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Conserved domains on  [gi|2074133566|gb|QYC38522|]
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Bifunctional NAD(P)H-hydrate repair enzyme Nnr [Nonomuraea coxensis DSM 45129]

Protein Classification

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase( domain architecture ID 11145907)

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
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 207-480 6.69e-88

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: 270.46  E-value: 6.69e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 207 DVAALTGGDVDDLLPRPGKESDKYRRGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEAVITL 286
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 287 LDRPS--IKDVGRVQAWVLGPGLGTGDWAHELAAQVLG-TGLPVLVDADGLTVVARDRSLLR-RAAPTLITPHAGELARL 362
Cdd:COG0063    81 LPEEDelLELLERADAVVIGPGLGRDEETRELLRALLEaADKPLVLDADALNLLAEDPELLAaLPAPTVLTPHPGEFARL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 363 IRAERADIEAARLQHARAAAAELGVTVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAG 442
Cdd:COG0063   161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2074133566 443 SCAAYLHGLAGRLAADGAPL--AAADVATALPAAFRAVAA 480
Cdd:COG0063   241 AAGVYLHGLAGDLAAEERGRglLASDLIEALPAALRELLE 280
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 45-179 1.74e-36

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: 132.35  E-value: 1.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  45 VYGSRVVLLVGSGDNGGDALYAGERLARRGARVEAILAGSRAHEAGLAA-----LLRAGGRV-------AGPGALTRADL 112
Cdd:pfam03853  22 PAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARrqldlFKKLGGKIvtdnpdeDLEKLLSPVDL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074133566 113 IMDGLVGIGVSGALREPYAGLAEEANAARAPVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVKTG 179
Cdd:pfam03853 102 IIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 207-480 6.69e-88

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: 270.46  E-value: 6.69e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 207 DVAALTGGDVDDLLPRPGKESDKYRRGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEAVITL 286
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 287 LDRPS--IKDVGRVQAWVLGPGLGTGDWAHELAAQVLG-TGLPVLVDADGLTVVARDRSLLR-RAAPTLITPHAGELARL 362
Cdd:COG0063    81 LPEEDelLELLERADAVVIGPGLGRDEETRELLRALLEaADKPLVLDADALNLLAEDPELLAaLPAPTVLTPHPGEFARL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 363 IRAERADIEAARLQHARAAAAELGVTVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAG 442
Cdd:COG0063   161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2074133566 443 SCAAYLHGLAGRLAADGAPL--AAADVATALPAAFRAVAA 480
Cdd:COG0063   241 AAGVYLHGLAGDLAAEERGRglLASDLIEALPAALRELLE 280
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 225-454 6.88e-78

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: 243.67  E-value: 6.88e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 225 KESDKYRRGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEAVITLLDRPSI----KDVGRVQA 300
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIeellELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 301 WVLGPGLGTGDWAHELAAQVLGTGLPVLVDADGLTVVARDRSLLRRAAPTLITPHAGELARLIRAERADIEAARLQHARA 380
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2074133566 381 AAAELGVTVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAGSCAAYLHGLAGR 454
Cdd:cd01171   161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGD 234
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 52-452 7.53e-63

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 212.61  E-value: 7.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  52 LLVGSGDNGGDAlYAGERLARR-GARVEAI-LAGSRA--HEAGLA--ALLRAGGRVAGPGAL--TRADLIMDGLVGIGVS 123
Cdd:PRK10565   65 VLCGHGNNGGDG-YVVARLAQAaGIDVTLLaQESDKPlpEEAALAreAWLNAGGEIHAADIVwpESVDLIVDALLGTGLR 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 124 GALREPYAGLAEEANAARAPVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVKTGLLVDPGAGHAGRVELVDIGLGPCL 203
Cdd:PRK10565  144 QAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWL 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 204 P--DPDVAALTGGDVDDLLP--RPGkeSDKYRRGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAW 279
Cdd:PRK10565  224 AgqEAPIQRFDAEQLSQWLKprRPT--SHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTAR 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 280 PEAVITLLDRPSIKD-VGRVQAWVLGPGLGTGDWAHELAAQVLGTGLPVLVDADGLTVVA--RDRSLLRraaptLITPHA 356
Cdd:PRK10565  302 PELMVHELTPDSLEEsLEWADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAinPDKRHNR-----VITPHP 376

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 357 GELARLIRAERADIEAARLQHARAAAAELGVTVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGL 436
Cdd:PRK10565  377 GEAARLLGCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKL 456

                         410
                  ....*....|....*.
gi 2074133566 437 GAYDAGSCAAYLHGLA 452
Cdd:PRK10565  457 SPYDAACAGCVAHGAA 472
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 235-454 9.18e-54

