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Conserved domains on  [gi|2164975462|gb|UGV29660|]
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NAD(P)H-hydrate dehydratase [Halopseudomonas aestusnigri]

Protein Classification

carbohydrate kinase family protein( domain architecture ID 1008582)

carbohydrate kinase family protein similar to bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, allowing the repair of both epimers of NAD(P)HX

CATH:  3.40.1190.20|3.40.50.10260
EC:  5.1.99.6
Gene Ontology:  GO:0005524|GO:0052857
PubMed:  21994945

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK10565 super family cl32537
putative carbohydrate kinase; Provisional
 5-495 1.00e-106

putative carbohydrate kinase; Provisional


The actual alignment was detected with superfamily member PRK10565:

Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 327.40  E-value: 1.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462   5 MPAWVHSRQQTRQLDA-ALIASGIAGIDLMQRAAMAAWQAVFARWPDAGCITVLCGSGNNAGDGYLIARLALLAGWRVQV 83
Cdd:PRK10565   13 IPHSVWPADDIRRGEReAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  84 WAVSAPERLVGDAALA---WLQArdAGV---PIANWFSGATLdgvLVDALLGTGLTGSVRAPFAEAIAAINGARCPVLSV 157
Cdd:PRK10565   93 LAQESDKPLPEEAALAreaWLNA--GGEihaADIVWPESVDL---IVDALLGTGLRQAPREPYAALIDQANAHPAPVVAL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 158 DVPSGLDADRGVALGVAVKADVTVTFIALKLGLLTSQGPDLCGELVYAALA-DPLPSNVPAALELL---QWSRWqgcLPA 233
Cdd:PRK10565  168 DIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGlDSWLAGQEAPIQRFdaeQLSQW---LKP 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 234 RMKSAHKGRFGHLLLVGGGPGMGGAIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAVADaEALAPLLATADA 313
Cdd:PRK10565  245 RRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTP-DSLEESLEWADV 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 314 LVLGPGLGRCPWAEQMISACLDAALPRVLDADALNLLACQsamPELGADTVITPHPAEAARLLRCSTAEVQDDRLAALQQ 393
Cdd:PRK10565  324 VVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAIN---PDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 394 LIEPLGCHAVLKGVGSLVGSPARfEMlpGVCAAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVHALAGDLLA 473
Cdd:PRK10565  401 LVKRYGGVVVLKGAGTVIAAEPD-AL--AIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLA 477

                         490       500
                  ....*....|....*....|..
gi 2164975462 474 GELGEVGMRAGEMMPAMRRVLN 495
Cdd:PRK10565  478 ARFGTRGMLATDLFSTLQRIVN 499
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 5-495 1.00e-106

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 327.40  E-value: 1.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462   5 MPAWVHSRQQTRQLDA-ALIASGIAGIDLMQRAAMAAWQAVFARWPDAGCITVLCGSGNNAGDGYLIARLALLAGWRVQV 83
Cdd:PRK10565   13 IPHSVWPADDIRRGEReAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  84 WAVSAPERLVGDAALA---WLQArdAGV---PIANWFSGATLdgvLVDALLGTGLTGSVRAPFAEAIAAINGARCPVLSV 157
Cdd:PRK10565   93 LAQESDKPLPEEAALAreaWLNA--GGEihaADIVWPESVDL---IVDALLGTGLRQAPREPYAALIDQANAHPAPVVAL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 158 DVPSGLDADRGVALGVAVKADVTVTFIALKLGLLTSQGPDLCGELVYAALA-DPLPSNVPAALELL---QWSRWqgcLPA 233
Cdd:PRK10565  168 DIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGlDSWLAGQEAPIQRFdaeQLSQW---LKP 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 234 RMKSAHKGRFGHLLLVGGGPGMGGAIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAVADaEALAPLLATADA 313
Cdd:PRK10565  245 RRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTP-DSLEESLEWADV 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 314 LVLGPGLGRCPWAEQMISACLDAALPRVLDADALNLLACQsamPELGADTVITPHPAEAARLLRCSTAEVQDDRLAALQQ 393
Cdd:PRK10565  324 VVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAIN---PDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 394 LIEPLGCHAVLKGVGSLVGSPARfEMlpGVCAAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVHALAGDLLA 473
Cdd:PRK10565  401 LVKRYGGVVVLKGAGTVIAAEPD-AL--AIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLA 477

