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Conserved domains on  [gi|1092263533|gb|AOY72617|]
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carbohydrate kinase [Arthrobacter sp. ZXY-2]

Protein Classification

NAD(P)H-hydrate dehydratase( domain architecture ID 10000556)

ADP-dependent NAD(P)H-hydrate dehydratase catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 11-303 3.68e-71

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


:

Pssm-ID: 439833  Cd Length: 280  Bit Score: 221.15  E-value: 3.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  11 VTPSLLRDWsLPAPGED--KYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGAVGLPE 88
Cdd:COG0063     5 LTPADLRAL-LPPRPPDshKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  89 DskgsitgkglDRISSYLDRADAVLIGPGLDDQELSRDLLFALLEReedrggqaptQGPAVVLDAFALGALPELEDRLDP 168
Cdd:COG0063    84 E----------DELLELLERADAVVIGPGLGRDEETRELLRALLEA----------ADKPLVLDADALNLLAEDPELLAA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 169 WRGRMILTPNPTEAGILLGRDVEDLEAD----VAAVARKFDAVVSCQG---YIAGApgtsetESTLWKITTGYGGLGTSG 241
Cdd:COG0063   144 LPAPTVLTPHPGEFARLLGCSVAEIQADrleaAREAAKRYGAVVVLKGagtVIAAP------DGRVYINPTGNPGLATAG 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092263533 242 SGDVLAGAIAGLRARGTSSTQAACWGTHLHAAAADRLASTMGPlGFLARELADQLPALMLEL 303
Cdd:COG0063   218 SGDVLAGIIAGLLAQGLDPFEAAAAGVYLHGLAGDLAAEERGR-GLLASDLIEALPAALREL 278
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 11-303 3.68e-71

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


Pssm-ID: 439833  Cd Length: 280  Bit Score: 221.15  E-value: 3.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  11 VTPSLLRDWsLPAPGED--KYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGAVGLPE 88
Cdd:COG0063     5 LTPADLRAL-LPPRPPDshKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  89 DskgsitgkglDRISSYLDRADAVLIGPGLDDQELSRDLLFALLEReedrggqaptQGPAVVLDAFALGALPELEDRLDP 168
Cdd:COG0063    84 E----------DELLELLERADAVVIGPGLGRDEETRELLRALLEA----------ADKPLVLDADALNLLAEDPELLAA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 169 WRGRMILTPNPTEAGILLGRDVEDLEAD----VAAVARKFDAVVSCQG---YIAGApgtsetESTLWKITTGYGGLGTSG 241
Cdd:COG0063   144 LPAPTVLTPHPGEFARLLGCSVAEIQADrleaAREAAKRYGAVVVLKGagtVIAAP------DGRVYINPTGNPGLATAG 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092263533 242 SGDVLAGAIAGLRARGTSSTQAACWGTHLHAAAADRLASTMGPlGFLARELADQLPALMLEL 303
Cdd:COG0063   218 SGDVLAGIIAGLLAQGLDPFEAAAAGVYLHGLAGDLAAEERGR-GLLASDLIEALPAALREL 278
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 24-297 5.79e-49

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


Pssm-ID: 238576  Cd Length: 254  Bit Score: 163.55  E-value: 5.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  24 PGEDKYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGAVGLPEDSKGSITGKgldris 103
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLEL------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 104 syLDRADAVLIGPGLDDQELSRDLLFALLEReedrggqaptqGPAVVLDAFALGALPELEDRLDPwRGRMILTPNPTEAG 183
Cdd:cd01171    75 --LERADAVVIGPGLGRDEEAAEILEKALAK-----------DKPLVLDADALNLLADEPSLIKR-YGPVVLTPHPGEFA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 184 ILLGRDVEDLEAD----VAAVARKFDAVVSCQG---YIAGAPGtsetesTLWKITTGYGGLGTSGSGDVLAGAIAGLRAR 256
Cdd:cd01171   141 RLLGALVEEIQADrlaaAREAAAKLGATVVLKGavtVIADPDG------RVYVNPTGNPGLATGGSGDVLAGIIAALLAQ 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1092263533 257 GTSSTQAACWGTHLHAAAADRLASTMGpLGFLARELADQLP 297
Cdd:cd01171   215 GLSPLEAAALAVYLHGLAGDLAAKKKG-AGLTAADLVAEIP 254
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 24-301 4.10e-36

yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]