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: 180.64  E-value: 9.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 235 LGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEAVITLLDRPS--IKDVGRVQAWVLGPGLGTGDW 312
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSsiLEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 313 AHELAAQVLGTGLPVLVDADGLTVVARDRSLLRRAAPTLITPHAGELARLIRAERAdIEAARLQHARAAAAELGVTVLLK 392
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINNEKPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2074133566 393 GSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAGSCAAYLHGLAGR 454
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASD 221
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 214-453 1.31e-43

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: 154.85  E-value: 1.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 214 GDVDDLLPRPgKESDKYRRGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEavitLLDRPSIK 293
Cdd:TIGR00196   7 GDLLTLPLRD-PNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPE----LIVHRLMW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 294 DVG-------RVQAWVLGPGLGTGDWAHELAAQVLGTGLPVLVDADGLTVVARDRSllrRAAPTLITPHAGELARLIRAE 366
Cdd:TIGR00196  82 KVDedeelleRYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQK---REGEVILTPHPGEFKRLLGVN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 367 RadIEAARLQHARAAAAELGVTVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAGSCAA 446
Cdd:TIGR00196 159 E--IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAA 236


                  ....*..
gi 2074133566 447 YLHGLAG 453
Cdd:TIGR00196 237 FAHGLAG 243
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 45-179 1.74e-36

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: 132.35  E-value: 1.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  45 VYGSRVVLLVGSGDNGGDALYAGERLARRGARVEAILAGSRAHEAGLAA-----LLRAGGRV-------AGPGALTRADL 112
Cdd:pfam03853  22 PAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARrqldlFKKLGGKIvtdnpdeDLEKLLSPVDL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074133566 113 IMDGLVGIGVSGALREPYAGLAEEANAARAPVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVKTG 179
Cdd:pfam03853 102 IIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 45-201 9.87e-28

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: 109.81  E-value: 9.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  45 VYGSRVVLLVGSGDNGGDALYAGERLARRGARVEAILAGSRAHEAGLAALLRAGGRVAGPG-------ALTRADLIMDGL 117
Cdd:TIGR00197  43 PLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRIECTEQAEVNLKALKVGGISidegnlvKPEDCDVIIDAI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 118 VGIGVSGALREPYAGLAEEANAARAPVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVKTGLLVDPgAGHAGRVELVDI 197
Cdd:TIGR00197 123 LGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDR-ADVTGELKVGGI 201


                  ....
gi 2074133566 198 GLGP 201
Cdd:TIGR00197 202 GIPP 205
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 48-179 1.13e-14

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 73.76  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  48 SRVVLLVGSGDNGGDALYAGERLARRGARVEAILA--GSRAHEAGLAA----------LLRAGGRVAGPGALTRADLIMD 115
Cdd:PLN03050   61 PRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPkqSSKPHYENLVTqcedlgipfvQAIGGTNDSSKPLETTYDVIVD 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074133566 116 GLVGIGVSGALREPYAGLAEEANAARA---PVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVKTG 179
Cdd:PLN03050  141 AIFGFSFHGAPRAPFDTLLAQMVQQQKsppPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLS 207
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 207-480 6.69e-88

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: 270.46  E-value: 6.69e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 207 DVAALTGGDVDDLLPRPGKESDKYRRGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEAVITL 286
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 287 LDRPS--IKDVGRVQAWVLGPGLGTGDWAHELAAQVLG-TGLPVLVDADGLTVVARDRSLLR-RAAPTLITPHAGELARL 362
Cdd:COG0063    81 LPEEDelLELLERADAVVIGPGLGRDEETRELLRALLEaADKPLVLDADALNLLAEDPELLAaLPAPTVLTPHPGEFARL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 363 IRAERADIEAARLQHARAAAAELGVTVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAG 442
Cdd:COG0063   161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2074133566 443 SCAAYLHGLAGRLAADGAPL--AAADVATALPAAFRAVAA 480
Cdd:COG0063   241 AAGVYLHGLAGDLAAEERGRglLASDLIEALPAALRELLE 280
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 225-454 6.88e-78

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: 243.67  E-value: 6.88e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 225 KESDKYRRGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEAVITLLDRPSI----KDVGRVQA 300
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIeellELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 301 WVLGPGLGTGDWAHELAAQVLGTGLPVLVDADGLTVVARDRSLLRRAAPTLITPHAGELARLIRAERADIEAARLQHARA 380
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2074133566 381 AAAELGVTVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAGSCAAYLHGLAGR 454
Cdd:cd01171   161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGD 234
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 52-452 7.53e-63

