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Conserved domains on  [gi|520845946|ref|WP_020303706|]
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MULTISPECIES: gluconokinase [Hafnia]

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

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List of domain hits

 Name Accession Description Interval E-value
gntK PRK11545
gluconokinase;
14-175 3.87e-121

gluconokinase;


:

Pssm-ID: 236926  Cd Length: 163  Bit Score: 338.61  E-value: 3.87e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  14 MGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQRTNDVSVIVCSALKKR 93
Cdd:PRK11545   1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  94 YRDRLREGNANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEQDVCAIDINQPLDAVIADTLKHIQQ 173
Cdd:PRK11545  81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLVVDIDQPLEGVVASTIEVIKK 160


                 ..
gi 520845946 174 RS 175
Cdd:PRK11545 161 GK 162
 
Name Accession Description Interval E-value
gntK PRK11545
gluconokinase;
14-175 3.87e-121

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 338.61  E-value: 3.87e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  14 MGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQRTNDVSVIVCSALKKR 93
Cdd:PRK11545   1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  94 YRDRLREGNANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEQDVCAIDINQPLDAVIADTLKHIQQ 173
Cdd:PRK11545  81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLVVDIDQPLEGVVASTIEVIKK 160


                 ..
gi 520845946 174 RS 175
Cdd:PRK11545 161 GK 162
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 8-172 3.04e-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: 270.46  E-value: 3.04e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946   8 HHVYVVMGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQRTNDVSVIVC 87
Cdd:COG3265    1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  88 SALKKRYRDRLREGNANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEqDVCAIDINQPLDAVIADT 167
Cdd:COG3265   81 SALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDE-DAIVVDIDQPPEEIVAQI 159


                 ....*
gi 520845946 168 LKHIQ 172
Cdd:COG3265  160 LAALG 164
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 11-168 1.07e-88

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: 256.56  E-value: 1.07e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946   11 YVVMGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQRTNDVSVIVCSAL 90
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSAL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520845946   91 KKRYRDRLREGNANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEQDVCAIDINQPLDAVIADTL 168
Cdd:TIGR01313  81 KRHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADETDVLRVDIDQPLEGVEEDCI 158
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 10-156 1.84e-69

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: 207.49  E-value: 1.84e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  10 VYVVMGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQ-RTNDVSVIVCS 88
Cdd:cd02021    1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAKLaSAGEGVVVACS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  89 ALKKRYRDRLREG--NANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEQDVCAIDI 156
Cdd:cd02021   81 ALKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIVIDV 150
SKI pfam01202
Shikimate kinase;
18-125 5.53e-09

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 52.59  E-value: 5.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946   18 GSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDED--RAPWLSALNDaafAMQRTNdvSVIVC---SALKK 92
Cdd:pfam01202   2 GAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEgfRRLESEVLKE---LLAEHG--LVIATgggAVLSE 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 520845946   93 RYRDRLREGNanlSFIYMDGDFDLIESRMKARK 125
Cdd:pfam01202  77 ENRDLLKERG---IVIYLDAPLEVLLERLKRDK 106
 
Name Accession Description Interval E-value
gntK PRK11545
gluconokinase;
14-175 3.87e-121

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 338.61  E-value: 3.87e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  14 MGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQRTNDVSVIVCSALKKR 93
Cdd:PRK11545   1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  94 YRDRLREGNANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEQDVCAIDINQPLDAVIADTLKHIQQ 173
Cdd:PRK11545  81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLVVDIDQPLEGVVASTIEVIKK 160


                 ..
gi 520845946 174 RS 175
Cdd:PRK11545 161 GK 162
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 8-172 3.04e-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: 270.46  E-value: 3.04e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946   8 HHVYVVMGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQRTNDVSVIVC 87
Cdd:COG3265    1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  88 SALKKRYRDRLREGNANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEqDVCAIDINQPLDAVIADT 167
Cdd:COG3265   81 SALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDE-DAIVVDIDQPPEEIVAQI 159


                 ....*
gi 520845946 168 LKHIQ 172
Cdd:COG3265  160 LAALG 164
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 11-168 1.07e-88

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: 256.56  E-value: 1.07e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946   11 YVVMGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQRTNDVSVIVCSAL 90
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSAL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520845946   91 KKRYRDRLREGNANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEQDVCAIDINQPLDAVIADTL 168
Cdd:TIGR01313  81 KRHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADETDVLRVDIDQPLEGVEEDCI 158
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 10-156 1.84e-69

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: 207.49  E-value: 1.84e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  10 VYVVMGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQ-RTNDVSVIVCS 88
Cdd:cd02021    1 IIVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAKLaSAGEGVVVACS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  89 ALKKRYRDRLREG--NANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEQDVCAIDI 156
Cdd:cd02021   81 ALKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIVIDV 150
idnK PRK09825
gluconokinase;
11-172 2.22e-65

gluconokinase;


