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Conserved domains on  [gi|2449771515|gb|WDU59668|]
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NAD(P)H-hydrate dehydratase [Pseudemcibacter aquimaris]

Protein Classification

NAD(P)H-hydrate epimerase( domain architecture ID 10000547)

NAD(P)H-hydrate epimerase catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 9-486 1.74e-99

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: 308.34  E-value: 1.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515   9 VLTTTQMGEADKITIDQLqdvGKTGADLMENAGLTVVREIVGC--VDGRAALILCGPGNNGGDGFVIARHLKKHGWSVDV 86
Cdd:COG0062     3 LLTAAQMRALDRAAIEAL---GIPGLVLMERAGRAVARAIRRRfpSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  87 ALLGSVEKLSGDARVMADFWEA---EILNLTPDI--FKDQDLIVDALFGTGLSKNIGGELAKVIETANHHPAYKIAVDIP 161
Cdd:COG0062    80 FLLGDPEKLSGDAAANLERLKAagiPILELDDELpeLAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 162 SGVEGNTGKILGIAFYADKTVTFARKKPAHLIYPGKELCGDVIVTDIGInDRTIEAVEPNMFENYPALWLNAYPINSQDA 241
Cdd:COG0062   160 SGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGI-GIPAAAEAPAALLLLADLLALLLPPRRRSH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 242 HKYHHGHAVVVSGGCTKTGAARLAATSALRTGAGLVSVSSPEDALIVHASHLTSVMIRK-RAELNVDLEDQRLNAWCIGP 320
Cdd:COG0062   239 HKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALAlDDDEELLLLLAAAVVVAGGG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 321 AAGVNGQTRKDVLSIIKANKRAVLDADALTVFEEGPLELFQAINTTDEDVILTPHAGEFARLFPYQKEEDKLSATLSAAK 400
Cdd:COG0062   319 GGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAA 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 401 LSGAVVVYKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECANRIGVGLISE 480
Cdd:COG0062   399 AVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAAL 478


                  ....*.
gi 2449771515 481 DLEKEI 486
Cdd:COG0062   479 LAAAAA 484
 
Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 9-486 1.74e-99

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: 308.34  E-value: 1.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515   9 VLTTTQMGEADKITIDQLqdvGKTGADLMENAGLTVVREIVGC--VDGRAALILCGPGNNGGDGFVIARHLKKHGWSVDV 86
Cdd:COG0062     3 LLTAAQMRALDRAAIEAL---GIPGLVLMERAGRAVARAIRRRfpSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  87 ALLGSVEKLSGDARVMADFWEA---EILNLTPDI--FKDQDLIVDALFGTGLSKNIGGELAKVIETANHHPAYKIAVDIP 161
Cdd:COG0062    80 FLLGDPEKLSGDAAANLERLKAagiPILELDDELpeLAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 162 SGVEGNTGKILGIAFYADKTVTFARKKPAHLIYPGKELCGDVIVTDIGInDRTIEAVEPNMFENYPALWLNAYPINSQDA 241
Cdd:COG0062   160 SGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGI-GIPAAAEAPAALLLLADLLALLLPPRRRSH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 242 HKYHHGHAVVVSGGCTKTGAARLAATSALRTGAGLVSVSSPEDALIVHASHLTSVMIRK-RAELNVDLEDQRLNAWCIGP 320
Cdd:COG0062   239 HKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALAlDDDEELLLLLAAAVVVAGGG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 321 AAGVNGQTRKDVLSIIKANKRAVLDADALTVFEEGPLELFQAINTTDEDVILTPHAGEFARLFPYQKEEDKLSATLSAAK 400
Cdd:COG0062   319 GGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAA 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 401 LSGAVVVYKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECANRIGVGLISE 480
Cdd:COG0062   399 AVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAAL 478


                  ....*.
gi 2449771515 481 DLEKEI 486
Cdd:COG0062   479 LAAAAA 484
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 240-487 4.22e-76

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: 239.44  E-value: 4.22e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 240 DAHKYHHGHAVVVSGGCTKTGAARLAATSALRTGAGLVSVSSPEDALIVHASHLTSVMIRKRAELN---VDLEDQRLNAW 316
Cdd:cd01171     2 DSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 317 CIGPAAGVNGQTRKDVLSIIKANKRAVLDADALTVFEEGPLELFQAINttdedVILTPHAGEFARLFPY---QKEEDKLS 393
Cdd:cd01171    82 VIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKRYGP-----VVLTPHPGEFARLLGAlveEIQADRLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 394 ATLSAAKLSGAVVVYKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECANRI 473
Cdd:cd01171   157 AAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLA 236