                         490       500
                  ....*....|....*....|..
gi 2164975462 474 GELGEVGMRAGEMMPAMRRVLN 495
Cdd:PRK10565  478 ARFGTRGMLATDLFSTLQRIVN 499
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 9-485 1.06e-84

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: 270.20  E-value: 1.06e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462   9 VHSRQQTRQLDAALIAS-GIAGIDLMQRAAMAAWQAVFARWPDAGC-ITVLCGSGNNAGDGYLIARLALLAGWRVQVWAV 86
Cdd:COG0062     3 LLTAAQMRALDRAAIEAlGIPGLVLMERAGRAVARAIRRRFPSAARrVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  87 SAPERLVGDAALAWLQARDAGVPIANWFSGATL---DGVLVDALLGTGLTGSVRAPFAEAIAAINGARCPVLSVDVPSGL 163
Cdd:COG0062    83 GDPEKLSGDAAANLERLKAAGIPILELDDELPElaeADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 164 DADRGVALGVAVKADVTVTFIALKLGLLTSQGPDLCGELVYAALADP-LPSNVPAALELLQWSRWQGCLPARMKSAHKGR 242
Cdd:COG0062   163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGiPAAAEAPAALLLLADLLALLLPPRRRSHHKGG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 243 FGHLLLVGGGPGMGGAIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAVADAEALAPLLATADALVLGPGLGR 322
Cdd:COG0062   243 GGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGGGG 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 323 CPWAEQMISACLDAALPRVLDADALNLLACQSAMPELGADTviTPHPAEAARLLRCSTAEVQDDRLAALQQLIEPLGCHA 402
Cdd:COG0062   323 GGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLL--PPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 403 VLKGVGSLVGSPARFEMLPGVCAAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVHALAGDLLAGELGEVGMR 482
Cdd:COG0062   401 AAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLA 480


                  ...
gi 2164975462 483 AGE 485
Cdd:COG0062   481 AAA 483
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 258-483 4.94e-57

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: 190.13  E-value: 4.94e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 258 AIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAV--ADAEALAPLLATADALVLGPGLGRCPWAEQMISACLD 335
Cdd:cd01171    23 AAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLleTDIEELLELLERADAVVIGPGLGRDEEAAEILEKALA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 336 AALPRVLDADALNLLACQSAMPELGADTVITPHPAEAARLLRCSTAEVQDDRLAALQQLIEPLGCHAVLKGVGSLVGSPA 415
Cdd:cd01171   103 KDKPLVLDADALNLLADEPSLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAAAREAAAKLGATVVLKGAVTVIADPD 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2164975462 416 RFEMlpgVCAAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVHALAGDLLAGELGEVGMRA 483
Cdd:cd01171   183 GRVY---VNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKKGAGLTAA 247
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 29-189 1.44e-45

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: 157.00  E-value: 1.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  29 GIDLMQRAAMAAWQAVFARWPDAG-CITVLCGSGNNAGDGYLIARLALLAGWRVQVWAVSAPERLVGDAALAWLQARDAG 107
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLSPAGpKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 108 VPIANWFSGATLD------GVLVDALLGTGLTGSVRAPFAEAIAAINGARCPVLSVDVPSGLDADRGVALGVAVKADVTV 181
Cdd:pfam03853  81 GKIVTDNPDEDLEkllspvDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTV 160


                  ....*...
gi 2164975462 182 TFIALKLG 189
Cdd:pfam03853 161 TFGAPKPG 168
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 230-496 8.69e-44

