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Conserved domains on  [gi|1073970376|gb|AOV10090|]
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bifunctional ADP-dependent (S)-NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase [Klebsiella sp. LTGPAF-6F]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 1-508 0e+00

putative carbohydrate kinase; Provisional


:

Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 973.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376   1 MMDHTMTKNTGSIPHIIWSAEALRRAEKEAADTLGLTLYELMRRAGEAAFELARVQYPESRHWLILCGHGNNGGDGYVVA 80
Cdd:PRK10565    1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  81 RLAQSRGIQVTLLALESEKPLPEEASLAREEWLNAGGTIHAASIPWPEDITLIIDGLLGTGLQSAPRENVAALIARANAH 160
Cdd:PRK10565   81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 161 PAAVVALDIPSGLNAQTGTTPGAVIHAAHTITFIALKPGLLTGKARDVVGRLHHHALGLEGWLAGQTTALSRFDASQLPG 240
Cdd:PRK10565  161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 241 WLPPRRPTSHKGDHGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHELTSRSLEESLHW 320
Cdd:PRK10565  241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 321 ADVIAIGPGLGQGEWGKNALRQAENFRKPMVWDADALNLLAINPDKRHNRVLTPHPGEAARLLNVSVAEIESDRLHSAQR 400
Cdd:PRK10565  321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 401 LVKRYGGIVVLKGAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAHGEAADRLAARH 480
Cdd:PRK10565  401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480

                         490       500
                  ....*....|....*....|....*...
gi 1073970376 481 GTRGMLATDLFFTLRRVVNPDVIDVDHD 508
Cdd:PRK10565  481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 1-508 0e+00

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 973.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376   1 MMDHTMTKNTGSIPHIIWSAEALRRAEKEAADTLGLTLYELMRRAGEAAFELARVQYPESRHWLILCGHGNNGGDGYVVA 80
Cdd:PRK10565    1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  81 RLAQSRGIQVTLLALESEKPLPEEASLAREEWLNAGGTIHAASIPWPEDITLIIDGLLGTGLQSAPRENVAALIARANAH 160
Cdd:PRK10565   81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 161 PAAVVALDIPSGLNAQTGTTPGAVIHAAHTITFIALKPGLLTGKARDVVGRLHHHALGLEGWLAGQTTALSRFDASQLPG 240
Cdd:PRK10565  161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 241 WLPPRRPTSHKGDHGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHELTSRSLEESLHW 320
Cdd:PRK10565  241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 321 ADVIAIGPGLGQGEWGKNALRQAENFRKPMVWDADALNLLAINPDKRHNRVLTPHPGEAARLLNVSVAEIESDRLHSAQR 400
Cdd:PRK10565  321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 401 LVKRYGGIVVLKGAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAHGEAADRLAARH 480
Cdd:PRK10565  401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480

                         490       500
                  ....*....|....*....|....*...
gi 1073970376 481 GTRGMLATDLFFTLRRVVNPDVIDVDHD 508
Cdd:PRK10565  481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 229-500 2.50e-117

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: 346.72  E-value: 2.50e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 229 ALSRFDASQLPGWLPPRRPTSHKGDHGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHE 308
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 309 LTS-RSLEESLHWADVIAIGPGLGQGEWGKNALRQA-ENFRKPMVWDADALNLLAINPD----KRHNRVLTPHPGEAARL 382
Cdd:COG0063    81 LPEeDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 383 LNVSVAEIESDRLHSAQRLVKRYGGIVVLKGAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAA 462
Cdd:COG0063   161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1073970376 463 CAGCVAHGEAADRLAARHGtRGMLATDLFFTLRRVVNP 500
Cdd:COG0063   241 AAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 232-500 8.52e-106

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: 316.63  E-value: 8.52e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 232 RFDASQLPGWLPPRRPTSHKGDHGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHEL-- 309
Cdd:TIGR00196   2 TFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmw 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 310 TSRSLEESLHWADVIAIGPGLGQGEWGKNALRQAENFRKPMVWDADALNLLAINPDKRHNRVLTPHPGEAARLLNVSvaE 389
Cdd:TIGR00196  82 KVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLGVN--E 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 390 IESDRLHSAQRLVKRYGGIVVLKGAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAH 469
Cdd:TIGR00196 160 IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAH 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1073970376 470 GEAADRLAARHGTRGMLATDLFFTLRRVVNP 500
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 247-490 4.06e-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: 4.06e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 247 PTSHKGDHGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHELTSRS---LEESLHWADV 323
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 324 IAIGPGLGQGEWGKNALRQAENFRKPMVWDADALNLLAINPDKRH---NRVLTPHPGEAARLLNVSVAEIESDRLHSAQR 400
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 401 LVKRYGGIVVLKGAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAHGEAADRLAARH 480
Cdd:cd01171   161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240