                         250
                  ....*....|....*...
gi 2449771515 474 ----GVGLISEDLEKEIP 487
Cdd:cd01171   237 akkkGAGLTAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 29-487 6.13e-71

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 234.18  E-value: 6.13e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  29 VGKTGADLMENAGLTVVREIVGCV-DGRAALILCGPGNNGGDGFVIARHLKKHGWSVDVALLGSVEKLSGDARVMADFWE 107
Cdd:PRK10565   34 LGLTLYELMLRAGEAAFQVARSAYpDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKPLPEEAALAREAWL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 108 A---EILnlTPDIF--KDQDLIVDALFGTGLSKNIGGELAKVIETANHHPAYKIAVDIPSGVEGNTGKILGIAFYADKTV 182
Cdd:PRK10565  114 NaggEIH--AADIVwpESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINADHTV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 183 TFARKKPAHLIYPGKELCGDVIVTDIGINDRTIEAVEP--NMFENYPALWLnayPINSQDAHKYHHGHAVVVSGGCTKTG 260
Cdd:PRK10565  192 TFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPiqRFDAEQLSQWL---KPRRPTSHKGDHGRLLIIGGDHGTAG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 261 AARLAATSALRTGAGLVSVsspedalIVHASHLTSVMIrKRAELNVD-LEDQRLNA---WC----IGPAAGvNGQTRKDV 332
Cdd:PRK10565  269 AIRMAGEAALRSGAGLVRV-------LTRSENIAPLLT-ARPELMVHeLTPDSLEEsleWAdvvvIGPGLG-QQEWGKKA 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 333 LSIIKA-NKRAVLDADALTVFeegplelfqAIN-TTDEDVILTPHAGEFARLFP---YQKEEDKLSATLSAAKLSGAVVV 407
Cdd:PRK10565  340 LQKVENfRKPMLWDADALNLL---------AINpDKRHNRVITPHPGEAARLLGcsvAEIESDRLLSARRLVKRYGGVVV 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 408 YKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECANRIGV-----GLISEDL 482
Cdd:PRK10565  411 LKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAArfgtrGMLATDL 490


                  ....*
gi 2449771515 483 EKEIP 487
Cdd:PRK10565  491 FSTLQ 495
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 240-490 1.27e-49

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: 171.03  E-value: 1.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 240 DAHKYHHGHAVVVSGGCTKTGAARLAATSALRTGAGLVSVSSPEDALIVHASHLTSVMIRkRAELNVDLEDQ---RLNAW 316
Cdd:TIGR00196  18 NSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVH-RLMWKVDEDEElleRYDVV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 317 CIGPAAGVNGQTRKDVLSIIKANKRAVLDADALTVFEEGPLElfqainttDEDVILTPHAGEFARLFPYQKEE-DKLSAT 395
Cdd:TIGR00196  97 VIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKR--------EGEVILTPHPGEFKRLLGVNEIQgDRLEAA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 396 LSAAKLSGAVVVYKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECA----- 470
Cdd:TIGR00196 169 QDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGdlalk 248

                         250       260
                  ....*....|....*....|
gi 2449771515 471 NRIGVGLISEDLEKEIPFVL 490
Cdd:TIGR00196 249 NHGAYGLTALDLIEKIPRVC 268
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 33-190 5.68e-48

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 163.17  E-value: 5.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  33 GADLMENAGLTVVREIV--GCVDGRAALILCGPGNNGGDGFVIARHLKKHGWSVDVALLGSVEKLSGDARVMADFWEAE- 109
Cdd:pfam03853   1 SAVLMENAGRAAARVLKalLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 110 --ILNLTPDIFKDQ-----DLIVDALFGTGLSKNIGGELAKVIETANHHPAYKIAVDIPSGVEGNTGKILGIAFYADKTV 182
Cdd:pfam03853  81 gkIVTDNPDEDLEKllspvDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTV 160


