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Conserved domains on  [gi|578181816|gb|EUL42140|]
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YjeF family domain-containing protein [Enterobacter asburiae]

Protein Classification

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase( domain architecture ID 11484799)

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
1-502 0e+00

putative carbohydrate kinase; Provisional


:

Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 1003.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816   1 MKKNPASIPHSIWHADDLRRAEKEAADSLGITLYELMLRAGEAAFNVARSAYPQAAHWMILCGHGNNGGDGYVVARLAVA 80
Cdd:PRK10565   6 MKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  81 AGIRVTLLALESDKPLPEEASGAREAWLNAGGVIHAPDIVWPEEVDLIVDGLLGTGLRSAPRENIAALIEHANRHSAPVV 160
Cdd:PRK10565  86 AGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 161 ALDIPSGLIAQTGATPGAVIQAAHTVTFIALKPGLLTGKARDVVGVLHHHALGLESWLSGQETHLARFDASQLAAWLPPR 240
Cdd:PRK10565 166 ALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 241 RPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHELTPQSLEESLEWADVVV 320
Cdd:PRK10565 246 RPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEWADVVV 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 321 IGPGLGQQAWGKQALQKVENFRKPMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNCSVAEIESDRLLSAQRLVKRY 400
Cdd:PRK10565 326 IGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 401 GGVAVLKGAGTVVASDETQ-GIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAHGVAADKLAARYGTRGM 479
Cdd:PRK10565 406 GGVVVLKGAGTVIAAEPDAlAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGM 485
                        490       500
                 ....*....|....*....|...
gi 578181816 480 LATDLFCTLRRVVNPDVIDVEND 502
Cdd:PRK10565 486 LATDLFSTLQRIVNPEVIDKNHD 508
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
1-502 0e+00

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 1003.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816   1 MKKNPASIPHSIWHADDLRRAEKEAADSLGITLYELMLRAGEAAFNVARSAYPQAAHWMILCGHGNNGGDGYVVARLAVA 80
Cdd:PRK10565   6 MKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  81 AGIRVTLLALESDKPLPEEASGAREAWLNAGGVIHAPDIVWPEEVDLIVDGLLGTGLRSAPRENIAALIEHANRHSAPVV 160
Cdd:PRK10565  86 AGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 161 ALDIPSGLIAQTGATPGAVIQAAHTVTFIALKPGLLTGKARDVVGVLHHHALGLESWLSGQETHLARFDASQLAAWLPPR 240
Cdd:PRK10565 166 ALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 241 RPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHELTPQSLEESLEWADVVV 320
Cdd:PRK10565 246 RPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEWADVVV 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 321 IGPGLGQQAWGKQALQKVENFRKPMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNCSVAEIESDRLLSAQRLVKRY 400
Cdd:PRK10565 326 IGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 401 GGVAVLKGAGTVVASDETQ-GIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAHGVAADKLAARYGTRGM 479
Cdd:PRK10565 406 GGVVVLKGAGTVIAAEPDAlAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGM 485
                        490       500
                 ....*....|....*....|...
gi 578181816 480 LATDLFCTLRRVVNPDVIDVEND 502
Cdd:PRK10565 486 LATDLFSTLQRIVNPEVIDKNHD 508
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
227-494 3.85e-111

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: 330.55  E-value: 3.85e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 227 RFDASQLAAWLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHEL-T 305
Cdd:COG0063    4 LLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLpE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 306 PQSLEESLEWADVVVIGPGLGQQAWGKQALQKV-ENFRKPMLWDADALNLLAINPD----KRHNRILTPHPGEAARLLNC 380
Cdd:COG0063   84 EDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARLLGC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 381 SVAEIESDRLLSAQRLVKRYGGVAVLKGAGTVVAS-DETQGIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAG 459
Cdd:COG0063  164 SVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAApDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAG 243
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 578181816 460 CVAHGVAADKLAARYGtRGMLATDLFCTLRRVVNP 494
Cdd:COG0063  244 VYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
227-494 8.90e-109

