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Conserved domains on  [gi|515989842|ref|WP_017420425|]
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MULTISPECIES: gluconokinase [Vibrio]

Protein Classification

gluconokinase( domain architecture ID 10790049)

gluconokinase catalyzes the phosphoryl transfer from ATP to gluconate to form gluconate-6-phoshate

Gene Ontology:  GO:0046316|GO:0046177|GO:0005524
SCOP:  4003925

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
3-165 1.66e-96

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: 276.24  E-value: 1.66e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   3 GSSVIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVC 82
Cdd:COG3265    1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842  83 SALKKSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLLVSIDTTIEDVVANAA 162
Cdd:COG3265   81 SALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQIL 160

                 ...
gi 515989842 163 ELI 165
Cdd:COG3265  161 AAL 163
 
Name Accession Description Interval E-value
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
3-165 1.66e-96

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: 276.24  E-value: 1.66e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   3 GSSVIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVC 82
Cdd:COG3265    1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842  83 SALKKSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLLVSIDTTIEDVVANAA 162
Cdd:COG3265   81 SALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQIL 160

                 ...
gi 515989842 163 ELI 165
Cdd:COG3265  161 AAL 163
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
7-167 4.69e-77

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: 226.90  E-value: 4.69e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842    7 IVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVCSALK 86
Cdd:TIGR01313   2 VLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSALK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   87 KSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDG-EPRTLLVSIDTTIEDVVANAAELI 165
Cdd:TIGR01313  82 RHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLAdETDVLRVDIDQPLEGVEEDCIAVV 161

                  ..
gi 515989842  166 LE 167
Cdd:TIGR01313 162 LK 163
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
6-152 1.94e-73

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: 217.12  E-value: 1.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYS-LESKNEHGIIVCSA 84
Cdd:cd02021    2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAkLASAGEGVVVACSA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842  85 LKKSYRDQIRDG--NNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLLVsIDT 152
Cdd:cd02021   82 LKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIV-IDV 150
gntK PRK11545
gluconokinase;
9-165 1.27e-70

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 210.73  E-value: 1.27e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   9 MGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVCSALKKS 88
Cdd:PRK11545   1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515989842  89 YRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERP-DGEPRTLLVSIDTTIEDVVANAAELI 165
Cdd:PRK11545  81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPgADETDVLVVDIDQPLEGVVASTIEVI 158
SKI pfam01202
Shikimate kinase;
9-120 4.49e-10

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 55.28  E-value: 4.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842    9 MGvcaSGKTTIGELLAEKLGRKFIDGDDLHPRANiqKMASGQPLNDD----DRKPWLERIRDAAysleskNEHGIIVC-- 82
Cdd:pfam01202   1 MG---AGKSTIGRLLAKALGLPFIDTDEEIEKRT--GMSIAEIFEEEgeegFRRLESEVLKELL------AEHGLVIAtg 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 515989842   83 --SALKKSYRDQIRDGNnnvTFLFLDGDKSLILERMRQRQ 120
Cdd:pfam01202  70 ggAVLSEENRDLLKERG---IVIYLDAPLEVLLERLKRDK 106
 
Name Accession Description Interval E-value
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
3-165 1.66e-96

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: 276.24  E-value: 1.66e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   3 GSSVIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVC 82
Cdd:COG3265    1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842  83 SALKKSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLLVSIDTTIEDVVANAA 162
Cdd:COG3265   81 SALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQIL 160

                 ...
gi 515989842 163 ELI 165
Cdd:COG3265  161 AAL 163
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
7-167 4.69e-77

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: 226.90  E-value: 4.69e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842    7 IVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVCSALK 86
Cdd:TIGR01313   2 VLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSALK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   87 KSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDG-EPRTLLVSIDTTIEDVVANAAELI 165
Cdd:TIGR01313  82 RHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLAdETDVLRVDIDQPLEGVEEDCIAVV 161

                  ..
gi 515989842  166 LE 167
Cdd:TIGR01313 162 LK 163
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
6-152 1.94e-73

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: 217.12  E-value: 1.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYS-LESKNEHGIIVCSA 84
Cdd:cd02021    2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAkLASAGEGVVVACSA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842  85 LKKSYRDQIRDG--NNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLLVsIDT 152
Cdd:cd02021   82 LKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIV-IDV 150
gntK PRK11545
gluconokinase;
9-165 1.27e-70

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 210.73  E-value: 1.27e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   9 MGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVCSALKKS 88
Cdd:PRK11545   1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515989842  89 YRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERP-DGEPRTLLVSIDTTIEDVVANAAELI 165
Cdd:PRK11545  81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPgADETDVLVVDIDQPLEGVVASTIEVI 158
idnK PRK09825
gluconokinase;
1-157 1.19e-64

gluconokinase;