Pssm-ID: 272955  Cd Length: 270  Bit Score: 130.58  E-value: 4.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  24 PGEDKYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGAVGLPEDskgsitgkgLDRIS 103
Cdd:TIGR00196  17 PNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMWK---------VDEDE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 104 SYLDRADAVLIGPGLDDQELSRDLLFALLEREEdrggqaptqgpAVVLDAFALgalpELEDRLDPWRGRMILTPNPTEAG 183
Cdd:TIGR00196  88 ELLERYDVVVIGPGLGQDPSFKKAVEEVLELDK-----------PVVLDADAL----NLLTYNQKREGEVILTPHPGEFK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 184 ILLGRDVE--DLEADVAAVARKFDAVVSCQG---YIAGAPGTsetestLWKITTGYGGLGTSGSGDVLAGAIAGLRARGT 258
Cdd:TIGR00196 153 RLLGVNEIqgDRLEAAQDIAQKLQAVVVLKGaadVIAAPDGD------LWINKTGNAALAKGGTGDVLAGLIGGLLAQNL 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1092263533 259 SSTQAACWGTHLHAAAADRLASTMGPLGFLARELADQLPALML 301
Cdd:TIGR00196 227 DPFDAACNAAFAHGLAGDLALKNHGAYGLTALDLIEKIPRVCK 269
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 34-297 1.61e-31

Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).


Pssm-ID: 396007  Cd Length: 242  Bit Score: 117.85  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  34 VLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGAVGLPEDSkgsitgkgldRISSYLDRADAVL 113
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETS----------SILEKLSRYDAVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 114 IGPGLDDQELSRDLLFALLEREEdrggqaptqgpAVVLDAFALGALPELEDRLDPwRGRMILTPNPTEAGILLGrDVEDL 193
Cdd:pfam01256  71 IGPGLGRDEKGKAALEEVLAKDC-----------PLVIDADALNLLAINNEKPAR-EGPTVLTPHPGEFERLCG-LAGIL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 194 EADVAAVARKFDAVVSCQGYIAGAPGTSET-ESTLWKITTGYGGLGTSGSGDVLAGAIAGLRARGTSSTQAACWGTHLHA 272
Cdd:pfam01256 138 GDDRLEAARELAQKLNGTILLKGNVTVIAApGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHG 217

                         250       260
                  ....*....|....*....|....*
gi 1092263533 273 AAADRLASTMGPlGFLARELADQLP 297
Cdd:pfam01256 218 AASDLAAENHGV-YMLPTLLSKIIP 241
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 5-297 1.12e-26

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 108.99  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533   5 ANTPTPV---TPSLLRDWSLP-APGEDKYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKL-TLAVAESVSVQLgVALP 79
Cdd:PRK10565  224 AGQEAPIqrfDAEQLSQWLKPrRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVrVLTRSENIAPLL-TARP 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  80 ECGAVGLPEDSkgsitgkgldrISSYLDRADAVLIGPGLDDQELSRDLLfALLEReedrggqapTQGPAVvLDAFALGAL 159
Cdd:PRK10565  303 ELMVHELTPDS-----------LEESLEWADVVVIGPGLGQQEWGKKAL-QKVEN---------FRKPML-WDADALNLL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 160 PELEDRldpwRGRMILTPNPTEAGILLGRDVEDLEAD----VAAVARKFDAVVSCQGyiAGAPGTSETEStLWKITTGYG 235
Cdd:PRK10565  361 AINPDK----RHNRVITPHPGEAARLLGCSVAEIESDrllsARRLVKRYGGVVVLKG--AGTVIAAEPDA-LAIIDVGNA 433

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092263533 236 GLGTSGSGDVLAGAIAGLRARGTSSTQAACWGTHLHAAAADRLASTMGPLGFLARELADQLP 297
Cdd:PRK10565  434 GMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGMLATDLFSTLQ 495
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 11-303 3.68e-71