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: 324.34  E-value: 8.90e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  227 RFDASQLAAWLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHEL-- 304
Cdd:TIGR00196   2 TFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmw 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  305 TPQSLEESLEWADVVVIGPGLGQQAWGKQALQKVENFRKPMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNcsVAE 384
Cdd:TIGR00196  82 KVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VNE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  385 IESDRLLSAQRLVKRYGGVAVLKGAGTVVASDETQ-GIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAH 463
Cdd:TIGR00196 160 IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDlWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAH 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578181816  464 GVAADKLAARYGTRGMLATDLFCTLRRVVNP 494
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
242-484 4.06e-90

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: 275.65  E-value: 4.06e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 242 PTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHELTPQS---LEESLEWADV 318
Cdd:cd01171    1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 319 VVIGPGLGQQAWGKQALQKVENFRKPMLWDADALNLLAINPDKRH---NRILTPHPGEAARLLNCSVAEIESDRLLSAQR 395
Cdd:cd01171   81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 396 LVKRYGGVAVLKGAGTVVAS-DETQGIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAHGVAADKLAARY 474
Cdd:cd01171  161 AAAKLGATVVLKGAVTVIADpDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240
                        250
                 ....*....|
gi 578181816 475 GTRGMLATDL 484
Cdd:cd01171  241 GAGLTAADLV 250
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
252-490 6.18e-85

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: 261.91  E-value: 6.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  252 LVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHELTPQSLE-ESLEWADVVVIGPGLGQQAW 330
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  331 GKQALQKVENFRKPMLWDADALNLLAIN---PDKRHNRILTPHPGEAARLLNCSVAeIESDRLLSAQRLVKRYGGVAVLK 407
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  408 GAGTVVASDETQ-GIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAHGVAADKLAARYGtRGMLATDLFC 486
Cdd:pfam01256 160 GNVTVIAAPGGEvWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238

                  ....
gi 578181816  487 TLRR 490
Cdd:pfam01256 239 IIPR 242
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
1-502 0e+00

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 1003.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816   1 MKKNPASIPHSIWHADDLRRAEKEAADSLGITLYELMLRAGEAAFNVARSAYPQAAHWMILCGHGNNGGDGYVVARLAVA 80
Cdd:PRK10565   6 MKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  81 AGIRVTLLALESDKPLPEEASGAREAWLNAGGVIHAPDIVWPEEVDLIVDGLLGTGLRSAPRENIAALIEHANRHSAPVV 160
Cdd:PRK10565  86 AGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 161 ALDIPSGLIAQTGATPGAVIQAAHTVTFIALKPGLLTGKARDVVGVLHHHALGLESWLSGQETHLARFDASQLAAWLPPR 240
Cdd:PRK10565 166 ALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 241 RPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHELTPQSLEESLEWADVVV 320
Cdd:PRK10565 246 RPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEWADVVV 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 321 IGPGLGQQAWGKQALQKVENFRKPMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNCSVAEIESDRLLSAQRLVKRY 400
Cdd:PRK10565 326 IGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 401 GGVAVLKGAGTVVASDETQ-GIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAHGVAADKLAARYGTRGM 479
Cdd:PRK10565 406 GGVVVLKGAGTVIAAEPDAlAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGM 485
                        490       500
                 ....*....|....*....|...
gi 578181816 480 LATDLFCTLRRVVNPDVIDVEND 502
Cdd:PRK10565 486 LATDLFSTLQRIVNPEVIDKNHD 508
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
227-494 3.85e-111

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: 330.55  E-value: 3.85e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 227 RFDASQLAAWLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHEL-T 305
Cdd:COG0063    4 LLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLpE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 306 PQSLEESLEWADVVVIGPGLGQQAWGKQALQKV-ENFRKPMLWDADALNLLAINPD----KRHNRILTPHPGEAARLLNC 380
Cdd:COG0063   84 EDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARLLGC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 381 SVAEIESDRLLSAQRLVKRYGGVAVLKGAGTVVAS-DETQGIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAG 459
Cdd:COG0063  164 SVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAApDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAG 243
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 578181816 460 CVAHGVAADKLAARYGtRGMLATDLFCTLRRVVNP 494
Cdd:COG0063  244 VYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
227-494 8.90e-109

