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Conserved domains on  [gi|1447699868|ref|NP_313169|]
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carbohydrate kinase [Escherichia coli O157:H7 str. Sakai]

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

CATH:  3.40.1190.20|3.40.50.10260
EC:  5.1.99.6|4.2.1.136
Gene Ontology:  GO:0005524|GO:0052855|GO:0052856|GO:0052857|GO:0046496
PubMed:  21994945

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 1-503 0e+00

putative carbohydrate kinase; Provisional


:

Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 1013.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868   1 MKKNPVSIPHTVWHADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVARLAKA 80
Cdd:PRK10565    6 MKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  81 VGIEVTLLAQESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVALIVDALLGTGLQQAPRESISQLIDHANSHPAPIV 160
Cdd:PRK10565   86 AGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 161 AVDIPSGLLAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSHWLKPR 240
Cdd:PRK10565  166 ALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 241 RPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLTESLEWADVVV 320
Cdd:PRK10565  246 RPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEWADVVV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 321 IGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLHCAKRLVQRY 400
Cdd:PRK10565  326 IGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 401 GGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGM 480
Cdd:PRK10565  406 GGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGM 485

                         490       500
                  ....*....|....*....|...
gi 1447699868 481 LATDLFSTLQRIVNPEVTDKNHD 503
Cdd:PRK10565  486 LATDLFSTLQRIVNPEVIDKNHD 508
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 1-503 0e+00

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 1013.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868   1 MKKNPVSIPHTVWHADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVARLAKA 80
Cdd:PRK10565    6 MKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  81 VGIEVTLLAQESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVALIVDALLGTGLQQAPRESISQLIDHANSHPAPIV 160
Cdd:PRK10565   86 AGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 161 AVDIPSGLLAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSHWLKPR 240
Cdd:PRK10565  166 ALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 241 RPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLTESLEWADVVV 320
Cdd:PRK10565  246 RPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEWADVVV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 321 IGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLHCAKRLVQRY 400
Cdd:PRK10565  326 IGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 401 GGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGM 480
Cdd:PRK10565  406 GGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGM 485

                         490       500
                  ....*....|....*....|...
gi 1447699868 481 LATDLFSTLQRIVNPEVTDKNHD 503
Cdd:PRK10565  486 LATDLFSTLQRIVNPEVIDKNHD 508
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 226-495 5.01e-123

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: 360.93  E-value: 5.01e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 226 QRFSAEQLSHWLKPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHEL- 304
Cdd:TIGR00196   1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLm 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 305 -TMDSLTESLEWADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGcsVA 383
Cdd:TIGR00196  81 wKVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 384 EIESDRLHCAKRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVA 463
Cdd:TIGR00196 159 EIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFA 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1447699868 464 HGAAADVLAARFGTRGMLATDLFSTLQRIVNP 495
Cdd:TIGR00196 239 HGLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 224-495 1.98e-114

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: 339.41  E-value: 1.98e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 224 KIQRFSAEQLSHWLKPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHE 303
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 304 L-TMDSLTESLEWADVVVIGPGLGQQEWGKKALQKV-ENFRKPMLWDADALNLLAINPD----KRHNRVITPHPGEAARL 377
Cdd:COG0063    81 LpEEDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 378 LGCSVAEIESDRLHCAKRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAA 457
Cdd:COG0063   161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1447699868 458 CAGCVAHGAAADVLAARFGtRGMLATDLFSTLQRIVNP 495
Cdd:COG0063   241 AAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 242-485 3.91e-98

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: 296.45  E-value: 3.91e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 242 PTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDS---LTESLEWADV 318
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 319 VVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRH---NRVITPHPGEAARLLGCSVAEIESDRLHCAKR 395
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 396 LVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 475
Cdd:cd01171   161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240

                         250
                  ....*....|
gi 1447699868 476 GTRGMLATDL 485
Cdd:cd01171   241 GAGLTAADLV 250
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 252-491 6.55e-97

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: 293.12  E-value: 6.55e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 252 LVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLT-ESLEWADVVVIGPGLGQQEW 330
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 331 GKKALQKVENFRKPMLWDADALNLLAIN---PDKRHNRVITPHPGEAARLLGCSVAeIESDRLHCAKRLVQRYGGVAVLK 407
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 408 GAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGtRGMLATDLFS 487
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238


                  ....
gi 1447699868 488 TLQR 491
Cdd:pfam01256 239 IIPR 242
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 1-503 0e+00