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


Pssm-ID: 439833  Cd Length: 280  Bit Score: 221.15  E-value: 3.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  11 VTPSLLRDWsLPAPGED--KYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGAVGLPE 88
Cdd:COG0063     5 LTPADLRAL-LPPRPPDshKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  89 DskgsitgkglDRISSYLDRADAVLIGPGLDDQELSRDLLFALLEReedrggqaptQGPAVVLDAFALGALPELEDRLDP 168
Cdd:COG0063    84 E----------DELLELLERADAVVIGPGLGRDEETRELLRALLEA----------ADKPLVLDADALNLLAEDPELLAA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 169 WRGRMILTPNPTEAGILLGRDVEDLEAD----VAAVARKFDAVVSCQG---YIAGApgtsetESTLWKITTGYGGLGTSG 241
Cdd:COG0063   144 LPAPTVLTPHPGEFARLLGCSVAEIQADrleaAREAAKRYGAVVVLKGagtVIAAP------DGRVYINPTGNPGLATAG 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092263533 242 SGDVLAGAIAGLRARGTSSTQAACWGTHLHAAAADRLASTMGPlGFLARELADQLPALMLEL 303
Cdd:COG0063   218 SGDVLAGIIAGLLAQGLDPFEAAAAGVYLHGLAGDLAAEERGR-GLLASDLIEALPAALREL 278
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 24-297 5.79e-49

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


Pssm-ID: 238576  Cd Length: 254  Bit Score: 163.55  E-value: 5.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  24 PGEDKYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGAVGLPEDSKGSITGKgldris 103
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLEL------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 104 syLDRADAVLIGPGLDDQELSRDLLFALLEReedrggqaptqGPAVVLDAFALGALPELEDRLDPwRGRMILTPNPTEAG 183
Cdd:cd01171    75 --LERADAVVIGPGLGRDEEAAEILEKALAK-----------DKPLVLDADALNLLADEPSLIKR-YGPVVLTPHPGEFA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 184 ILLGRDVEDLEAD----VAAVARKFDAVVSCQG---YIAGAPGtsetesTLWKITTGYGGLGTSGSGDVLAGAIAGLRAR 256
Cdd:cd01171   141 RLLGALVEEIQADrlaaAREAAAKLGATVVLKGavtVIADPDG------RVYVNPTGNPGLATGGSGDVLAGIIAALLAQ 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1092263533 257 GTSSTQAACWGTHLHAAAADRLASTMGpLGFLARELADQLP 297
Cdd:cd01171   215 GLSPLEAAALAVYLHGLAGDLAAKKKG-AGLTAADLVAEIP 254
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 24-301 4.10e-36

yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]


Pssm-ID: 272955  Cd Length: 270  Bit Score: 130.58  E-value: 4.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  24 PGEDKYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGAVGLPEDskgsitgkgLDRIS 103
Cdd:TIGR00196  17 PNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMWK---------VDEDE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 104 SYLDRADAVLIGPGLDDQELSRDLLFALLEREEdrggqaptqgpAVVLDAFALgalpELEDRLDPWRGRMILTPNPTEAG 183
Cdd:TIGR00196  88 ELLERYDVVVIGPGLGQDPSFKKAVEEVLELDK-----------PVVLDADAL----NLLTYNQKREGEVILTPHPGEFK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 184 ILLGRDVE--DLEADVAAVARKFDAVVSCQG---YIAGAPGTsetestLWKITTGYGGLGTSGSGDVLAGAIAGLRARGT 258
Cdd:TIGR00196 153 RLLGVNEIqgDRLEAAQDIAQKLQAVVVLKGaadVIAAPDGD------LWINKTGNAALAKGGTGDVLAGLIGGLLAQNL 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1092263533 259 SSTQAACWGTHLHAAAADRLASTMGPLGFLARELADQLPALML 301
Cdd:TIGR00196 227 DPFDAACNAAFAHGLAGDLALKNHGAYGLTALDLIEKIPRVCK 269
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 34-297 1.61e-31

Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).