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: 324.34  E-value: 8.90e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  227 RFDASQLAAWLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHEL-- 304
Cdd:TIGR00196   2 TFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmw 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  305 TPQSLEESLEWADVVVIGPGLGQQAWGKQALQKVENFRKPMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNcsVAE 384
Cdd:TIGR00196  82 KVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VNE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  385 IESDRLLSAQRLVKRYGGVAVLKGAGTVVASDETQ-GIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAH 463
Cdd:TIGR00196 160 IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDlWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAH 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578181816  464 GVAADKLAARYGTRGMLATDLFCTLRRVVNP 494
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
12-502 1.66e-105

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: 324.13  E-value: 1.66e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  12 IWHADDLRRAEKEAADSLGITLYELMLRAGEAAFNVARSAYP-QAAHWMILCGHGNNGGDGYVVARLAVAAGIRVTLLAL 90
Cdd:COG0062    3 LLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  91 ESDKPLPEEASGAREAWLNAGGVIH--APDIVWPEEVDLIVDGLLGTGLRSAPRENIAALIEHANRHSAPVVALDIPSGL 168
Cdd:COG0062   83 GDPEKLSGDAAANLERLKAAGIPILelDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 169 IAQTGATPGAVIQAAHTVTFIALKPGLLTGKARDVVGVLHHHALGLESWLSGQETHLARFDASQLAAWLPPRRPTSHKGD 248
Cdd:COG0062  163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHKGG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 249 HGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHELTPQSLEESLEWA-DVVVIGPGLGQ 327
Cdd:COG0062  243 GGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAaVVVAGGGGGGG 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 328 QAWGKQALQKVENFRKPMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNCSVAEIESDRLLSAQRLVKRYGGVAVLK 407
Cdd:COG0062  323 GGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVAA 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 408 GAGTVVASDETQGIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAHGVAADKLAARYGTRGMLATDLFCT 487
Cdd:COG0062  403 AAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAAA 482
                        490
                 ....*....|....*
gi 578181816 488 LRRVVNPDVIDVEND 502
Cdd:COG0062  483 AALIALLLAAALLLL 497
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
242-484 4.06e-90

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: 275.65  E-value: 4.06e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 242 PTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHELTPQS---LEESLEWADV 318
Cdd:cd01171    1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 319 VVIGPGLGQQAWGKQALQKVENFRKPMLWDADALNLLAINPDKRH---NRILTPHPGEAARLLNCSVAEIESDRLLSAQR 395
Cdd:cd01171   81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 396 LVKRYGGVAVLKGAGTVVAS-DETQGIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAHGVAADKLAARY 474
Cdd:cd01171  161 AAAKLGATVVLKGAVTVIADpDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240
                        250
                 ....*....|
gi 578181816 475 GTRGMLATDL 484
Cdd:cd01171  241 GAGLTAADLV 250
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
252-490 6.18e-85

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: 261.91  E-value: 6.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  252 LVIIGGDHGTAGAIRMTGEAALRSGAGLVRVLTRIENIAPIVTARPELMVHELTPQSLE-ESLEWADVVVIGPGLGQQAW 330
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  331 GKQALQKVENFRKPMLWDADALNLLAIN---PDKRHNRILTPHPGEAARLLNCSVAeIESDRLLSAQRLVKRYGGVAVLK 407
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  408 GAGTVVASDETQ-GIIDAGNAGMASGGMGDVLSGIIGALLGQKLPLYDAACAGCVAHGVAADKLAARYGtRGMLATDLFC 486
Cdd:pfam01256 160 GNVTVIAAPGGEvWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238

                  ....
gi 578181816  487 TLRR 490
Cdd:pfam01256 239 IIPR 242
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
13-214 4.40e-71

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: 224.98  E-value: 4.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816   13 WHADDLRRAEKEAADSLGITLYELMLRAGEAAFNVARSAYPQAAHWMILCGHGNNGGDGYVVARLAVAAGIRVTLLALES 92
Cdd:TIGR00197   3 VVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816   93 DKPLPEEASGAREAWLNAGGVIHAPDIVWPEEVDLIVDGLLGTGLRSAPRENIAALIEHANRHSAPVVALDIPSGLIAQT 172
Cdd:TIGR00197  83 RIECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDT 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578181816  173 GATPGAVIQAAHTVTFIALKPGLLTGKArDVVGVLHHHALGL 214
Cdd:TIGR00197 163 GAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGI 203
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
34-194 1.34e-47