Pssm-ID: 182097  Cd Length: 176  Bit Score: 196.02  E-value: 1.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   1 MAGSSVIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGII 80
Cdd:PRK09825   1 MAGESYILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515989842  81 VCSALKKSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLL-VSIDTTIEDV 157
Cdd:PRK09825  81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPCADEHDIArIDVNHDIENV 158
SKI pfam01202
Shikimate kinase;
9-120 4.49e-10

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 55.28  E-value: 4.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842    9 MGvcaSGKTTIGELLAEKLGRKFIDGDDLHPRANiqKMASGQPLNDD----DRKPWLERIRDAAysleskNEHGIIVC-- 82
Cdd:pfam01202   1 MG---AGKSTIGRLLAKALGLPFIDTDEEIEKRT--GMSIAEIFEEEgeegFRRLESEVLKELL------AEHGLVIAtg 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 515989842   83 --SALKKSYRDQIRDGNnnvTFLFLDGDKSLILERMRQRQ 120
Cdd:pfam01202  70 ggAVLSEENRDLLKERG---IVIYLDAPLEVLLERLKRDK 106
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
6-162 2.27e-08

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 50.68  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDlhpranIQKMASGQPLNDDDRKPWL-ERIRDAAYSLESKN-EHG---II 80
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRLRSDV------VRKRLFGAGLAPLERSPEAtARTYARLLALARELlAAGrsvIL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842  81 VCSALKKSYRDQIRD--GNNNVTF--LFLDGDKSLILERMRQRQGHFMK----ENMVNSQFETLERPDGEPRTLLVsIDT 152
Cdd:COG0645   76 DATFLRRAQREAFRAlaEEAGAPFvlIWLDAPEEVLRERLEARNAEGGDsdatWEVLERQLAFEEPLTEDEGFLLV-VDT 154
                        170
                 ....*....|
gi 515989842 153 TIEDVVANAA 162
Cdd:COG0645  155 SGLEEALAAL 164
aroK PRK00131
shikimate kinase; Reviewed
1-54 3.29e-07

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 47.88  E-value: 3.29e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515989842   1 MAGSSVIV----MGvcaSGKTTIGELLAEKLGRKFIDGDDLhpranIQKMAsGQPLND 54
Cdd:PRK00131   1 MLKGPNIVligfMG---AGKSTIGRLLAKRLGYDFIDTDHL-----IEARA-GKSIPE 49
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
5-37 8.71e-07

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: 46.39  E-value: 8.71e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 515989842   5 SVIVMGVCASGKTTIGELLAEKLGRKFIDGDDL 37
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDEL 33
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
9-37 1.67e-06

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


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 45.50  E-value: 1.67e-06
                         10        20
                 ....*....|....*....|....*....
gi 515989842   9 MGvcaSGKTTIGELLAEKLGRKFIDGDDL 37
Cdd:COG0703    7 MG---AGKSTVGRLLAKRLGLPFVDTDAE 32
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
1-164 2.10e-05

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 42.70  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842   1 MAGSSVIVMGVCASGKTTIGELLAEKL---GRKF--IDGDDLhpRANIQKmasGQPLNDDDRKpwlERIRDAAYSLESKN 75
Cdd:PRK00889   2 QRGVTVWFTGLSGAGKTTIARALAEKLreaGYPVevLDGDAV--RTNLSK---GLGFSKEDRD---TNIRRIGFVANLLT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842  76 EHGIIVCSALKKSYRD---QIRDGNNNVTFLFLDGDKSLILER------MRQRQG---HFMKenmVNSQFETLERPDGEP 143
Cdd:PRK00889  74 RHGVIVLVSAISPYREtreEVRANIGNFLEVFVDAPLEVCEQRdvkglyAKARAGeikHFTG---IDDPYEPPLNPEVEC 150
                        170       180
                 ....*....|....*....|.
gi 515989842 144 RTLLVSIDTTIEDVVANAAEL 164
Cdd:PRK00889 151 RTDLESLEESVDKVLQKLEEL 171
AAA_18 pfam13238
AAA domain;
6-119 4.81e-05

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.87  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842    6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPR----ANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNehgIIV 81
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENglvlGDDPETRESKRLDEDKLDRLLDLLEENAALEEGGN---LII 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 515989842   82 CSALKKSYRDQIRDGNnnvtFLFLDGDKSLILERMRQR 119
Cdd:pfam13238  78 DGHLAELEPERAKDLV----GIVLRASPEELLERLEKR 111
aroL PRK03731
shikimate kinase AroL;
13-35 4.83e-05

shikimate kinase AroL;


