NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|506486102|ref|WP_015962647|]
View 

gluconokinase [Pseudocitrobacter corydidari]

Protein Classification

gluconokinase( domain architecture ID 10793587)

gluconokinase catalyzes the phosphoryl transfer from ATP to gluconate to form gluconate-6-phoshate; similar to Escherichia coli thermoresistant gluconokinase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
gntK PRK11545
gluconokinase;
14-176 4.19e-131

gluconokinase;


:

Pssm-ID: 236926  Cd Length: 163  Bit Score: 363.65  E-value: 4.19e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  14 MGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKA 93
Cdd:PRK11545   1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  94 YRDILRKGNPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADERDVLVVDIDQPLEGVINSTIEVINK 173
Cdd:PRK11545  81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLVVDIDQPLEGVVASTIEVIKK 160


                 ...
gi 506486102 174 GSN 176
Cdd:PRK11545 161 GKT 163
 
Name Accession Description Interval E-value
gntK PRK11545
gluconokinase;
14-176 4.19e-131

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 363.65  E-value: 4.19e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  14 MGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKA 93
Cdd:PRK11545   1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  94 YRDILRKGNPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADERDVLVVDIDQPLEGVINSTIEVINK 173
Cdd:PRK11545  81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLVVDIDQPLEGVVASTIEVIKK 160


                 ...
gi 506486102 174 GSN 176
Cdd:PRK11545 161 GKT 163
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 11-173 3.67e-97

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: 278.13  E-value: 3.67e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   11 YVLMGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSAL 90
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   91 KKAYRDILRKGNPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADERDVLVVDIDQPLEGVINSTIEV 170
Cdd:TIGR01313  81 KRHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADETDVLRVDIDQPLEGVEEDCIAV 160


                  ...
gi 506486102  171 INK 173
Cdd:TIGR01313 161 VLK 163
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 8-169 5.58e-94

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: 269.69  E-value: 5.58e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   8 HHVYVLMGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVC 87
Cdd:COG3265    1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  88 SALKKAYRDILRKGNPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADErDVLVVDIDQPLEGVINST 167
Cdd:COG3265   81 SALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDE-DAIVVDIDQPPEEIVAQI 159


                 ..
gi 506486102 168 IE 169
Cdd:COG3265  160 LA 161
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 10-156 4.19e-74

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: 219.05  E-value: 4.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  10 VYVLMGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQ-RTNKVSLIVCS 88
Cdd:cd02021    1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAKLaSAGEGVVVACS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  89 ALKKAYRDILRKG--NPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADERDVLVVDI 156
Cdd:cd02021   81 ALKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIVIDV 150
SKI pfam01202
Shikimate kinase;
18-171 1.14e-12

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 62.22  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   18 GSGKSAVASEVAHRLNAAFLDGDFLHprSNIVKMSSGEPLN----DDDRKPWLQALNDaafAMQRTNKV-SLIVCSALKK 92
Cdd:pfam01202   2 GAGKSTIGRLLAKALGLPFIDTDEEI--EKRTGMSIAEIFEeegeEGFRRLESEVLKE---LLAEHGLViATGGGAVLSE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   93 AYRDILRKGNPnlsFVYLKGDFDVIESRLKARKGH-FFKTQMLVTQFETLQ----EPSADERDVLVVDID-QPLEGVINS 166
Cdd:pfam01202  77 ENRDLLKERGI---VIYLDAPLEVLLERLKRDKTRpLLQNKDPEEELLELLfeerDPLYEEAADIVIDTDeSSPEEVATE 153


                  ....*
gi 506486102  167 TIEVI 171
Cdd:pfam01202 154 ILEAL 158
 
Name Accession Description Interval E-value
gntK PRK11545
gluconokinase;
14-176 4.19e-131

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 363.65  E-value: 4.19e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  14 MGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKA 93
Cdd:PRK11545   1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  94 YRDILRKGNPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADERDVLVVDIDQPLEGVINSTIEVINK 173
Cdd:PRK11545  81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLVVDIDQPLEGVVASTIEVIKK 160


                 ...
gi 506486102 174 GSN 176
Cdd:PRK11545 161 GKT 163
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 11-173 3.67e-97

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: 278.13  E-value: 3.67e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   11 YVLMGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSAL 90
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   91 KKAYRDILRKGNPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADERDVLVVDIDQPLEGVINSTIEV 170
Cdd:TIGR01313  81 KRHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADETDVLRVDIDQPLEGVEEDCIAV 160