                         250
                  ....*....|
gi 1073970376 481 GTRGMLATDL 490
Cdd:cd01171   241 GAGLTAADLV 250
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 257-496 9.75e-86

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: 264.23  E-value: 9.75e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 257 LVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHELTSRSLE-ESLHWADVIAIGPGLGQGEW 335
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 336 GKNALRQAENFRKPMVWDADALNLLAIN---PDKRHNRVLTPHPGEAARLLNVSVAeIESDRLHSAQRLVKRYGGIVVLK 412
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 413 GAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAHGEAADRLAARHGtRGMLATDLFF 492
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238


                  ....
gi 1073970376 493 TLRR 496
Cdd:pfam01256 239 IIPR 242
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 1-508 0e+00

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 973.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376   1 MMDHTMTKNTGSIPHIIWSAEALRRAEKEAADTLGLTLYELMRRAGEAAFELARVQYPESRHWLILCGHGNNGGDGYVVA 80
Cdd:PRK10565    1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  81 RLAQSRGIQVTLLALESEKPLPEEASLAREEWLNAGGTIHAASIPWPEDITLIIDGLLGTGLQSAPRENVAALIARANAH 160
Cdd:PRK10565   81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 161 PAAVVALDIPSGLNAQTGTTPGAVIHAAHTITFIALKPGLLTGKARDVVGRLHHHALGLEGWLAGQTTALSRFDASQLPG 240
Cdd:PRK10565  161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 241 WLPPRRPTSHKGDHGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHELTSRSLEESLHW 320
Cdd:PRK10565  241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 321 ADVIAIGPGLGQGEWGKNALRQAENFRKPMVWDADALNLLAINPDKRHNRVLTPHPGEAARLLNVSVAEIESDRLHSAQR 400
Cdd:PRK10565  321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 401 LVKRYGGIVVLKGAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAHGEAADRLAARH 480
Cdd:PRK10565  401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480

                         490       500
                  ....*....|....*....|....*...
gi 1073970376 481 GTRGMLATDLFFTLRRVVNPDVIDVDHD 508
Cdd:PRK10565  481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 229-500 2.50e-117

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: 346.72  E-value: 2.50e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 229 ALSRFDASQLPGWLPPRRPTSHKGDHGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHE 308
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 309 LTS-RSLEESLHWADVIAIGPGLGQGEWGKNALRQA-ENFRKPMVWDADALNLLAINPD----KRHNRVLTPHPGEAARL 382
Cdd:COG0063    81 LPEeDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 383 LNVSVAEIESDRLHSAQRLVKRYGGIVVLKGAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAA 462
Cdd:COG0063   161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1073970376 463 CAGCVAHGEAADRLAARHGtRGMLATDLFFTLRRVVNP 500
Cdd:COG0063   241 AAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 17-508 8.83e-108

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: 330.29  E-value: 8.83e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  17 IWSAEALRRAEKEAADTLGLTLYELMRRAGEAAFELARVQYP-ESRHWLILCGHGNNGGDGYVVARLAQSRGIQVTLLAL 95
Cdd:COG0062     3 LLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  96 ESEKPLPEEASLAREEWLNAGGTIH--AASIPWPEDITLIIDGLLGTGLQSAPRENVAALIARANAHPAAVVALDIPSGL 173
Cdd:COG0062    83 GDPEKLSGDAAANLERLKAAGIPILelDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 174 NAQTGTTPGAVIHAAHTITFIALKPGLLTGKARDVVGRLHHHALGLEGWLAGQTTALSRFDASQLPGWLPPRRPTSHKGD 253
Cdd:COG0062   163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHKGG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 254 HGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHELTSrSLEESLHWADVIAIGPGLGQG 333
Cdd:COG0062   243 GGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDD-DEELLLLLAAAVVVAGGGGGG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 334 EWGKNALRQAENFRKPMVWDADALNLLAINPDKRHNRVLTPHPGEAARLLNVSVAEIESDRLHSAQRLVKRYGGIVVLKG 413
Cdd:COG0062   322 GGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVA 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 414 AGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAHGEAADRLAARHGTRGMLATDLFFT 493
Cdd:COG0062   402 AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAA 481

