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Conserved domains on  [gi|1385865507|gb|PVO78788|]
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gluconokinase [Salmonella enterica subsp. enterica serovar Anatum]

Protein Classification

nucleoside/nucleotide kinase family protein; thymidylate kinase( domain architecture ID 10793313)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars| thymidylate kinase with a major facilitator superfamily (MFS) transporter domain may function in the phosphorylation of thymidine monophosphate and the transport across cytoplasmic or internal membranes of various substrates including sugar phosphates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
idnK PRK09825
gluconokinase;
1-176 3.26e-142

gluconokinase;


:

Pssm-ID: 182097  Cd Length: 176  Bit Score: 392.47  E-value: 3.26e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   1 MAGESYILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFI 80
Cdd:PRK09825    1 MAGESYILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIEHVTE 160
Cdd:PRK09825   81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIENVTE 160
                         170
                  ....*....|....*.
gi 1385865507 161 QCRLAVQAFRQALSAS 176
Cdd:PRK09825  161 QCRQAVQAFRQALSAS 176
 
Name Accession Description Interval E-value
idnK PRK09825
gluconokinase;
1-176 3.26e-142

gluconokinase;


Pssm-ID: 182097  Cd Length: 176  Bit Score: 392.47  E-value: 3.26e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   1 MAGESYILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFI 80
Cdd:PRK09825    1 MAGESYILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIEHVTE 160
Cdd:PRK09825   81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIENVTE 160
                         170
                  ....*....|....*.
gi 1385865507 161 QCRLAVQAFRQALSAS 176
Cdd:PRK09825  161 QCRQAVQAFRQALSAS 176
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
6-166 1.09e-93

carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.


Pssm-ID: 273551  Cd Length: 163  Bit Score: 269.27  E-value: 1.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   6 YILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFIVCSSL 85
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  86 KKQYRDILRKSSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIEHVTEQCRLA 165
Cdd:TIGR01313  81 KRHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADETDVLRVDIDQPLEGVEEDCIAV 160

                  .
gi 1385865507 166 V 166
Cdd:TIGR01313 161 V 161
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
5-167 1.19e-87

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 253.90  E-value: 1.19e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   5 SYILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFIVCSS 84
Cdd:COG3265     3 VIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLACSA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  85 LKKQYRDILRKSSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIaRIDVNHDIEHVTEQCRL 164
Cdd:COG3265    83 LKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAI-VVDIDQPPEEIVAQILA 161

                  ...
gi 1385865507 165 AVQ 167
Cdd:COG3265   162 ALG 164
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
6-151 4.81e-71

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 211.34  E-value: 4.81e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   6 YILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYS-LYKKNETGFIVCSS 84
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAkLASAGEGVVVACSA 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1385865507  85 LKKQYRDILRK--SSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDV 151
Cdd:cd02021    82 LKRIYRDILRGgaANPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIVIDV 150
SKI pfam01202
Shikimate kinase;
13-153 4.44e-07

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 47.19  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  13 GSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDED--RLPWLERLNDASyslykkNETGFIVC----SSLK 86
Cdd:pfam01202   2 GAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEgfRRLESEVLKELL------AEHGLVIAtgggAVLS 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1385865507  87 KQYRDILRKSSPNVhflWLDGDYATILQRMQRRAG-----HFMPPDLLQSQFDALERPCADEHDIARIDVNH 153
Cdd:pfam01202  76 EENRDLLKERGIVI---YLDAPLEVLLERLKRDKTrpllqNKDPEEELLELLFEERDPLYEEAADIVIDTDE 144
 
Name Accession Description Interval E-value
idnK PRK09825
gluconokinase;
1-176 3.26e-142

gluconokinase;


Pssm-ID: 182097  Cd Length: 176  Bit Score: 392.47  E-value: 3.26e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   1 MAGESYILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFI 80
Cdd:PRK09825    1 MAGESYILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIEHVTE 160
Cdd:PRK09825   81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIENVTE 160
                         170
                  ....*....|....*.
gi 1385865507 161 QCRLAVQAFRQALSAS 176
Cdd:PRK09825  161 QCRQAVQAFRQALSAS 176
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
6-166 1.09e-93

carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.


Pssm-ID: 273551  Cd Length: 163  Bit Score: 269.27  E-value: 1.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   6 YILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFIVCSSL 85
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  86 KKQYRDILRKSSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIEHVTEQCRLA 165
Cdd:TIGR01313  81 KRHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADETDVLRVDIDQPLEGVEEDCIAV 160

                  .
gi 1385865507 166 V 166
Cdd:TIGR01313 161 V 161
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
5-167 1.19e-87

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 253.90  E-value: 1.19e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   5 SYILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFIVCSS 84
Cdd:COG3265     3 VIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLACSA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  85 LKKQYRDILRKSSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIaRIDVNHDIEHVTEQCRL 164
Cdd:COG3265    83 LKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAI-VVDIDQPPEEIVAQILA 161

                  ...
gi 1385865507 165 AVQ 167
Cdd:COG3265   162 ALG 164
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
6-151 4.81e-71

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 211.34  E-value: 4.81e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   6 YILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYS-LYKKNETGFIVCSS 84
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAkLASAGEGVVVACSA 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1385865507  85 LKKQYRDILRK--SSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDV 151
Cdd:cd02021    82 LKRIYRDILRGgaANPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIVIDV 150
gntK PRK11545
gluconokinase;
9-158 9.97e-67

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 201.10  E-value: 9.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507   9 MGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFIVCSSLKKQ 88
Cdd:PRK11545    1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  89 YRDILRKSSPNVHFLWLDGDYATILQRMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIEHV 158
Cdd:PRK11545   81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLVVDIDQPLEGV 150
SKI pfam01202
Shikimate kinase;
13-153 4.44e-07

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 47.19  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385865507  13 GSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDED--RLPWLERLNDASyslykkNETGFIVC----SSLK 86
Cdd:pfam01202   2 GAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEgfRRLESEVLKELL------AEHGLVIAtgggAVLS 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1385865507  87 KQYRDILRKSSPNVhflWLDGDYATILQRMQRRAG-----HFMPPDLLQSQFDALERPCADEHDIARIDVNH 153
Cdd:pfam01202  76 EENRDLLKERGIVI---YLDAPLEVLLERLKRDKTrpllqNKDPEEELLELLFEERDPLYEEAADIVIDTDE 144
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
7-37 9.18e-04

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 37.92  E-value: 9.18e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1385865507   7 ILMGVSGSGKSLIGSKIATLFSAKFIDGDDL 37
Cdd:cd00464     3 VLIGMMGAGKTTVGRLLAKALGLPFVDLDEL 33
PRK13947 PRK13947
shikimate kinase; Provisional
7-47 9.71e-03

shikimate kinase; Provisional


Pssm-ID: 184412 [Multi-domain]  Cd Length: 171  Bit Score: 35.07  E-value: 9.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1385865507   7 ILMGVSGSGKSLIGSKIATLFSAKFIDGDdlhpaKNIDKMS 47
Cdd:PRK13947    5 VLIGFMGTGKTTVGKRVATTLSFGFIDTD-----KEIEKMT 40
PLN02748 PLN02748
tRNA dimethylallyltransferase
7-59 9.72e-03

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 35.63  E-value: 9.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1385865507   7 ILMGVSGSGKSLIGSKIATLFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLP 59
Cdd:PLN02748   26 VVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVP 78
 
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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