                  ....*...
gi 2449771515 183 TFARKKPA 190
Cdd:pfam03853 161 TFGAPKPG 168
 
Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 9-486 1.74e-99

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: 308.34  E-value: 1.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515   9 VLTTTQMGEADKITIDQLqdvGKTGADLMENAGLTVVREIVGC--VDGRAALILCGPGNNGGDGFVIARHLKKHGWSVDV 86
Cdd:COG0062     3 LLTAAQMRALDRAAIEAL---GIPGLVLMERAGRAVARAIRRRfpSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  87 ALLGSVEKLSGDARVMADFWEA---EILNLTPDI--FKDQDLIVDALFGTGLSKNIGGELAKVIETANHHPAYKIAVDIP 161
Cdd:COG0062    80 FLLGDPEKLSGDAAANLERLKAagiPILELDDELpeLAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 162 SGVEGNTGKILGIAFYADKTVTFARKKPAHLIYPGKELCGDVIVTDIGInDRTIEAVEPNMFENYPALWLNAYPINSQDA 241
Cdd:COG0062   160 SGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGI-GIPAAAEAPAALLLLADLLALLLPPRRRSH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 242 HKYHHGHAVVVSGGCTKTGAARLAATSALRTGAGLVSVSSPEDALIVHASHLTSVMIRK-RAELNVDLEDQRLNAWCIGP 320
Cdd:COG0062   239 HKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALAlDDDEELLLLLAAAVVVAGGG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 321 AAGVNGQTRKDVLSIIKANKRAVLDADALTVFEEGPLELFQAINTTDEDVILTPHAGEFARLFPYQKEEDKLSATLSAAK 400
Cdd:COG0062   319 GGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAA 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 401 LSGAVVVYKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECANRIGVGLISE 480
Cdd:COG0062   399 AVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAAL 478


                  ....*.
gi 2449771515 481 DLEKEI 486
Cdd:COG0062   479 LAAAAA 484
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 227-495 3.14e-97

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: 294.72  E-value: 3.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 227 PALWLNAYPINSQDAHKYHHGHAVVVSGGCTKTGAARLAATSALRTGAGLVSVSSPEDALIVHASHLTSVMIRKRAELNV 306
Cdd:COG0063     7 PADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPEEDE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 307 DLED-QRLNAWCIGPAAGVNGQTRKDVLSIIKA-NKRAVLDADALTVFEEGPLELFQAinttDEDVILTPHAGEFARLFP 384
Cdd:COG0063    87 LLELlERADAVVIGPGLGRDEETRELLRALLEAaDKPLVLDADALNLLAEDPELLAAL----PAPTVLTPHPGEFARLLG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 385 YQKEE---DKLSATLSAAKLSGAVVVYKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACA 461
Cdd:COG0063   163 CSVAEiqaDRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAA 242

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2449771515 462 AVWMHSECANR----IGVGLISEDLEKEIPFVLQNLLE 495
Cdd:COG0063   243 GVYLHGLAGDLaaeeRGRGLLASDLIEALPAALRELLE 280
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 240-487 4.22e-76

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: 239.44  E-value: 4.22e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 240 DAHKYHHGHAVVVSGGCTKTGAARLAATSALRTGAGLVSVSSPEDALIVHASHLTSVMIRKRAELN---VDLEDQRLNAW 316
Cdd:cd01171     2 DSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 317 CIGPAAGVNGQTRKDVLSIIKANKRAVLDADALTVFEEGPLELFQAINttdedVILTPHAGEFARLFPY---QKEEDKLS 393
Cdd:cd01171    82 VIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKRYGP-----VVLTPHPGEFARLLGAlveEIQADRLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 394 ATLSAAKLSGAVVVYKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECANRI 473
Cdd:cd01171   157 AAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLA 236

                         250
                  ....*....|....*...
gi 2449771515 474 ----GVGLISEDLEKEIP 487
Cdd:cd01171   237 akkkGAGLTAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 29-487 6.13e-71