Pssm-ID: 182097  Cd Length: 176  Bit Score: 197.94  E-value: 2.22e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  11 YVVMGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQRTNDVSVIVCSAL 90
Cdd:PRK09825   6 YILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFIVCSSL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  91 KKRYRDRLREGNANLSFIYMDGDFDLIESRMKARKGHFFKPQMLVSQFEALEVPNADEQDVCAIDINQPLDAVIADTLKH 170
Cdd:PRK09825  86 KKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPCADEHDIARIDVNHDIENVTEQCRQA 165


                 ..
gi 520845946 171 IQ 172
Cdd:PRK09825 166 VQ 167
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
10-165 3.60e-10

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 55.69  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  10 VYVVMGVSGSGKSAVASAVAQKLSCGFLDGD----FLHprsninkmseGHALNDEDRAPWLSA-----LNDAAfAMQRTN 80
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAERLGAVRLRSDvvrkRLF----------GAGLAPLERSPEATArtyarLLALA-RELLAA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  81 DVSVIV-CSALKKRYRDRLR----EGNANLSFIYMDGDFDLIESRMKARKGHF----FKPQMLVSQFEALEVPNADEQDV 151
Cdd:COG0645   70 GRSVILdATFLRRAQREAFRalaeEAGAPFVLIWLDAPEEVLRERLEARNAEGgdsdATWEVLERQLAFEEPLTEDEGFL 149

                        170
                 ....*....|....
gi 520845946 152 CAIDiNQPLDAVIA 165
Cdd:COG0645  150 LVVD-TSGLEEALA 162
SKI pfam01202
Shikimate kinase;
18-125 5.53e-09

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 52.59  E-value: 5.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946   18 GSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDED--RAPWLSALNDaafAMQRTNdvSVIVC---SALKK 92
Cdd:pfam01202   2 GAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEgfRRLESEVLKE---LLAEHG--LVIATgggAVLSE 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 520845946   93 RYRDRLREGNanlSFIYMDGDFDLIESRMKARK 125
Cdd:pfam01202  77 ENRDLLKERG---IVIYLDAPLEVLLERLKRDK 106
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 15-126 2.55e-07

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: 47.86  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  15 GVSGSGKSAVASAVAQKL-----SCGFLDGDFLhpRSNINKmseGHALNDEDRAP------WLSAL-NDAAFamqrtndv 82
Cdd:cd02027    6 GLSGSGKSTIARALEEKLfqrgrPVYVLDGDNV--RHGLNK---DLGFSREDREEnirriaEVAKLlADAGL-------- 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 520845946  83 sVIVCSALK--KRYRDRLREGNANLSF--IYMDGDFDLIESR------MKARKG 126
Cdd:cd02027   73 -IVIAAFISpyREDREAARKIIGGGDFleVFVDTPLEVCEQRdpkglyKKARAG 125
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 15-126 4.14e-06

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: 45.08  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  15 GVSGSGKSAVASAVAQKL-SCGF----LDGDFLhpRSNINK---MSeghalnDEDRAP------WLSALndaafaMQRtN 80
Cdd:COG0529   23 GLSGSGKSTLANALERRLfERGRhvylLDGDNV--RHGLNKdlgFS------KEDRDEnirrigEVAKL------LAD-A 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 520845946  81 DVSVIVCS-ALKKRYRDRLRE--GNANLSFIYMDGDFDLIESR------MKARKG 126
Cdd:COG0529   88 GLIVLVAFiSPYRADREEAREliGEGEFIEVYVDTPLEVCEARdpkglyAKARAG 142
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 15-151 5.67e-06

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: 44.38  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946   15 GVSGSGKSAVASAVAQKL-----SCGFLDGDFLhpRSNINKmseGHALNDEDRAPWLSALNDAAFAMQRTNDVSVIVCSA 89
Cdd:TIGR00455  25 GLSGSGKSTIANALEKKLeskgyRVYVLDGDNV--RHGLNK---DLGFSEEDRKENIRRIGEVAKLFVRNGIIVITSFIS 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520845946   90 LKKRYRDRLRE--GNANLSFIYMDGDFDLIESR------MKARKGHFFKPQMLVSQFEALEVP----NADEQDV 151
Cdd:TIGR00455 100 PYRADRQMVREliEKGEFIEVFVDCPLEVCEQRdpkglyKKARNGEIKGFTGIDSPYEAPENPevvlDTDQNDR 173
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 15-126 1.45e-05