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 1013.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868   1 MKKNPVSIPHTVWHADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVARLAKA 80
Cdd:PRK10565    6 MKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  81 VGIEVTLLAQESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVALIVDALLGTGLQQAPRESISQLIDHANSHPAPIV 160
Cdd:PRK10565   86 AGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 161 AVDIPSGLLAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSHWLKPR 240
Cdd:PRK10565  166 ALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 241 RPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLTESLEWADVVV 320
Cdd:PRK10565  246 RPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEWADVVV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 321 IGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLHCAKRLVQRY 400
Cdd:PRK10565  326 IGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 401 GGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGM 480
Cdd:PRK10565  406 GGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGM 485

                         490       500
                  ....*....|....*....|...
gi 1447699868 481 LATDLFSTLQRIVNPEVTDKNHD 503
Cdd:PRK10565  486 LATDLFSTLQRIVNPEVIDKNHD 508
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 226-495 5.01e-123

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: 360.93  E-value: 5.01e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 226 QRFSAEQLSHWLKPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHEL- 304
Cdd:TIGR00196   1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLm 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 305 -TMDSLTESLEWADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGcsVA 383
Cdd:TIGR00196  81 wKVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 384 EIESDRLHCAKRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVA 463
Cdd:TIGR00196 159 EIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFA 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1447699868 464 HGAAADVLAARFGTRGMLATDLFSTLQRIVNP 495
Cdd:TIGR00196 239 HGLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 224-495 1.98e-114

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: 339.41  E-value: 1.98e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 224 KIQRFSAEQLSHWLKPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHE 303
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 304 L-TMDSLTESLEWADVVVIGPGLGQQEWGKKALQKV-ENFRKPMLWDADALNLLAINPD----KRHNRVITPHPGEAARL 377
Cdd:COG0063    81 LpEEDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 378 LGCSVAEIESDRLHCAKRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAA 457
Cdd:COG0063   161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1447699868 458 CAGCVAHGAAADVLAARFGtRGMLATDLFSTLQRIVNP 495
Cdd:COG0063   241 AAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 12-499 7.06e-111

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: 338.00  E-value: 7.06e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  12 VWHADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPD-ARHWLVLCGHGNNGGDGYVVARLAKAVGIEVTLLAQ 90
Cdd:COG0062     3 LLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSaARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  91 ESDKPLPEEAALAREAWLNAGGEIH--ASNIVWPESVALIVDALLGTGLQQAPRESISQLIDHANSHPAPIVAVDIPSGL 168
Cdd:COG0062    83 GDPEKLSGDAAANLERLKAAGIPILelDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 169 LAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSHWLKPRRPTSHKGD 248
Cdd:COG0062   163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHKGG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 249 HGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTmDSLTESLEWADVVVIGPGLGQQ 328
Cdd:COG0062   243 GGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALD-DDEELLLLLAAAVVVAGGGGGG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 329 EWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLHCAKRLVQRYGGVAVLKG 408
Cdd:COG0062   322 GGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVA 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 409 AGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGMLATDLFST 488
Cdd:COG0062   402 AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAA 481

                         490
                  ....*....|.
gi 1447699868 489 LQRIVNPEVTD 499
Cdd:COG0062   482 AAALIALLLAA 492
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 242-485 3.91e-98

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: 296.45  E-value: 3.91e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 242 PTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDS---LTESLEWADV 318
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 319 VVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRH---NRVITPHPGEAARLLGCSVAEIESDRLHCAKR 395
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 396 LVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 475
Cdd:cd01171   161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240

                         250
                  ....*....|
gi 1447699868 476 GTRGMLATDL 485
Cdd:cd01171   241 GAGLTAADLV 250
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 252-491 6.55e-97

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: 293.12  E-value: 6.55e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 252 LVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLT-ESLEWADVVVIGPGLGQQEW 330
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 331 GKKALQKVENFRKPMLWDADALNLLAIN---PDKRHNRVITPHPGEAARLLGCSVAeIESDRLHCAKRLVQRYGGVAVLK 407
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 408 GAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGtRGMLATDLFS 487
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238


                  ....
gi 1447699868 488 TLQR 491
Cdd:pfam01256 239 IIPR 242
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 11-216 1.35e-91

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: 278.14  E-value: 1.35e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  11 TVWHADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVARLAKAVGIEVTLLAQ 90
Cdd:TIGR00197   1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  91 ESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVALIVDALLGTGLQQAPRESISQLIDHANSHPAPIVAVDIPSGLLA 170
Cdd:TIGR00197  81 EKRIECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1447699868 171 ETGATPGAVINADHTITFIALKPGLLTGKArDVTGQLHFDSLGLDS 216
Cdd:TIGR00197 161 DTGAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIPP 205
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 34-194 1.50e-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: 1.50e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  34 YELMLRAGEAAFQV-CRSAYPDARHWLVLCGHGNNGGDGYVVARLAKAVGIEVTLLAQESDKPLPEEAALAREAWLNAGG 112
Cdd:pfam03853   2 AVLMENAGRAAARVlKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 113 EIHASNIV-----WPESVALIVDALLGTGLQQAPRESISQLIDHANSHPAPIVAVDIPSGLLAETGATPGAVINADHTIT 187
Cdd:pfam03853  82 KIVTDNPDedlekLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVT 161