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 234.18  E-value: 6.13e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  29 VGKTGADLMENAGLTVVREIVGCV-DGRAALILCGPGNNGGDGFVIARHLKKHGWSVDVALLGSVEKLSGDARVMADFWE 107
Cdd:PRK10565   34 LGLTLYELMLRAGEAAFQVARSAYpDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKPLPEEAALAREAWL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 108 A---EILnlTPDIF--KDQDLIVDALFGTGLSKNIGGELAKVIETANHHPAYKIAVDIPSGVEGNTGKILGIAFYADKTV 182
Cdd:PRK10565  114 NaggEIH--AADIVwpESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINADHTV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 183 TFARKKPAHLIYPGKELCGDVIVTDIGINDRTIEAVEP--NMFENYPALWLnayPINSQDAHKYHHGHAVVVSGGCTKTG 260
Cdd:PRK10565  192 TFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPiqRFDAEQLSQWL---KPRRPTSHKGDHGRLLIIGGDHGTAG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 261 AARLAATSALRTGAGLVSVsspedalIVHASHLTSVMIrKRAELNVD-LEDQRLNA---WC----IGPAAGvNGQTRKDV 332
Cdd:PRK10565  269 AIRMAGEAALRSGAGLVRV-------LTRSENIAPLLT-ARPELMVHeLTPDSLEEsleWAdvvvIGPGLG-QQEWGKKA 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 333 LSIIKA-NKRAVLDADALTVFeegplelfqAIN-TTDEDVILTPHAGEFARLFP---YQKEEDKLSATLSAAKLSGAVVV 407
Cdd:PRK10565  340 LQKVENfRKPMLWDADALNLL---------AINpDKRHNRVITPHPGEAARLLGcsvAEIESDRLLSARRLVKRYGGVVV 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 408 YKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECANRIGV-----GLISEDL 482
Cdd:PRK10565  411 LKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAArfgtrGMLATDL 490


                  ....*
gi 2449771515 483 EKEIP 487
Cdd:PRK10565  491 FSTLQ 495
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 240-490 1.27e-49

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: 171.03  E-value: 1.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 240 DAHKYHHGHAVVVSGGCTKTGAARLAATSALRTGAGLVSVSSPEDALIVHASHLTSVMIRkRAELNVDLEDQ---RLNAW 316
Cdd:TIGR00196  18 NSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVH-RLMWKVDEDEElleRYDVV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 317 CIGPAAGVNGQTRKDVLSIIKANKRAVLDADALTVFEEGPLElfqainttDEDVILTPHAGEFARLFPYQKEE-DKLSAT 395
Cdd:TIGR00196  97 VIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKR--------EGEVILTPHPGEFKRLLGVNEIQgDRLEAA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 396 LSAAKLSGAVVVYKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECA----- 470
Cdd:TIGR00196 169 QDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGdlalk 248

                         250       260
                  ....*....|....*....|
gi 2449771515 471 NRIGVGLISEDLEKEIPFVL 490
Cdd:TIGR00196 249 NHGAYGLTALDLIEKIPRVC 268
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 33-190 5.68e-48

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 163.17  E-value: 5.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  33 GADLMENAGLTVVREIV--GCVDGRAALILCGPGNNGGDGFVIARHLKKHGWSVDVALLGSVEKLSGDARVMADFWEAE- 109
Cdd:pfam03853   1 SAVLMENAGRAAARVLKalLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 110 --ILNLTPDIFKDQ-----DLIVDALFGTGLSKNIGGELAKVIETANHHPAYKIAVDIPSGVEGNTGKILGIAFYADKTV 182
Cdd:pfam03853  81 gkIVTDNPDEDLEKllspvDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTV 160


                  ....*...
gi 2449771515 183 TFARKKPA 190
Cdd:pfam03853 161 TFGAPKPG 168
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 250-487 4.00e-46

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: 160.99  E-value: 4.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 250 VVVSGGCTK-TGAARLAATSALRTGAGLVSVSSPEDALIVHASHLTSVMIRKRAELNVDLED-QRLNAWCIGPAAGVNGQ 327
Cdd:pfam01256   1 VLVIGGSKDyTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILEKlSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 328 TRKDVLSIIKANKRAVLDADALTVFEEGPLELFQAINTtdedvILTPHAGEFARLF--PYQKEEDKLSATLSAAKLSGAV 405
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINNEKPAREGPT-----VLTPHPGEFERLCglAGILGDDRLEAARELAQKLNGT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 406 VVYKGADTVIASPDGRCVINSHAPETLATAGSGDVLAGIITGLIAQNMPGFEAACAAVWMHSECANRI----GVGLISED 481
Cdd:pfam01256 156 ILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAaenhGVYMLPTL 235


                  ....*.
gi 2449771515 482 LEKEIP 487
Cdd:pfam01256 236 LSKIIP 241
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 8-210 3.09e-42

yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]