Pssm-ID: 396007  Cd Length: 242  Bit Score: 117.85  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  34 VLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGAVGLPEDSkgsitgkgldRISSYLDRADAVL 113
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETS----------SILEKLSRYDAVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 114 IGPGLDDQELSRDLLFALLEREEdrggqaptqgpAVVLDAFALGALPELEDRLDPwRGRMILTPNPTEAGILLGrDVEDL 193
Cdd:pfam01256  71 IGPGLGRDEKGKAALEEVLAKDC-----------PLVIDADALNLLAINNEKPAR-EGPTVLTPHPGEFERLCG-LAGIL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 194 EADVAAVARKFDAVVSCQGYIAGAPGTSET-ESTLWKITTGYGGLGTSGSGDVLAGAIAGLRARGTSSTQAACWGTHLHA 272
Cdd:pfam01256 138 GDDRLEAARELAQKLNGTILLKGNVTVIAApGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHG 217

                         250       260
                  ....*....|....*....|....*
gi 1092263533 273 AAADRLASTMGPlGFLARELADQLP 297
Cdd:pfam01256 218 AASDLAAENHGV-YMLPTLLSKIIP 241
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 5-297 1.12e-26

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 108.99  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533   5 ANTPTPV---TPSLLRDWSLP-APGEDKYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKL-TLAVAESVSVQLgVALP 79
Cdd:PRK10565  224 AGQEAPIqrfDAEQLSQWLKPrRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVrVLTRSENIAPLL-TARP 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  80 ECGAVGLPEDSkgsitgkgldrISSYLDRADAVLIGPGLDDQELSRDLLfALLEReedrggqapTQGPAVvLDAFALGAL 159
Cdd:PRK10565  303 ELMVHELTPDS-----------LEESLEWADVVVIGPGLGQQEWGKKAL-QKVEN---------FRKPML-WDADALNLL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 160 PELEDRldpwRGRMILTPNPTEAGILLGRDVEDLEAD----VAAVARKFDAVVSCQGyiAGAPGTSETEStLWKITTGYG 235
Cdd:PRK10565  361 AINPDK----RHNRVITPHPGEAARLLGCSVAEIESDrllsARRLVKRYGGVVVLKG--AGTVIAAEPDA-LAIIDVGNA 433

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092263533 236 GLGTSGSGDVLAGAIAGLRARGTSSTQAACWGTHLHAAAADRLASTMGPLGFLARELADQLP 297
Cdd:PRK10565  434 GMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGMLATDLFSTLQ 495
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 4-303 1.80e-12

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];


Pssm-ID: 439832 [Multi-domain]  Cd Length: 499  Bit Score: 67.59  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533   4 PANTPTPVTPSLLRDWSLPAPGEDKYSRGAVLVVGGGRSTPGAVLLAGASALRAGAGKLTLAVAESVSVQLGVALPECGA 83
Cdd:COG0062   216 APAALLLLADLLALLLPPRRRSHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533  84 VGLPEDSKGSITgkgldrissyLDRADAVLIGPGLDDQELSRDLLFALLEREEdrggqaptqgPAVVLDAFALGALPELE 163
Cdd:COG0062   296 LALDDDEELLLL----------LAAAVVVAGGGGGGGGGAGGGLLLLLLLLLL----------LLVLLAAALLLLLALAA 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 164 DRLDPWRGRMILTPNPTEAGILLGRDVEDLEADVAAVARKFDAVVSCQGYIAGAPGTSETESTLWKITTGYGGLGTSGSG 243
Cdd:COG0062   356 ALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGG 435

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 244 DVLAGAIAGLRARGTSSTQAACWGTHLHAAAADRLASTMGPLGFLARELADQLPALMLEL 303
Cdd:COG0062   436 GGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAAAAALIALLLAAALL 495
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 174-264 1.21e-05

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 45.89  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 174 ILTPNPTEAGILLGRDVEDLEADVAAVARKFDAvVSCQGYIA--GAPGTSE-------TESTLWKITTG-YGGLGTSGSG 243
Cdd:PRK06427  136 LITPNLPEAEALTGLPIADTEDEMKAAARALHA-LGCKAVLIkgGHLLDGEesvdwlfDGEGEERFSAPrIPTKNTHGTG 214