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: 43.07  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946   15 GVSGSGKSAVASAVAQKL-----SCGFLDGDFLhpRSNINKmseGHALNDEDRApwlSALNDAAFAMQRTNDVSVIVCSA 89
Cdd:pfam01583   9 GLSGAGKSTIANALERKLfeqgrSVYVLDGDNV--RHGLNK---DLGFSEEDRT---ENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 520845946   90 LKKRY---RDRLREGNANLSFI--YMDGDFDLIESR------MKARKG 126
Cdd:pfam01583  81 FISPYredREQARELHEEGKFIevFVDTPLEVCEQRdpkglyKKARAG 128
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 15-128 6.59e-05

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 41.55  E-value: 6.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  15 GVSGSGKSAVASAVAQKL-----SCGFLDGDFLhpRSNINKmseGHALNDEDRAPWLSALNDAAFAMQRtNDVSVIVcSA 89
Cdd:PRK00889  11 GLSGAGKTTIARALAEKLreagyPVEVLDGDAV--RTNLSK---GLGFSKEDRDTNIRRIGFVANLLTR-HGVIVLV-SA 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 520845946  90 LKKrYRDRLREGNANL-SFI--YMDGDFDLIESR------MKARKG---HF 128
Cdd:PRK00889  84 ISP-YRETREEVRANIgNFLevFVDAPLEVCEQRdvkglyAKARAGeikHF 133
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 15-151 1.04e-04

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 41.08  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  15 GVSGSGKSAVASAVAQKL-SCGF----LDGDflhprsNINkmsegHALN------DEDRAPWLSALNDAAFAMQrtnDVS 83
Cdd:PRK03846  31 GLSGSGKSTVAGALEEALhELGVstylLDGD------NVR-----HGLCsdlgfsDADRKENIRRVGEVAKLMV---DAG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  84 VIVCSAL-------KKRYRDRLREGNanlsFI--YMDGDFDLIESR------MKARKG---HFfkpQMLVSQFEALEVP- 144
Cdd:PRK03846  97 LVVLTAFisphraeRQMVRERLGEGE----FIevFVDTPLAICEARdpkglyKKARAGeirNF---TGIDSVYEAPESPe 169

                        170
                 ....*....|
gi 520845946 145 ---NADEQDV 151
Cdd:PRK03846 170 ihlDTGEQLV 179
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 15-126 1.52e-03

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 38.37  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946  15 GVSGSGKSAVASAVAQKL-----SCGFLDGDFLhpRSNINKmseGHALNDEDRAPWLSALNDAAFAMqrtNDVSVIVCSA 89
Cdd:PRK05506 467 GLSGSGKSTIANLVERRLhalgrHTYLLDGDNV--RHGLNR---DLGFSDADRVENIRRVAEVARLM---ADAGLIVLVS 538

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 520845946  90 LKKRY---RDRLREGNANLSFI--YMDGDFDLIESR------MKARKG 126
Cdd:PRK05506 539 FISPFreeRELARALHGEGEFVevFVDTPLEVCEARdpkglyAKARAG 586
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 12-131 1.63e-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: 36.90  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520845946   12 VVM-GVSGSGKSAVASAVAQKLSCGFLDGDFLhprsnINKMSEGHALNDEDRAPWLSALNDAAF-----AMQRTNDVsVI 85
Cdd:pfam13671   2 ILLvGLPGSGKSTLARRLLEELGAVRLSSDDE-----RKRLFGEGRPSISYYTDATDRTYERLHelariALRAGRPV-IL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 520845946   86 VCSALKKRYRDRL----REGNANLSFIYMDGDFDLIESRMKARKGHFFKP 131
Cdd:pfam13671  76 DATNLRRDERARLlalaREYGVPVRIVVFEAPEEVLRERLAARARAGGDP 125
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
15-38 3.10e-03

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 36.93  E-value: 3.10e-03
                         10        20
                 ....*....|....*....|....
gi 520845946  15 GVSGSGKSAVASAVAQKLSCGFLD 38
Cdd:COG0283    7 GPAGSGKSTVAKALAKRLGYHYLD 30
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
10-83 4.18e-03

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 36.95  E-value: 4.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520845946  10 VYVVMGVSGSGKSAVASAVAQKLSCGFLDGDFLHPRSNINKMSEGHALNDEDRAPWLSALNDAAFAMQR----TNDVS 83
Cdd:PRK11860 444 VICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRAGVALDDEAAIAALARGLPVRFEGDRiwlgGEDVT 521
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 12-42 4.37e-03

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: 35.99  E-value: 4.37e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 520845946  12 VVMGVSGSGKSAVASAVAQKLSCGFLDGDFL 42
Cdd:cd00464    3 VLIGMMGAGKTTVGRLLAKALGLPFVDLDEL 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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