Pssm-ID: 272956 [Multi-domain]  Cd Length: 205  Bit Score: 149.48  E-value: 3.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515   8 AVLTTTQMgEADKITIDQLqdvGKTGADLMENAGLTVVREIV-GCVDGRAALILCGPGNNGGDGFVIARHLKkhGWSVDV 86
Cdd:TIGR00197   2 VVVSPKDM-AIDKENAEYL---GLTLDLLMENAGKAVAQAVLqAYPLAGHVIIFCGPGNNGGDGFVVARHLK--GFGVEV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  87 ALLGSVEKLSG--DARVMADFWEAEIL-----NLTPDIfkDQDLIVDALFGTGLSKNIGGELAKVIETANHHPAYKIAVD 159
Cdd:TIGR00197  76 FLLKKEKRIECteQAEVNLKALKVGGIsidegNLVKPE--DCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVD 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2449771515 160 IPSGVEGNTGKILGIAFYADKTVTFARKKPAhLIYPGKELCGDVIVTDIGI 210
Cdd:TIGR00197 154 IPSGLDVDTGAIEGPAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGI 203
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 15-188 1.02e-16

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 82.59  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  15 MGEADKITIDQ--LQDVGKTGADLMENAGLTV---VREIVGCVDGRAALILCGPGNNGGDGFVIARHLKKHGWSVDV--- 86
Cdd:PLN03049   15 LSQREAIAIDEhlMGPLGFSVDQLMELAGLSVasaIAEVYSPSEYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSIcyp 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  87 ---------ALLGSVEKLSgdarVMADFWEaeilNLTPDIFKDQDLIVDALFGTGLSKNIGGELAKVIE--TANHHPAYK 155
Cdd:PLN03049   95 krtdkplynGLVTQLESLS----VPFLSVE----DLPSDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQklVRAAGPPPI 166

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2449771515 156 IAVDIPSGVEGNTGKILGIAFYADKTVTFARKK 188
Cdd:PLN03049  167 VSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPK 199
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 36-201 6.41e-15

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 74.53  E-value: 6.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  36 LMENAGLTVVREIVGCVDGRAA----------LILCGPGNNGGDGFVIARHLKKHGWSVDVA------------LLGSVE 93
Cdd:PLN03050   32 LMELAGLSVAEAVYEVADGEKAsnppgrhprvLLVCGPGNNGGDGLVAARHLAHFGYEVTVCypkqsskphyenLVTQCE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  94 KL--SGDARVMADFWEAEILNLTPDIfkdqdlIVDALFG---TGLSKNIGGELAKVIETANHHPAYKIAVDIPSGVEGNT 168
Cdd:PLN03050  112 DLgiPFVQAIGGTNDSSKPLETTYDV------IVDAIFGfsfHGAPRAPFDTLLAQMVQQQKSPPPIVSVDVPSGWDVDE 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2449771515 169 GKILGIAFYADKTVTFARKKPAHLIYPGKELCG 201
Cdd:PLN03050  186 GDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 10-200 1.35e-12

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 69.97  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  10 LTTTQMGEADKITIDQLqdvGKTGADLMENAGLTV---VREIVGCVDGRAALILCGPGNNGGDGFVIARHLKKHGWSVDV 86
Cdd:PLN02918   91 LTQREAAEIDETLMGPL---GFSVDQLMELAGLSVaasIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515  87 ------------ALLGSVEKLSgdarvmADFWEAEilNLTPDIFKDQDLIVDALFG---TGLSKNIGGELAK------VI 145
Cdd:PLN02918  168 cypkrtakplytGLVTQLESLS------VPFVSVE--DLPADLSKDFDIIVDAMFGfsfHGAPRPPFDDLIRrlvslqNY 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 146 ETANHHPAYkIAVDIPSGVEGNTGKILGIAFYADKTVTFARKK--------PAHLI-------------------YPGKE 198
Cdd:PLN02918  240 EQTLKHPVI-VSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKlcakkfrgPHHFLggrfvppsivekyklhlppYPGTS 318


                  ..
gi 2449771515 199 LC 200
Cdd:PLN02918  319 MC 320
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 388-470 6.98e-05

4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.


Pssm-ID: 238575 [Multi-domain]  Cd Length: 242  Bit Score: 44.45  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449771515 388 EEDKLSATLSAAKLSGAVVVYKGADTVIASPDGRCVI-NSHAPETLATaGSGDVLAGIITGLIAQNMPGFEAACAAVWMH 466
Cdd:cd01170   138 EEDALELAKALARKYGAVVVVTGEVDYITDGERVVVVkNGHPLLTKIT-GTGCLLGAVIAAFLAVGDDPLEAAVSAVLVY 216


                  ....
gi 2449771515 467 SECA 470
Cdd:cd01170   217 GIAG 220
 
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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