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: 155.62  E-value: 8.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 230 CLPARMKSAHKGRFGHLLLVGGGPGMGGAIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAV-ADAEALAPLL 308
Cdd:TIGR00196  11 TLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmWKVDEDEELL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 309 ATADALVLGPGLGRCPWAEQMISACLDAALPRVLDADALNLLACQsamPELGADTVITPHPAEAARLlrCSTAEVQDDRL 388
Cdd:TIGR00196  91 ERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYN---QKREGEVILTPHPGEFKRL--LGVNEIQGDRL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 389 AALQQLIEPLGCHAVLKGVGSLVGSParfemlPGVC---AAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVH 465
Cdd:TIGR00196 166 EAAQDIAQKLQAVVVLKGAADVIAAP------DGDLwinKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAH 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2164975462 466 ALAGDLLAGELGEVGMRAGEMMPAMRRVLNR 496
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 5-495 1.00e-106

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 327.40  E-value: 1.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462   5 MPAWVHSRQQTRQLDA-ALIASGIAGIDLMQRAAMAAWQAVFARWPDAGCITVLCGSGNNAGDGYLIARLALLAGWRVQV 83
Cdd:PRK10565   13 IPHSVWPADDIRRGEReAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  84 WAVSAPERLVGDAALA---WLQArdAGV---PIANWFSGATLdgvLVDALLGTGLTGSVRAPFAEAIAAINGARCPVLSV 157
Cdd:PRK10565   93 LAQESDKPLPEEAALAreaWLNA--GGEihaADIVWPESVDL---IVDALLGTGLRQAPREPYAALIDQANAHPAPVVAL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 158 DVPSGLDADRGVALGVAVKADVTVTFIALKLGLLTSQGPDLCGELVYAALA-DPLPSNVPAALELL---QWSRWqgcLPA 233
Cdd:PRK10565  168 DIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGlDSWLAGQEAPIQRFdaeQLSQW---LKP 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 234 RMKSAHKGRFGHLLLVGGGPGMGGAIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAVADaEALAPLLATADA 313
Cdd:PRK10565  245 RRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTP-DSLEESLEWADV 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 314 LVLGPGLGRCPWAEQMISACLDAALPRVLDADALNLLACQsamPELGADTVITPHPAEAARLLRCSTAEVQDDRLAALQQ 393
Cdd:PRK10565  324 VVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAIN---PDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 394 LIEPLGCHAVLKGVGSLVGSPARfEMlpGVCAAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVHALAGDLLA 473
Cdd:PRK10565  401 LVKRYGGVVVLKGAGTVIAAEPD-AL--AIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLA 477

                         490       500
                  ....*....|....*....|..
gi 2164975462 474 GELGEVGMRAGEMMPAMRRVLN 495
Cdd:PRK10565  478 ARFGTRGMLATDLFSTLQRIVN 499
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 9-485 1.06e-84

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: 270.20  E-value: 1.06e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462   9 VHSRQQTRQLDAALIAS-GIAGIDLMQRAAMAAWQAVFARWPDAGC-ITVLCGSGNNAGDGYLIARLALLAGWRVQVWAV 86
Cdd:COG0062     3 LLTAAQMRALDRAAIEAlGIPGLVLMERAGRAVARAIRRRFPSAARrVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  87 SAPERLVGDAALAWLQARDAGVPIANWFSGATL---DGVLVDALLGTGLTGSVRAPFAEAIAAINGARCPVLSVDVPSGL 163
Cdd:COG0062    83 GDPEKLSGDAAANLERLKAAGIPILELDDELPElaeADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 164 DADRGVALGVAVKADVTVTFIALKLGLLTSQGPDLCGELVYAALADP-LPSNVPAALELLQWSRWQGCLPARMKSAHKGR 242
Cdd:COG0062   163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGiPAAAEAPAALLLLADLLALLLPPRRRSHHKGG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 243 FGHLLLVGGGPGMGGAIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAVADAEALAPLLATADALVLGPGLGR 322
Cdd:COG0062   243 GGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGGGG 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 323 CPWAEQMISACLDAALPRVLDADALNLLACQSAMPELGADTviTPHPAEAARLLRCSTAEVQDDRLAALQQLIEPLGCHA 402
Cdd:COG0062   323 GGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLL--PPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 403 VLKGVGSLVGSPARFEMLPGVCAAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVHALAGDLLAGELGEVGMR 482
Cdd:COG0062   401 AAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLA 480


                  ...
gi 2164975462 483 AGE 485
Cdd:COG0062   481 AAA 483
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 218-496 1.59e-66