                  ...
gi 506486102  171 INK 173
Cdd:TIGR01313 161 VLK 163
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 8-169 5.58e-94

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: 269.69  E-value: 5.58e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   8 HHVYVLMGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVC 87
Cdd:COG3265    1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  88 SALKKAYRDILRKGNPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADErDVLVVDIDQPLEGVINST 167
Cdd:COG3265   81 SALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDE-DAIVVDIDQPPEEIVAQI 159


                 ..
gi 506486102 168 IE 169
Cdd:COG3265  160 LA 161
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 10-156 4.19e-74

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: 219.05  E-value: 4.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  10 VYVLMGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQ-RTNKVSLIVCS 88
Cdd:cd02021    1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAKLaSAGEGVVVACS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  89 ALKKAYRDILRKG--NPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADERDVLVVDI 156
Cdd:cd02021   81 ALKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIVIDV 150
idnK PRK09825
gluconokinase;
11-163 2.29e-64

gluconokinase;


Pssm-ID: 182097  Cd Length: 176  Bit Score: 195.63  E-value: 2.29e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  11 YVLMGVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSAL 90
Cdd:PRK09825   6 YILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFIVCSSL 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506486102  91 KKAYRDILRKGNPNLSFVYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPSADERDVLVVDIDQPLEGV 163
Cdd:PRK09825  86 KKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIENV 158
SKI pfam01202
Shikimate kinase;
18-171 1.14e-12

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 62.22  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   18 GSGKSAVASEVAHRLNAAFLDGDFLHprSNIVKMSSGEPLN----DDDRKPWLQALNDaafAMQRTNKV-SLIVCSALKK 92
Cdd:pfam01202   2 GAGKSTIGRLLAKALGLPFIDTDEEI--EKRTGMSIAEIFEeegeEGFRRLESEVLKE---LLAEHGLViATGGGAVLSE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   93 AYRDILRKGNPnlsFVYLKGDFDVIESRLKARKGH-FFKTQMLVTQFETLQ----EPSADERDVLVVDID-QPLEGVINS 166
Cdd:pfam01202  77 ENRDLLKERGI---VIYLDAPLEVLLERLKRDKTRpLLQNKDPEEELLELLfeerDPLYEEAADIVIDTDeSSPEEVATE 153


                  ....*
gi 506486102  167 TIEVI 171
Cdd:pfam01202 154 ILEAL 158
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
10-159 9.07e-10

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 54.53  E-value: 9.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  10 VYVLMGVSGSGKSAVASEVAHRLNAAFLDGDFLhpRSNIVkmssGEPLNDDDRKPWL-----QALNDAAfAMQRTNKVSL 84
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAERLGAVRLRSDVV--RKRLF----GAGLAPLERSPEAtartyARLLALA-RELLAAGRSV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  85 IV-CSALKKAYRD----ILRKGNPNLSFVYLKGDFDVIESRLKARKGHF----FKTQMLVTQFETLQEPSADERDVLVVD 155
Cdd:COG0645   74 ILdATFLRRAQREafraLAEEAGAPFVLIWLDAPEEVLRERLEARNAEGgdsdATWEVLERQLAFEEPLTEDEGFLLVVD 153


                 ....
gi 506486102 156 IDQP 159
Cdd:COG0645  154 TSGL 157
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 12-173 2.37e-05

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: 42.42  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  12 VLMGVSGSGKSAVASEVAHRLNAAFLDGDFLhprsnIVKMsSGEPLndddrkPWLQALN-DAAF----------AMQRTN 80
Cdd:COG0703    2 VLIGMMGAGKSTVGRLLAKRLGLPFVDTDAE-----IEER-AGMSI------PEIFAEEgEAGFrelerevlaeLLEEEN 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  81 KV-SL---IVCSAlkkAYRDILRKGNPNlsfVYLKGDFDVIESRLKARKGH-FFKTQMLVTQFETLqepsADERDVL--- 152
Cdd:COG0703   70 AViATgggAVLSP---ENRELLKEHGTV---VYLDASPETLLERLRRDDNRpLLQGEDPRERLEEL----LAEREPLyre 139

                        170       180
                 ....*....|....*....|....*.
gi 506486102 153 ----VVDID-QPLEGVINSTIEVINK 173
Cdd:COG0703  140 vadiTVDTDgRSPEEVVDEILEALEE 165
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 12-125 3.10e-05