                         490
                  ....*....|....*
gi 1073970376 494 LRRVVNPDVIDVDHD 508
Cdd:COG0062   482 AAALIALLLAAALLL 496
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 232-500 8.52e-106

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: 316.63  E-value: 8.52e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 232 RFDASQLPGWLPPRRPTSHKGDHGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHEL-- 309
Cdd:TIGR00196   2 TFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmw 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 310 TSRSLEESLHWADVIAIGPGLGQGEWGKNALRQAENFRKPMVWDADALNLLAINPDKRHNRVLTPHPGEAARLLNVSvaE 389
Cdd:TIGR00196  82 KVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLGVN--E 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 390 IESDRLHSAQRLVKRYGGIVVLKGAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAH 469
Cdd:TIGR00196 160 IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAH 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1073970376 470 GEAADRLAARHGTRGMLATDLFFTLRRVVNP 500
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 247-490 4.06e-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: 4.06e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 247 PTSHKGDHGKLVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHELTSRS---LEESLHWADV 323
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 324 IAIGPGLGQGEWGKNALRQAENFRKPMVWDADALNLLAINPDKRH---NRVLTPHPGEAARLLNVSVAEIESDRLHSAQR 400
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 401 LVKRYGGIVVLKGAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAHGEAADRLAARH 480
Cdd:cd01171   161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240

                         250
                  ....*....|
gi 1073970376 481 GTRGMLATDL 490
Cdd:cd01171   241 GAGLTAADLV 250
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 257-496 9.75e-86

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: 264.23  E-value: 9.75e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 257 LVIIGGEPGTAGAIRMSGEAALRAGAGLVRVLTHRDNIAPILTARPELMVHELTSRSLE-ESLHWADVIAIGPGLGQGEW 335
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 336 GKNALRQAENFRKPMVWDADALNLLAIN---PDKRHNRVLTPHPGEAARLLNVSVAeIESDRLHSAQRLVKRYGGIVVLK 412
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 413 GAGTIVASETGEMAIIDAGNAGMASGGMGDVLTGIVAALLGQRLTPYDAACAGCVAHGEAADRLAARHGtRGMLATDLFF 492
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238


                  ....
gi 1073970376 493 TLRR 496
Cdd:pfam01256 239 IIPR 242
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 18-219 4.12e-68

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: 217.28  E-value: 4.12e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  18 WSAEALRRAEKEAADTLGLTLYELMRRAGEAAFELARVQYPESRHWLILCGHGNNGGDGYVVARLAQSRGIQVTLLALES 97
Cdd:TIGR00197   3 VVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  98 EKPLPEEASLAREEWLNAGGTIHAASIPWPEDITLIIDGLLGTGLQSAPRENVAALIARANAHPAAVVALDIPSGLNAQT 177
Cdd:TIGR00197  83 RIECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDT 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1073970376 178 GTTPGAVIHAAHTITFIALKPGLLTGKArDVVGRLHHHALGL 219
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 ...
 39-199 1.25e-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: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  39 YELMRRAGEAAFELARVQY-PESRHWLILCGHGNNGGDGYVVARLAQSRGIQVTLLALESEKPLPEEASLAREEWLNAGG 117
Cdd:pfam03853   2 AVLMENAGRAAARVLKALLsPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 118 TIHAAS-----IPWPEDITLIIDGLLGTGLQSAPRENVAALIARANAHPAAVVALDIPSGLNAQTGTTPGAVIHAAHTIT 192
Cdd:pfam03853  82 KIVTDNpdedlEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVT 161


                  ....*..
gi 1073970376 193 FIALKPG 199
Cdd:pfam03853 162 FGAPKPG 168
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 19-210 4.26e-16