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 212.61  E-value: 7.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  52 LLVGSGDNGGDAlYAGERLARR-GARVEAI-LAGSRA--HEAGLA--ALLRAGGRVAGPGAL--TRADLIMDGLVGIGVS 123
Cdd:PRK10565   65 VLCGHGNNGGDG-YVVARLAQAaGIDVTLLaQESDKPlpEEAALAreAWLNAGGEIHAADIVwpESVDLIVDALLGTGLR 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 124 GALREPYAGLAEEANAARAPVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVKTGLLVDPGAGHAGRVELVDIGLGPCL 203
Cdd:PRK10565  144 QAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWL 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 204 P--DPDVAALTGGDVDDLLP--RPGkeSDKYRRGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAW 279
Cdd:PRK10565  224 AgqEAPIQRFDAEQLSQWLKprRPT--SHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTAR 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 280 PEAVITLLDRPSIKD-VGRVQAWVLGPGLGTGDWAHELAAQVLGTGLPVLVDADGLTVVA--RDRSLLRraaptLITPHA 356
Cdd:PRK10565  302 PELMVHELTPDSLEEsLEWADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAinPDKRHNR-----VITPHP 376

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 357 GELARLIRAERADIEAARLQHARAAAAELGVTVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGL 436
Cdd:PRK10565  377 GEAARLLGCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKL 456

                         410
                  ....*....|....*.
gi 2074133566 437 GAYDAGSCAAYLHGLA 452
Cdd:PRK10565  457 SPYDAACAGCVAHGAA 472
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 5-480 8.37e-55

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: 190.85  E-value: 8.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566   5 YTADQIRAAEHVLMA--GLPPGTLMQRAAAGLAAACAGLLgRVYGSRVVLLVGSGDNGGDALYAGERLARRGARVEAILA 82
Cdd:COG0062     4 LTAAQMRALDRAAIEalGIPGLVLMERAGRAVARAIRRRF-PSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  83 GSRAHEAGLAA-----LLRAGGRV----AGPGALTRADLIMDGLVGIGVSGALREPYAGLAEEANAARAPVVAVDVPSGV 153
Cdd:COG0062    83 GDPEKLSGDAAanlerLKAAGIPIleldDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 154 DASTGRVQGAAVRALVTVTMGAVKTGLLVDPGAGHAGRVELVDIGLGPCL--PDPDVAALTGGDVDDLLPRPGKESDKYR 231
Cdd:COG0062   163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAaaEAPAALLLLADLLALLLPPRRRSHHKGG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 232 RGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEAVITLLDRPSIKDVGRVQAWVLGPGLGTGD 311
Cdd:COG0062   243 GGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGGGG 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 312 WAHELAAQVLGTGLP----VLVDADGLTVVARDRSLLRRAAPTLITPHAGELARLIRAERADIEAARLQHARAAAAELGV 387
Cdd:COG0062   323 GGAGGGLLLLLLLLLlllvLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVAA 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 388 TVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAGSCAAYLHGLAGRLAADGAPLAAADV 467
Cdd:COG0062   403 AAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAAA 482

                         490
                  ....*....|...
gi 2074133566 468 ATALPAAFRAVAA 480
Cdd:COG0062   483 AALIALLLAAALL 495
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 235-454 9.18e-54

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: 180.64  E-value: 9.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 235 LGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEAVITLLDRPS--IKDVGRVQAWVLGPGLGTGDW 312
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSsiLEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 313 AHELAAQVLGTGLPVLVDADGLTVVARDRSLLRRAAPTLITPHAGELARLIRAERAdIEAARLQHARAAAAELGVTVLLK 392
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINNEKPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2074133566 393 GSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAGSCAAYLHGLAGR 454
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASD 221
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 214-453 1.31e-43

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: 154.85  E-value: 1.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 214 GDVDDLLPRPgKESDKYRRGVLGVLAGSDLYTGAAVLAVGGALRAGAGMVRYAGPAEPVAQVRAAWPEavitLLDRPSIK 293
Cdd:TIGR00196   7 GDLLTLPLRD-PNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPE----LIVHRLMW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 294 DVG-------RVQAWVLGPGLGTGDWAHELAAQVLGTGLPVLVDADGLTVVARDRSllrRAAPTLITPHAGELARLIRAE 366
Cdd:TIGR00196  82 KVDedeelleRYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQK---REGEVILTPHPGEFKRLLGVN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 367 RadIEAARLQHARAAAAELGVTVLLKGSTTVVAEEPRPVRVNPTGTSWLATGGTGDVLSGVAGALLAQGLGAYDAGSCAA 446
Cdd:TIGR00196 159 E--IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAA 236


                  ....*..
gi 2074133566 447 YLHGLAG 453
Cdd:TIGR00196 237 FAHGLAG 243
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 45-179 1.74e-36