                  ....*..
gi 1447699868 188 FIALKPG 194
Cdd:pfam03853 162 FGAPKPG 168
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 30-205 2.65e-16

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 78.38  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  30 GLTLYELMLRAG----EAAFQVCRSAYPDA-----RHWLVLCGHGNNGGDGYVVARLAKAVGIEVTLL-AQESDKPLPEE 99
Cdd:PLN03050   26 GFSLEQLMELAGlsvaEAVYEVADGEKASNppgrhPRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCyPKQSSKPHYEN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 100 -----AALAREAWLNAGGEIhASNIVWPESVALIVDALLGTGLQQAPRES----ISQLIDHANShPAPIVAVDIPSGLLA 170
Cdd:PLN03050  106 lvtqcEDLGIPFVQAIGGTN-DSSKPLETTYDVIVDAIFGFSFHGAPRAPfdtlLAQMVQQQKS-PPPIVSVDVPSGWDV 183

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1447699868 171 ETGATPGAVINADHTITFIALKPGLLTGKARDVTG 205
Cdd:PLN03050  184 DEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 29-209 4.27e-14

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 74.50  E-value: 4.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  29 LGLTLYELMLRAGEAAFQVCRSAYPDARHW--LVLCGHGNNGGDGYVVARLAKAVGIEVTLL-AQESDKPL-------PE 98
Cdd:PLN03049   31 LGFSVDQLMELAGLSVASAIAEVYSPSEYRrvLALCGPGNNGGDGLVAARHLHHFGYKPSICyPKRTDKPLynglvtqLE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  99 EAALAREAWLNAGGEIhasnivwPESVALIVDALLGTGLQQAPRESISQLIDH--ANSHPAPIVAVDIPSGLLAETGATP 176
Cdd:PLN03049  111 SLSVPFLSVEDLPSDL-------SSQFDIVVDAMFGFSFHGAPRPPFDDLIQKlvRAAGPPPIVSVDIPSGWHVEEGDVN 183

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1447699868 177 GAVINADHTITFIALKPGlltgkARDVTGQLHF 209
Cdd:PLN03049  184 GEGLKPDMLVSLTAPKLC-----AKMFKGPHHF 211
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 22-209 6.39e-10

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 61.49  E-value: 6.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  22 EREAAD-------ALGLTLYELMLRAGEAAFQVCRSAYPDARH--WLVLCGHGNNGGDGYVVARLAKAVGIEVTL-LAQE 91
Cdd:PLN02918   93 QREAAEidetlmgPLGFSVDQLMELAGLSVAASIAEVYKPGEYsrVLAICGPGNNGGDGLVAARHLHHFGYKPFVcYPKR 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868  92 SDKPLPEEAALAREA----WLNAggEIHASNIvwPESVALIVDALLGTGLQQAPRESISQLI---------DHANSHPAp 158
Cdd:PLN02918  173 TAKPLYTGLVTQLESlsvpFVSV--EDLPADL--SKDFDIIVDAMFGFSFHGAPRPPFDDLIrrlvslqnyEQTLKHPV- 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1447699868 159 IVAVDIPSGLLAETGATPGAVINADHTITFIAlkPGLLtgkARDVTGQLHF 209
Cdd:PLN02918  248 IVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTA--PKLC---AKKFRGPHHF 293
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 381-474 2.76e-06

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: 48.69  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 381 SVAEIESDRLHCAKRLVQRYGGVAVLKGAGTVVAaHPDALGIIDAGNAGMAS-GGMGDVLSGIIGALLGQKLSPYDAACA 459
Cdd:cd01170   133 SSSSDEEDALELAKALARKYGAVVVVTGEVDYIT-DGERVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVS 211

                          90
                  ....*....|....*
gi 1447699868 460 GCVAHGAAADVLAAR 474
Cdd:cd01170   212 AVLVYGIAGELAAER 226
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 372-474 1.07e-04

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 44.02  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699868 372 GEAARLLGCSVAEIESDRLHCAKRLVQRYGGVAVLKGAGTVVAaHPDALGIIDAGNAGMAS-GGMGDVLSGIIGALLGQK 450
Cdd:PRK09355  128 GEAAETKGVDSTDGSADAVEIAKAAAKKYGTVVVVTGEVDYIT-DGERVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVE 206

                          90       100
                  ....*....|....*....|....
gi 1447699868 451 LSPYDAACAGCVAHGAAADvLAAR 474
Cdd:PRK09355  207 KDYLEAAAAACAVYGIAGE-LAAE 229
 
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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