Pssm-ID: 235153 [Multi-domain]  Cd Length: 171  Bit Score: 41.47  E-value: 4.83e-05
                         10        20
                 ....*....|....*....|...
gi 515989842  13 ASGKTTIGELLAEKLGRKFIDGD 35
Cdd:PRK03731  12 GCGKTTVGMALAQALGYRFVDTD 34
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
14-165 7.99e-05

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 41.23  E-value: 7.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842  14 SGKTTIGELLAEKL---GRK--FIDGDDLhpRANiqkmasgqpLN------DDDRKPWLERIRDAAYSLeskNEHGIIVC 82
Cdd:COG0529   27 SGKSTLANALERRLferGRHvyLLDGDNV--RHG---------LNkdlgfsKEDRDENIRRIGEVAKLL---ADAGLIVL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842  83 SAL---KKSYRDQIRDgnnnvtfLFLDG-------DKSL-ILERmRQRQGHFMK------ENM--VNSQFETLERPDgep 143
Cdd:COG0529   93 VAFispYRADREEARE-------LIGEGefievyvDTPLeVCEA-RDPKGLYAKarageiKNFtgIDDPYEAPENPE--- 161
                        170       180
                 ....*....|....*....|..
gi 515989842 144 rtllVSIDTTIEDVVANAAELI 165
Cdd:COG0529  162 ----LVLDTDKESVEESVEKIL 179
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
6-139 1.50e-04

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 39.99  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842    6 VIVM-GVCASGKTTIGELLAEKLGRKFIDGDDLhpRANIQKMASGQPLNDDDRKPWL-ERIRDAAYSLESKNEHGIIVCS 83
Cdd:pfam13671   1 LILLvGLPGSGKSTLARRLLEELGAVRLSSDDE--RKRLFGEGRPSISYYTDATDRTyERLHELARIALRAGRPVILDAT 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515989842   84 ALKKSYRDQIRD--GNNNVTF--LFLDGDKSLILERMRQRQGH-----FMKENMVNSQFETLERP 139
Cdd:pfam13671  79 NLRRDERARLLAlaREYGVPVriVVFEAPEEVLRERLAARARAggdpsDVPEEVLDRQKARFEPP 143
PLN02199 PLN02199
shikimate kinase
1-41 5.26e-04

shikimate kinase


Pssm-ID: 177850 [Multi-domain]  Cd Length: 303  Bit Score: 39.30  E-value: 5.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 515989842   1 MAGSSVIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRA 41
Cdd:PLN02199 100 LNGRSMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQA 140
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
14-38 6.55e-04

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 38.65  E-value: 6.55e-04
                         10        20
                 ....*....|....*....|....*
gi 515989842  14 SGKTTIGELLAEKLGRKFIDGDDLH 38
Cdd:COG1102   11 SGGTTIAKRLAEKLGLPLYDGEILR 35
PRK13947 PRK13947
shikimate kinase; Provisional
6-47 6.76e-04

shikimate kinase; Provisional


Pssm-ID: 184412 [Multi-domain]  Cd Length: 171  Bit Score: 38.53  E-value: 6.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 515989842   6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDLhpranIQKMA 47
Cdd:PRK13947   4 IVLIGFMGTGKTTVGKRVATTLSFGFIDTDKE-----IEKMT 40
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
10-81 4.81e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 35.54  E-value: 4.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515989842  10 GVCASGKTTIGELLAEKLGRKFIDGDDLHpRANIQKMASGQPLNDDDRKPWLERIRDAAysleskNEHGIIV 81
Cdd:cd02020    6 GPAGSGKSTVAKLLAKKLGLPYLDTGGIR-TEEVGKLASEVAAIPEVRKALDERQRELA------KKPGIVL 70
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
6-33 5.50e-03

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 35.95  E-value: 5.50e-03
                         10        20
                 ....*....|....*....|....*...
gi 515989842   6 VIVMGVCASGKTTIGELLAEKLGRKFID 33
Cdd:COG1936    3 IAITGTPGTGKTTVAKLLAERLGLEVIH 30
PRK13949 PRK13949
shikimate kinase; Provisional
6-35 6.76e-03

shikimate kinase; Provisional


Pssm-ID: 140006 [Multi-domain]  Cd Length: 169  Bit Score: 35.48  E-value: 6.76e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 515989842   6 VIVMGVCASGKTTIGELLAEKLGRKFIDGD 35
Cdd:PRK13949   4 IFLVGYMGAGKTTLGKALARELGLSFIDLD 33
 
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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