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: 132.35  E-value: 1.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  45 VYGSRVVLLVGSGDNGGDALYAGERLARRGARVEAILAGSRAHEAGLAA-----LLRAGGRV-------AGPGALTRADL 112
Cdd:pfam03853  22 PAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARrqldlFKKLGGKIvtdnpdeDLEKLLSPVDL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074133566 113 IMDGLVGIGVSGALREPYAGLAEEANAARAPVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVKTG 179
Cdd:pfam03853 102 IIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 45-201 9.87e-28

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: 109.81  E-value: 9.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  45 VYGSRVVLLVGSGDNGGDALYAGERLARRGARVEAILAGSRAHEAGLAALLRAGGRVAGPG-------ALTRADLIMDGL 117
Cdd:TIGR00197  43 PLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRIECTEQAEVNLKALKVGGISidegnlvKPEDCDVIIDAI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 118 VGIGVSGALREPYAGLAEEANAARAPVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVKTGLLVDPgAGHAGRVELVDI 197
Cdd:TIGR00197 123 LGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDR-ADVTGELKVGGI 201


                  ....
gi 2074133566 198 GLGP 201
Cdd:TIGR00197 202 GIPP 205
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 48-179 1.13e-14

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 73.76  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  48 SRVVLLVGSGDNGGDALYAGERLARRGARVEAILA--GSRAHEAGLAA----------LLRAGGRVAGPGALTRADLIMD 115
Cdd:PLN03050   61 PRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPkqSSKPHYENLVTqcedlgipfvQAIGGTNDSSKPLETTYDVIVD 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074133566 116 GLVGIGVSGALREPYAGLAEEANAARA---PVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVKTG 179
Cdd:PLN03050  141 AIFGFSFHGAPRAPFDTLLAQMVQQQKsppPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLS 207
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 48-177 1.61e-07

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 53.70  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566  48 SRVVLLVGSGDNGGDALYAGERLARRGARVeAILAGSRAHEA---GLAALLRAGG----RVAG-PGAL-TRADLIMDGLV 118
Cdd:PLN03049   60 RRVLALCGPGNNGGDGLVAARHLHHFGYKP-SICYPKRTDKPlynGLVTQLESLSvpflSVEDlPSDLsSQFDIVVDAMF 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2074133566 119 GIGVSGALREPYAGLAEE--ANAARAPVVAVDVPSGVDASTGRVQGAAVRALVTVTMGAVK 177
Cdd:PLN03049  139 GFSFHGAPRPPFDDLIQKlvRAAGPPPIVSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPK 199
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 326-453 2.36e-05

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 45.95  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 326 PVLVDADGL-TVVARDrsLLRRAAPTLITPHAGELARLIRA-------ERADIEAARLQHARAAAAELGVTVLLKGSTTV 397
Cdd:PRK09355   91 PVGVGATSYrTEFALE--LLAEVKPAVIRGNASEIAALAGEaaetkgvDSTDGSADAVEIAKAAAKKYGTVVVVTGEVDY 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2074133566 398 VAEEPRPVRVNpTGTSWLAT-GGTGDVLSGVAGALLAQGLGAYDAGSCAAYLHGLAG 453
Cdd:PRK09355  169 ITDGERVVSVH-NGHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAACAVYGIAG 224
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 324-453 3.43e-05

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


Pssm-ID: 238575 [Multi-domain]  Cd Length: 242  Bit Score: 45.22  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 324 GLPVLVDADGL------TVVARDrsLLRRAAPTLITPHAGELARLIRAER--------ADIEAARLQHARAAAAELGVTV 389
Cdd:cd01170    79 GKPVVLDPVGVgatsfrTEVAKE--LLAEGQPTVIRGNASEIAALAGLTGlgkgvdssSSDEEDALELAKALARKYGAVV 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2074133566 390 LLKGSTTVVAEEPRPVRVnPTGTSWLA--TGgTGDVLSGVAGALLAQGLGAYDAGSCAAYLHGLAG 453
Cdd:cd01170   157 VVTGEVDYITDGERVVVV-KNGHPLLTkiTG-TGCLLGAVIAAFLAVGDDPLEAAVSAVLVYGIAG 220
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
341-435 2.10e-04

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 43.62  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074133566 341 RSLLRRAapTLITPHAGELARLIRAERADIEAARLQHARAAAAELGVTVLLKGSTTVVAEEPRPVrVNPTGTSWLATG-- 418
Cdd:PRK14713  152 RELVPRA--DLITPNLPELAVLLGEPPATTWEEALAQARRLAAETGTTVLVKGGHLDGQRAPDAL-VGPDGAVTEVPGpr 228

                          90       100
                  ....*....|....*....|....
gi 2074133566 419 -------GTGDVLSGVAGALLAQG 435
Cdd:PRK14713  229 vdtrnthGTGCSLSSALATRLGRG 252
 
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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