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: 215.76  E-value: 1.59e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 218 ALELLQWSRWQGCLPARMKSAHKGRFGHLLLVGGGPGMGGAIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRA 297
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 298 VADAEALAPLLATADALVLGPGLGRCPWAEQMISACLDAA-LPRVLDADALNLLA-CQSAMPELGADTVITPHPAEAARL 375
Cdd:COG0063    81 LPEEDELLELLERADAVVIGPGLGRDEETRELLRALLEAAdKPLVLDADALNLLAeDPELLAALPAPTVLTPHPGEFARL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 376 LRCSTAEVQDDRLAALQQLIEPLGCHAVLKGVGSLVGSParfEMLPGVCAAGNPGMAVGGMGDVLSGLLGALLAQRVPAG 455
Cdd:COG0063   161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAP---DGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPF 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2164975462 456 QAARYAVLVHALAGDLLAGElGEVGMRAGEMMPAMRRVLNR 496
Cdd:COG0063   238 EAAAAGVYLHGLAGDLAAEE-RGRGLLASDLIEALPAALRE 277
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 258-483 4.94e-57

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: 190.13  E-value: 4.94e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 258 AIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAV--ADAEALAPLLATADALVLGPGLGRCPWAEQMISACLD 335
Cdd:cd01171    23 AAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLleTDIEELLELLERADAVVIGPGLGRDEEAAEILEKALA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 336 AALPRVLDADALNLLACQSAMPELGADTVITPHPAEAARLLRCSTAEVQDDRLAALQQLIEPLGCHAVLKGVGSLVGSPA 415
Cdd:cd01171   103 KDKPLVLDADALNLLADEPSLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAAAREAAAKLGATVVLKGAVTVIADPD 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2164975462 416 RFEMlpgVCAAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVHALAGDLLAGELGEVGMRA 483
Cdd:cd01171   183 GRVY---VNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKKGAGLTAA 247
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 29-189 1.44e-45

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: 157.00  E-value: 1.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  29 GIDLMQRAAMAAWQAVFARWPDAG-CITVLCGSGNNAGDGYLIARLALLAGWRVQVWAVSAPERLVGDAALAWLQARDAG 107
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLSPAGpKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 108 VPIANWFSGATLD------GVLVDALLGTGLTGSVRAPFAEAIAAINGARCPVLSVDVPSGLDADRGVALGVAVKADVTV 181
Cdd:pfam03853  81 GKIVTDNPDEDLEkllspvDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTV 160


                  ....*...
gi 2164975462 182 TFIALKLG 189
Cdd:pfam03853 161 TFGAPKPG 168
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 230-496 8.69e-44

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: 155.62  E-value: 8.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 230 CLPARMKSAHKGRFGHLLLVGGGPGMGGAIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAV-ADAEALAPLL 308
Cdd:TIGR00196  11 TLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmWKVDEDEELL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 309 ATADALVLGPGLGRCPWAEQMISACLDAALPRVLDADALNLLACQsamPELGADTVITPHPAEAARLlrCSTAEVQDDRL 388
Cdd:TIGR00196  91 ERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYN---QKREGEVILTPHPGEFKRL--LGVNEIQGDRL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 389 AALQQLIEPLGCHAVLKGVGSLVGSParfemlPGVC---AAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVH 465
Cdd:TIGR00196 166 EAAQDIAQKLQAVVVLKGAADVIAAP------DGDLwinKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAH 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2164975462 466 ALAGDLLAGELGEVGMRAGEMMPAMRRVLNR 496
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 258-477 1.20e-41

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: 149.05  E-value: 1.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 258 AIMLAAEAALCSGAGKVSVATSAEHVAPLLARCPEVMVRAVADAEALAPLLATADALVLGPGLGRCPWAEQMISACLDAA 337
Cdd:pfam01256  13 APLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILEKLSRYDAVVIGPGLGRDEKGKAALEEVLAKD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 338 LPRVLDADALNLLACQSAMPELGADTVITPHPAEAARLLRCSTAeVQDDRLAALQQLIEPLGCHAVLKGVGSLVGSPARf 417
Cdd:pfam01256  93 CPLVIDADALNLLAINNEKPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLKGNVTVIAAPGG- 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 418 EMlpGVCAAGNPGMAVGGMGDVLSGLLGALLAQRVPAGQAARYAVLVHALAGDLLAGELG 477
Cdd:pfam01256 171 EV--WINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG 228
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 9-203 2.41e-39