                          90       100
                  ....*....|....*....|.
gi 1092263533 244 DVLAGAIAGLRARGTSSTQAA 264
Cdd:PRK06427  215 CTLSAAIAAELAKGASLLDAV 235
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 174-275 2.24e-05

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 45.14  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 174 ILTPNPTEAGILLGRDVEDLEaDVAAVARKFDA-----VV--SCQgYIAGAPGTSE----TESTLWKITTGYGGLGTSGS 242
Cdd:COG2240   141 IITPNLTELALLTGRPYETLE-EALAAARALLAlgpkiVVvtSVP-LDDTPADKIGnlavTADGAWLVETPLLPFSPNGT 218

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1092263533 243 GDVLAGAIAGLRARGTSSTQAACwgthlHAAAA 275
Cdd:COG2240   219 GDLFAALLLAHLLRGKSLEEALE-----RAAAF 246
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 174-264 6.49e-05

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 43.73  E-value: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 174 ILTPNPTEAGILLGRDVEDLEaDVAAVARKFDA-------VVSCQG--------YIAGAPGTSETESTLWKITTGYgglg 238
Cdd:cd01173   139 IITPNQFELELLTGKKINDLE-DAKAAARALHAkgpktvvVTSVELadddriemLGSTATEAWLVQRPKIPFPAYF---- 213

                          90       100
                  ....*....|....*....|....*.
gi 1092263533 239 tSGSGDVLAGAIAGLRARGTSSTQAA 264
Cdd:cd01173   214 -NGTGDLFAALLLARLLKGKSLAEAL 238
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 174-283 5.72e-04

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 40.54  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 174 ILTPNPTEAGILLGRDVEDLEaDVAAVARKF-----DAVVSCQGYIAGA---------PGTSETESTLWKITTGYgglgT 239
Cdd:pfam08543 122 LITPNLPEAEALTGRKIKTLE-DMKEAAKKLlalgaKAVLIKGGHLEGEeavvtdvlyDGGGFYTLEAPRIPTKN----T 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1092263533 240 SGSGDVLAGAIAGLRARGTSSTQAACWGTH-LHAAAADRLASTMG 283
Cdd:pfam08543 197 HGTGCTLSAAIAANLAKGLSLPEAVREAKEyVTEAIRDALNLGKG 241
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 174-289 1.01e-03

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 40.02  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 174 ILTPNPTEAGILLGRDVEDLEaDVAAVARKF-----DAVVSCQGYIAGAPGT----SETESTLW---KITTGYgglgTSG 241
Cdd:COG0351   129 VVTPNLPEAEALLGIEITTLD-DMREAAKALlelgaKAVLVKGGHLPGDEAVdvlyDGDGVREFsapRIDTGN----THG 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1092263533 242 SGDVLAGAIAGLRARGTSSTQAACWG-THLHAAAADRLASTMG--PLGFLA 289
Cdd:COG0351   204 TGCTLSSAIAALLAKGLDLEEAVREAkEYVTQAIRAALRLGMGhgPVNHFA 254
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 109-252 2.05e-03

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


Pssm-ID: 238177 [Multi-domain]  Cd Length: 196  Bit Score: 38.62  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092263533 109 ADAVLIGPGLDDQELSRDLLFALLEReedrggqaptqGPAVVLDAFALGALPELEDRLDPWRGRMILTPNPTEAGILLGR 188
Cdd:cd00287    58 ADAVVISGLSPAPEAVLDALEEARRR-----------GVPVVLDPGPRAVRLDGEELEKLLPGVDILTPNEEEAEALTGR 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092263533 189 DVEDLEADVAAVARK----FDAVV---SCQGYIAGAPGTSETESTLWKITTgyggLGTSGSGDVLAGAIAG 252
Cdd:cd00287   127 RDLEVKEAAEAAALLlskgPKVVIvtlGEKGAIVATRGGTEVHVPAFPVKV----VDTTGAGDAFLAALAA 193
 
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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