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: 162.40  E-value: 1.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816   34 YELMLRAGEAAFNVARSAY-PQAAHWMILCGHGNNGGDGYVVARLAVAAGIRVTLLALESDKPLPEEASGAREAWLNAGG 112
Cdd:pfam03853   2 AVLMENAGRAAARVLKALLsPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  113 VIHAPDIV-----WPEEVDLIVDGLLGTGLRSAPRENIAALIEHANRHSAPVVALDIPSGLIAQTGATPGAVIQAAHTVT 187
Cdd:pfam03853  82 KIVTDNPDedlekLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVT 161

                  ....*..
gi 578181816  188 FIALKPG 194
Cdd:pfam03853 162 FGAPKPG 168
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
11-205 9.43e-16

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 76.84  E-value: 9.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  11 SIWHADDLRRAEKEAADSLGITLYELMLRAG----EAAFNVARSAYPQA-----AHWMILCGHGNNGGDGYVVARLAVAA 81
Cdd:PLN03050   7 GYLNAQDAAALDEELMSTPGFSLEQLMELAGlsvaEAVYEVADGEKASNppgrhPRVLLVCGPGNNGGDGLVAARHLAHF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  82 GIRVTLL-ALESDKPLPE------EASGAREAWLNAGGVihAPDIVWPEEVDLIVDGLLGTGLRSAPRENIAALIEHANR 154
Cdd:PLN03050  87 GYEVTVCyPKQSSKPHYEnlvtqcEDLGIPFVQAIGGTN--DSSKPLETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVQ 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578181816 155 HSA---PVVALDIPSGLIAQTGATPGAVIQAAHTVTFIALKPGLLTGKARDVVG 205
Cdd:PLN03050 165 QQKsppPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
4-192 3.87e-12

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 68.34  E-value: 3.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816   4 NPASIPHsiwhaddLRRAEKEAADS-----LGITLYELMLRAGEAAFNVARSAYPqAAHW---MILCGHGNNGGDGYVVA 75
Cdd:PLN03049   8 NPDSISY-------LSQREAIAIDEhlmgpLGFSVDQLMELAGLSVASAIAEVYS-PSEYrrvLALCGPGNNGGDGLVAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816  76 RLAVAAGIRVTLL-ALESDKPLPEEASGAREAwlnaggvIHAPDIVW-------PEEVDLIVDGLLGTGLRSAPRENIAA 147
Cdd:PLN03049  80 RHLHHFGYKPSICyPKRTDKPLYNGLVTQLES-------LSVPFLSVedlpsdlSSQFDIVVDAMFGFSFHGAPRPPFDD 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 578181816 148 LIEH--ANRHSAPVVALDIPSGLIAQTGATPGAVIQAAHTVTFIALK 192
Cdd:PLN03049 153 LIQKlvRAAGPPPIVSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPK 199
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
381-473 1.63e-09

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: 58.32  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 381 SVAEIESDRLLSAQRLVKRYGGVAVLKGAGTVVASDETQGIIDAGNAGMAS-GGMGDVLSGIIGALLGQKLPLYDAACAG 459
Cdd:cd01170  133 SSSSDEEDALELAKALARKYGAVVVVTGEVDYITDGERVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVSA 212
                         90
                 ....*....|....
gi 578181816 460 CVAHGVAADKLAAR 473
Cdd:cd01170  213 VLVYGIAGELAAER 226
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
383-473 8.96e-06

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 47.10  E-value: 8.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181816 383 AEIESDRLLSAQRLVKRYGGVAVLKGAGTVVASDETQGIIDAGNAGMAS-GGMGDVLSGIIGALLGQKLPLYDAACAGCV 461
Cdd:PRK09355 139 TDGSADAVEIAKAAAKKYGTVVVVTGEVDYITDGERVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAACA 218
                         90
                 ....*....|..
gi 578181816 462 AHGVAADKLAAR 473
Cdd:PRK09355 219 VYGIAGELAAER 230
 
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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