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: 141.78  E-value: 2.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462   9 VHSRQQTRQLDAALIASGIAGIDLMQRAAMAAWQAVFARWPDAGCITVLCGSGNNAGDGYLIARLalLAGWRVQVWAVSA 88
Cdd:TIGR00197   3 VVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARH--LKGFGVEVFLLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  89 PERLVG--DAALAWLQARDAGVPI-ANWFSGATLDGVLVDALLGTGLTGSVRAPFAEAIAAINGARCPVLSVDVPSGLDA 165
Cdd:TIGR00197  81 EKRIECteQAEVNLKALKVGGISIdEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDV 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2164975462 166 DRGVALGVAVKADVTVTFIALKLGLLTSQgPDLCGELV 203
Cdd:TIGR00197 161 DTGAIEGPAVNADLTITFHAIKPCLLSDR-ADVTGELK 197
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 11-216 1.72e-18

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 84.93  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  11 SRQQTRQLDAALIASGIAGID-LMQRAAMAAWQAVF----ARWPDAGC-----ITVLCGSGNNAGDGYLIARLALLAGWR 80
Cdd:PLN03050   10 NAQDAAALDEELMSTPGFSLEqLMELAGLSVAEAVYevadGEKASNPPgrhprVLLVCGPGNNGGDGLVAARHLAHFGYE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  81 VQVwavSAPERlVGDAALAWL--QARDAGVPIANWFSG--------ATLDGVLVDALLGTGLTGSVRAPFAEAIAAINGA 150
Cdd:PLN03050   90 VTV---CYPKQ-SSKPHYENLvtQCEDLGIPFVQAIGGtndsskplETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVQQ 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 151 R---CPVLSVDVPSGLDADRGVALGVAVKADVTVTFIALKLGLLTSQGPD-LCGELVYAALADPLPSNVP 216
Cdd:PLN03050  166 QkspPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHfVGGRFLPPAIAEKYGLQKP 235
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 32-216 1.79e-12

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 69.11  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  32 LMQRAAMAAWQAVFARWP--DAGCITVLCGSGNNAGDGYLIARLALLAGWRVqvwAVSAPER--------LVgdaalawL 101
Cdd:PLN03049   38 LMELAGLSVASAIAEVYSpsEYRRVLALCGPGNNGGDGLVAARHLHHFGYKP---SICYPKRtdkplyngLV-------T 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462 102 QARDAGVPIANW--FSGATLDG--VLVDALLGTGLTGSVRAPFAEAIAAINGARC--PVLSVDVPSGLDADRGVALGVAV 175
Cdd:PLN03049  108 QLESLSVPFLSVedLPSDLSSQfdIVVDAMFGFSFHGAPRPPFDDLIQKLVRAAGppPIVSVDIPSGWHVEEGDVNGEGL 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2164975462 176 KADVTVTFIALKLGLLTSQGPD--LCGELVYAALADPLPSNVP 216
Cdd:PLN03049  188 KPDMLVSLTAPKLCAKMFKGPHhfLGGRFVPPAIVEKFKLHLP 230
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 54-196 1.16e-06

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 51.09  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2164975462  54 ITVLCGSGNNAGDGYLIARLALLAGWRVQVWAVSAPERLVGDAALAWLQARDAG-VPIANWFSGATLD-GVLVDALLGTG 131
Cdd:PLN02918  138 VLAICGPGNNGGDGLVAARHLHHFGYKPFVCYPKRTAKPLYTGLVTQLESLSVPfVSVEDLPADLSKDfDIIVDAMFGFS 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2164975462 132 LTGSVRAPFAEAIAAI-------NGARCPVL-SVDVPSGLDADRGVALGVAVKADVTVTFIALKLGLLTSQGP 196
Cdd:PLN02918  218 FHGAPRPPFDDLIRRLvslqnyeQTLKHPVIvSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKLCAKKFRGP 290
 
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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