREHGVDVKGKKLTVIGAGGAATAIQVQ-CALDGAkeITIFNIKddfYERAEQ 168


                 ...
gi 52696934   78 LAK 80
Cdd:PRK12548 169 TAE 171
PRK12749 PRK12749
quinate/shikimate dehydrogenase; Reviewed
 1-54 5.23e-06

quinate/shikimate dehydrogenase; Reviewed


Pssm-ID: 183721 [Multi-domain]  Cd Length: 288  Bit Score: 43.84  E-value: 5.23e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 52696934    1 LAGAVNTLKRlEDGRLLGDNTDGIGLLSDLERLSFIRSGLRILLIGAGGASRGV 54
Cdd:PRK12749  87 LVGAINTIVN-DDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAI 139
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 37-107 1.24e-04

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 39.24  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934    37 RSGLRILLIGAGGASRGVLLPLLSLDCAVTITNRtvSRAEELAK----LFAHTGSVQA--------LGMDELEGHEFDLI 104
Cdd:pfam10294  45 LSGLNVLELGSGTGLVGIAVALLLPGASVTITDL--EEALELLKknieLNALSSKVVVkvldwgenLPPDLFDGHPVDLI 122


                  ...
gi 52696934   105 INA 107
Cdd:pfam10294 123 LAA 125
PLN00203 PLN00203
glutamyl-tRNA reductase
 38-111 2.51e-04

glutamyl-tRNA reductase


Pssm-ID: 215101 [Multi-domain]  Cd Length: 519  Bit Score: 38.96  E-value: 2.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52696934   38 SGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEELAKLFAHTGSVQALgMDELEG--HEFDLIINATSSG 111
Cdd:PLN00203 265 ASARVLVIGAGKMGKLLVKHLVSKGCTkMVVVNRSEERVAALREEFPDVEIIYKP-LDEMLAcaAEADVVFTSTSSE 340
PRK12550 PRK12550
shikimate 5-dehydrogenase; Reviewed
 4-114 4.77e-04

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 183587 [Multi-domain]  Cd Length: 272  Bit Score: 38.01  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52696934    4 AVNTLKRlEDGRLLGDNTDGIGLLSDLERLSfIRSGLRILLIGAGGASRGVLLPLLSLDCA-VTITNRTVSRAEELAKLF 82
Cdd:PRK12550  89 SVNTIVN-TDGHLKAYNTDYIAIAKLLASYQ-VPPDLVVALRGSGGMAKAVAAALRDAGFTdGTIVARNEKTGKALAELY 166

                         90       100       110
                 ....*....|....*....|....*....|..
gi 52696934   83 AHTGSvqalgmDELEGHEFDLIINATSSGISG 114
Cdd:PRK12550 167 GYEWR------PDLGGIEADILVNVTPIGMAG 192
MviM COG0673
Predicted dehydrogenase [General function prediction only];
40-108 5.30e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 34.90  E-value: 5.30e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52696934  40 LRILLIGAGGASRGVLLPLLSLDCA--VTITNRTVSRAEELAKLF--AHTGSVQALgmdeLEGHEFDLIINAT 108
Cdd:COG0673   4 LRVGIIGAGGIGRAHAPALAALPGVelVAVADRDPERAEAFAEEYgvRVYTDYEEL----LADPDIDAVVIAT 72
 
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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