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 77.99  E-value: 4.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  19 SAEALRRAEKEAADTLGLTLYELMRRAG----EAAFELARVQYPES-----RHWLILCGHGNNGGDGYVVARLAQSRGIQ 89
Cdd:PLN03050   10 NAQDAAALDEELMSTPGFSLEQLMELAGlsvaEAVYEVADGEKASNppgrhPRVLLVCGPGNNGGDGLVAARHLAHFGYE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  90 VTLL-ALESEKPLPEE-----ASLAREEWLNAGGTihaASIPWPEDIT--LIIDGLLGTGLQSAPRENVAALIA---RAN 158
Cdd:PLN03050   90 VTVCyPKQSSKPHYENlvtqcEDLGIPFVQAIGGT---NDSSKPLETTydVIVDAIFGFSFHGAPRAPFDTLLAqmvQQQ 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1073970376 159 AHPAAVVALDIPSGLNAQTGTTPGAVIHAAHTITFIALKPGLLTGKARDVVG 210
Cdd:PLN03050  167 KSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 34-197 9.62e-13

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 70.26  E-value: 9.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  34 LGLTLYELMRRAG-EAAFELARVqYPESRHW--LILCGHGNNGGDGYVVARLAQSRGIQVTLL-ALESEKPLPEeaSLAR 109
Cdd:PLN03049   31 LGFSVDQLMELAGlSVASAIAEV-YSPSEYRrvLALCGPGNNGGDGLVAARHLHHFGYKPSICyPKRTDKPLYN--GLVT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 110 EewlnaggtIHAASIPW----------PEDITLIIDGLLGTGLQSAPRENVAALIAR--ANAHPAAVVALDIPSGLNAQT 177
Cdd:PLN03049  108 Q--------LESLSVPFlsvedlpsdlSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKlvRAAGPPPIVSVDIPSGWHVEE 179

                         170       180
                  ....*....|....*....|
gi 1073970376 178 GTTPGAVIHAAHTITFIALK 197
Cdd:PLN03049  180 GDVNGEGLKPDMLVSLTAPK 199
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 26-218 3.13e-09

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 59.18  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  26 AEKEAADT-------LGLTLYELMRRAG-EAAFELARVQYP-ESRHWLILCGHGNNGGDGYVVARLAQSRGIQvTLLALE 96
Cdd:PLN02918   92 TQREAAEIdetlmgpLGFSVDQLMELAGlSVAASIAEVYKPgEYSRVLAICGPGNNGGDGLVAARHLHHFGYK-PFVCYP 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376  97 SEKPLPEEASLAREewlnaggtIHAASIPW------PEDIT----LIIDGLLGTGLQSAPRENVAALIAR---------A 157
Cdd:PLN02918  171 KRTAKPLYTGLVTQ--------LESLSVPFvsvedlPADLSkdfdIIVDAMFGFSFHGAPRPPFDDLIRRlvslqnyeqT 242

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1073970376 158 NAHPaAVVALDIPSGLNAQTGTTPGAVIHAAHTITFIAlkPGLLTGKARDvvgrlHHHALG 218
Cdd:PLN02918  243 LKHP-VIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTA--PKLCAKKFRG-----PHHFLG 295
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 385-479 5.19e-08

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: 53.70  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 385 VSVAEIESDRLHSAQRLVKRYGGIVVLKGAGTIVASETgEMAIIDAGNAGMAS-GGMGDVLTGIVAALLGQRLTPYDAAC 463
Cdd:cd01170   132 DSSSSDEEDALELAKALARKYGAVVVVTGEVDYITDGE-RVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAV 210

                          90
                  ....*....|....*.
gi 1073970376 464 AGCVAHGEAADRLAAR 479
Cdd:cd01170   211 SAVLVYGIAGELAAER 226
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 377-479 4.70e-06

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 48.26  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073970376 377 GEAARLLNVSVAEIESDRLHSAQRLVKRYGGIVVLKGAGTIVaSETGEMAIIDAGNAGMAS-GGMGDVLTGIVAALLGQR 455
Cdd:PRK09355  128 GEAAETKGVDSTDGSADAVEIAKAAAKKYGTVVVVTGEVDYI-TDGERVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVE 206

                          90       100
                  ....*....|....*....|....
gi 1073970376 456 LTPYDAACAGCVAHGEAADRLAAR 479
Cdd:PRK09355  207 KDYLEAAAAACAVYGIAGELAAER 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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