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Conserved domains on  [gi|1622873270|ref|XP_014973490|]
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probable gluconokinase isoform X1 [Macaca mulatta]

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 ...
67-225 3.42e-67

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: 204.21  E-value: 3.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  67 ELGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVASGQHVVLACSALKKMYRDILTQGKDGAALkce 146
Cdd:COG3265    24 RLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLACSALKRSYRDRLREGNPDVRF--- 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622873270 147 esekeakraemqllvVHLSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPPAAPENFIQISVDKNVSEIIAKIMETLK 225
Cdd:COG3265   101 ---------------VYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQILAALG 164
 
Name Accession Description Interval E-value
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
67-225 3.42e-67

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: 204.21  E-value: 3.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  67 ELGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVASGQHVVLACSALKKMYRDILTQGKDGAALkce 146
Cdd:COG3265    24 RLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLACSALKRSYRDRLREGNPDVRF--- 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622873270 147 esekeakraemqllvVHLSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPPAAPENFIQISVDKNVSEIIAKIMETLK 225
Cdd:COG3265   101 ---------------VYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQILAALG 164
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
57-209 2.82e-54

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: 170.90  E-value: 2.82e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  57 VAGDGR----ERLGE-LGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVAS-GQHVVLACSALKKMY 130
Cdd:cd02021     7 VSGSGKstvgKALAErLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAKLASaGEGVVVACSALKRIY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270 131 RDILTQGkdgaalkceesekeakRAEMQLLVVHLSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPP-AAPENFIQISV 209
Cdd:cd02021    87 RDILRGG----------------AANPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPgEDEEDVIVIDV 150
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
57-222 3.59e-44

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: 145.62  E-value: 3.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  57 VAGDGRERLG-----ELGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVASGQHVVLACSALKKMYR 131
Cdd:TIGR01313   6 VAGSGKSTIAsalahRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSALKRHYR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270 132 DILtqgkdgaalkceesekeaKRAEMQLLVVHLSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPPAAPE-NFIQISVD 210
Cdd:TIGR01313  86 DIL------------------REAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADEtDVLRVDID 147
                         170
                  ....*....|..
gi 1622873270 211 KNVSEIIAKIME 222
Cdd:TIGR01313 148 QPLEGVEEDCIA 159
gntK PRK11545
gluconokinase;
67-225 3.16e-34

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 120.20  E-value: 3.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  67 ELGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVASGQHVVLACSALKKMYRDILTQGKDgaalkce 146
Cdd:PRK11545   18 QLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKHYRDLLREGNP------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270 147 esekeakraemQLLVVHLSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPPAAPENFIQ-ISVDKNVSEIIAKIMETLK 225
Cdd:PRK11545   91 -----------NLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLvVDIDQPLEGVVASTIEVIK 159
 
Name Accession Description Interval E-value
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
67-225 3.42e-67

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: 204.21  E-value: 3.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  67 ELGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVASGQHVVLACSALKKMYRDILTQGKDGAALkce 146
Cdd:COG3265    24 RLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLACSALKRSYRDRLREGNPDVRF--- 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622873270 147 esekeakraemqllvVHLSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPPAAPENFIQISVDKNVSEIIAKIMETLK 225
Cdd:COG3265   101 ---------------VYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQILAALG 164
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
57-209 2.82e-54

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: 170.90  E-value: 2.82e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  57 VAGDGR----ERLGE-LGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVAS-GQHVVLACSALKKMY 130
Cdd:cd02021     7 VSGSGKstvgKALAErLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAKLASaGEGVVVACSALKRIY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270 131 RDILTQGkdgaalkceesekeakRAEMQLLVVHLSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPP-AAPENFIQISV 209
Cdd:cd02021    87 RDILRGG----------------AANPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPgEDEEDVIVIDV 150
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
57-222 3.59e-44

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: 145.62  E-value: 3.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  57 VAGDGRERLG-----ELGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVASGQHVVLACSALKKMYR 131
Cdd:TIGR01313   6 VAGSGKSTIAsalahRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSALKRHYR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270 132 DILtqgkdgaalkceesekeaKRAEMQLLVVHLSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPPAAPE-NFIQISVD 210
Cdd:TIGR01313  86 DIL------------------REAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADEtDVLRVDID 147
                         170
                  ....*....|..
gi 1622873270 211 KNVSEIIAKIME 222
Cdd:TIGR01313 148 QPLEGVEEDCIA 159
gntK PRK11545
gluconokinase;
67-225 3.16e-34

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 120.20  E-value: 3.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  67 ELGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVASGQHVVLACSALKKMYRDILTQGKDgaalkce 146
Cdd:PRK11545   18 QLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKHYRDLLREGNP------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270 147 esekeakraemQLLVVHLSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPPAAPENFIQ-ISVDKNVSEIIAKIMETLK 225
Cdd:PRK11545   91 -----------NLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLvVDIDQPLEGVVASTIEVIK 159
idnK PRK09825
gluconokinase;
57-216 6.15e-34

gluconokinase;


Pssm-ID: 182097  Cd Length: 176  Bit Score: 119.75  E-value: 6.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270  57 VAGDGRERLGE-----LGWKFYDADDYHPEENRKKMGKGIPLDDQDRIPWLCNLHDILLRDVASGQHVVLACSALKKMYR 131
Cdd:PRK09825   11 VSGSGKSLIGSkiaalFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFIVCSSLKKQYR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873270 132 DILTQGKDGaalkceesekeakraemqllvVH---LSGSFEVISGRLLKRKGHFMPPELLQSQFETLEPPAAPE-NFIQI 207
Cdd:PRK09825   91 DILRKSSPN---------------------VHflwLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPCADEhDIARI 149

                  ....*....
gi 1622873270 208 SVDKNVSEI 216
Cdd:PRK09825  150 DVNHDIENV 158
 
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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