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: 42.16  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  12 VLMGVSGSGKSAVASEVAHRLNAAFLDGDFLhprsnIVK---MSSGEPLNDDD----RKPWLQALNDAAfamQRTNKV-S 83
Cdd:cd00464    3 VLIGMMGAGKTTVGRLLAKALGLPFVDLDEL-----IEQragMSIPEIFAEEGeegfRELEREVLLLLL---TKENAViA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 506486102  84 L---IVCSAlkKAYRDILRKGNpnlsFVYLKGDFDVIESRLKARK 125
Cdd:cd00464   75 TgggAVLRE--ENRRLLLENGI----VVWLDASPEELLERLARDK 113
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 15-126 3.46e-05

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 41.69  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  15 GVSGSGKSAVASEVAHRLNAA-----FLDGDFLhpRSNIvkmSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSA 89
Cdd:cd02027    6 GLSGSGKSTIARALEEKLFQRgrpvyVLDGDNV--RHGL---NKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 506486102  90 LKKAYRDILRKGNPNLSF--VYLKGDFDVIESR------LKARKG 126
Cdd:cd02027   81 PYREDREAARKIIGGGDFleVFVDTPLEVCEQRdpkglyKKARAG 125
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 15-126 4.97e-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: 42.00  E-value: 4.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  15 GVSGSGKSAVASEVAHRLNAA-----FLDGDFLhpRSNIvkmSSGEPLNDDDRKPWLQALNDAAFAMQRTNkvsLIVCSA 89
Cdd:COG0529   23 GLSGSGKSTLANALERRLFERgrhvyLLDGDNV--RHGL---NKDLGFSKEDRDENIRRIGEVAKLLADAG---LIVLVA 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 506486102  90 L---KKAYRDILRK--GNPNLSFVYLKGDFDVIESR----L--KARKG 126
Cdd:COG0529   95 FispYRADREEAREliGEGEFIEVYVDTPLEVCEARdpkgLyaKARAG 142
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 13-126 1.65e-04

Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.


Pssm-ID: 396247 [Multi-domain]  Cd Length: 154  Bit Score: 39.99  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   13 LMGVSGSGKSAVASEVAHRLN-----AAFLDGDflhprsNI-VKMSSGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLiv 86
Cdd:pfam01583   7 LTGLSGAGKSTIANALERKLFeqgrsVYVLDGD------NVrHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVI-- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 506486102   87 CSALK--KAYRDILRKGNPNLSF--VYLKGDFDVIESR------LKARKG 126
Cdd:pfam01583  79 TAFISpyREDREQARELHEEGKFieVFVDTPLEVCEQRdpkglyKKARAG 128
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 6-158 3.11e-04

adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 129547  Cd Length: 184  Bit Score: 39.37  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102    6 HDHHVYVLMGVSGSGKSAVASEVAHRL-----NAAFLDGDflhprsNI-VKMSSGEPLNDDDRKPWLQALNDAAFAMQRT 79
Cdd:TIGR00455  16 HRGVVIWLTGLSGSGKSTIANALEKKLeskgyRVYVLDGD------NVrHGLNKDLGFSEEDRKENIRRIGEVAKLFVRN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   80 NKVSLIVCSALKKAYRDILRKGNPNLSF--VYLKGDFDVIESR------LKARKGHFFKTQMLVTQFEtlqEPSADErdv 151
Cdd:TIGR00455  90 GIIVITSFISPYRADRQMVRELIEKGEFieVFVDCPLEVCEQRdpkglyKKARNGEIKGFTGIDSPYE---APENPE--- 163


                  ....*..
gi 506486102  152 LVVDIDQ 158
Cdd:TIGR00455 164 VVLDTDQ 170
aroK PRK00131
shikimate kinase; Reviewed
 12-122 3.83e-04

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.02  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  12 VLMGVSGSGKSAVASEVAHRLNAAFLDGDFLhprsnIVKMsSGEPLND--DD------RKPWLQALNDAAfamQRTNKV- 82
Cdd:PRK00131   8 VLIGFMGAGKSTIGRLLAKRLGYDFIDTDHL-----IEAR-AGKSIPEifEEegeaafRELEEEVLAELL---ARHNLVi 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 506486102  83 SL---IVcsaLKKAYRDILRKGNPNlsfVYLKGDFDVIESRLK 122
Cdd:PRK00131  79 STgggAV---LREENRALLRERGTV---VYLDASFEELLRRLR 115
COG3903 COG3903
Predicted ATPase [General function prediction only];
12-39 1.05e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 38.85  E-value: 1.05e-03
                         10        20
                 ....*....|....*....|....*...
gi 506486102  12 VLMGVSGSGKSAVASEVAHRLNAAFLDG 39
Cdd:COG3903  180 TLTGPGGVGKTRLALEVAHRLADRFPDG 207
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
15-38 1.34e-03

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 38.08  E-value: 1.34e-03
                         10        20
                 ....*....|....*....|....
gi 506486102  15 GVSGSGKSAVASEVAHRLNAAFLD 38
Cdd:COG0283    7 GPAGSGKSTVAKALAKRLGYHYLD 30
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 13-128 2.43e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 36.92  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102  13 LMGVSGSGKSAVASEVAHRLNAA-----FLDGDFLhpRSNIVKmssGEPLNDDDRKPWLQALndaAFAMQRTNKVSLIVC 87
Cdd:PRK00889   9 FTGLSGAGKTTIARALAEKLREAgypveVLDGDAV--RTNLSK---GLGFSKEDRDTNIRRI---GFVANLLTRHGVIVL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 506486102  88 SALKKAYRDI---LRKGNPNLSFVYLKGDFDVIESR------LKARKG---HF 128
Cdd:PRK00889  81 VSAISPYRETreeVRANIGNFLEVFVDAPLEVCEQRdvkglyAKARAGeikHF 133
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 15-38 2.84e-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: 36.31  E-value: 2.84e-03
                         10        20
                 ....*....|....*....|....
gi 506486102  15 GVSGSGKSAVASEVAHRLNAAFLD 38
Cdd:cd02020    6 GPAGSGKSTVAKLLAKKLGLPYLD 29
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 12-127 4.36e-03

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: 35.75  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   12 VLM-GVSGSGKSAVASEVAHRLNAAFLDGDFLHPRSNIVKMSSGEPLNdDDRKPWLQALNDAAFAMQRTNKVSLIVCSAL 90
Cdd:pfam13671   2 ILLvGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEGRPSISYYT-DATDRTYERLHELARIALRAGRPVILDATNL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 506486102   91 KKAYRDILRKGNPNLSF----VYLKGDFDVIESRLKARKGH 127
Cdd:pfam13671  81 RRDERARLLALAREYGVpvriVVFEAPEEVLRERLAARARA 121
PRK13946 PRK13946
shikimate kinase; Provisional
 7-40 4.44e-03

shikimate kinase; Provisional


Pssm-ID: 184411 [Multi-domain]  Cd Length: 184  Bit Score: 36.06  E-value: 4.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 506486102   7 DHHVYVLMGVSGSGKSAVASEVAHRLNAAFLDGD 40
Cdd:PRK13946   9 GKRTVVLVGLMGAGKSTVGRRLATMLGLPFLDAD 42
AAA_18 pfam13238
AAA domain;
12-130 5.45e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 35.48  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506486102   12 VLMGVSGSGKSAVASEVAHRLNAAFLDGDFLHPR----SNIVKMSSGEPLNDDDRKPWLQALNDAAfamQRTNKVSLIV- 86
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDNVRDLALENglvlGDDPETRESKRLDEDKLDRLLDLLEENA---ALEEGGNLIId 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 506486102   87 -CSALKKAYRDILRKgnpnlsFVYLKGDFDVIESRLKARKGHFFK 130
Cdd:pfam13238  79 gHLAELEPERAKDLV------GIVLRASPEELLERLEKRGYEEAK 117
Pgk2 COG2074
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ...
 15-37 7.56e-03

2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 441677  Cd Length: 207  Bit Score: 35.69  E-value: 7.56e-03
                         10        20
                 ....*....|....*....|...
gi 506486102  15 GVSGSGKSAVASEVAHRLNAAFL 37
Cdd:COG2074   13 GASGVGKSTIAAELARRLGIPRV 35
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 10-39 9.61e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 33.46  E-value: 9.61e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 506486102  10 VYVLMGVSGSGKSAVASEVAHRL---NAAFLDG 39
Cdd:cd02019    1 IIAITGGSGSGKSTVAKKLAEQLggrSVVVLDE 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH