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Conserved domains on  [gi|1938575349|gb|QPJ84920|]
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NAD(P)H-hydrate dehydratase [Sarcina sp. JB2]

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 ...
 237-495 1.21e-110

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: 329.01  E-value: 1.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 237 REKYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSYENND-FKELILNSDS 315
Cdd:COG0063    17 RPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPEEDeLLELLERADA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 316 IAIGPGMGNNENTFNIIKDILSKDGCPLVLDADALNVLQHNLDLLKNSKRKIVITPHIGEMGRLTGIDSKNIIKNRIDIA 395
Cdd:COG0063    97 VVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEAA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 396 RDFSKKYGIIVLLKGYNTIITNGE-EVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDILSK 474
Cdd:COG0063   177 REAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAGVYLHGLAGDLAAE 256

                         250       260
                  ....*....|....*....|..
gi 1938575349 475 D-MFCVNASHIVERLPYIIENL 495
Cdd:COG0063   257 ErGRGLLASDLIEALPAALREL 278
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 24-190 2.23e-46

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: 158.93  E-value: 2.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  24 STVLMENAAL---KVVKNINFEKFNSFTIICGTGNNGGDALAVARQLFSMNMKVDIFIIG-EHSMSKDCLINYNILKNMG 99
Cdd:pfam03853   1 SAVLMENAGRaaaRVLKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGpEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 100 VPIKQIVKTQDiqlLNDILNKNDMIIDGIFGSGLARNIDGIYKEVIKSINKSGMYILSIDVPSGMLCDSFGILGSCVKAN 179
Cdd:pfam03853  81 GKIVTDNPDED---LEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRAD 157

                         170
                  ....*....|.
gi 1938575349 180 KTVSFEVYKKG 190
Cdd:pfam03853 158 HTVTFGAPKPG 168
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 237-495 1.21e-110

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: 329.01  E-value: 1.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 237 REKYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSYENND-FKELILNSDS 315
Cdd:COG0063    17 RPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPEEDeLLELLERADA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 316 IAIGPGMGNNENTFNIIKDILSKDGCPLVLDADALNVLQHNLDLLKNSKRKIVITPHIGEMGRLTGIDSKNIIKNRIDIA 395
Cdd:COG0063    97 VVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEAA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 396 RDFSKKYGIIVLLKGYNTIITNGE-EVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDILSK 474
Cdd:COG0063   177 REAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAGVYLHGLAGDLAAE 256

                         250       260
                  ....*....|....*....|..
gi 1938575349 475 D-MFCVNASHIVERLPYIIENL 495
Cdd:COG0063   257 ErGRGLLASDLIEALPAALREL 278
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 239-489 5.59e-97

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: 293.36  E-value: 5.59e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 239 KYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSYENND---FKELILNSDS 315
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 316 IAIGPGMGNNENTFNIIKDILSKDgCPLVLDADALNVLQHNLDLLKnSKRKIVITPHIGEMGRLTGIDSKNIIKNRIDIA 395
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKD-KPLVLDADALNLLADEPSLIK-RYGPVVLTPHPGEFARLLGALVEEIQADRLAAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 396 RDFSKKYGIIVLLKGYNTIITNG-EEVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDILSK 474
Cdd:cd01171   159 REAAAKLGATVVLKGAVTVIADPdGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAK 238

                         250
                  ....*....|....*.
gi 1938575349 475 DMFCV-NASHIVERLP 489
Cdd:cd01171   239 KKGAGlTAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 49-473 9.14e-65

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 218.01  E-value: 9.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  49 IICGTGNNGGDALAVARQLFSMNMKVDIFII-GEHSMSKDCLINYNILKNMGvpikQIVKTQDIQLLNDIlnknDMIIDG 127
Cdd:PRK10565   65 VLCGHGNNGGDGYVVARLAQAAGIDVTLLAQeSDKPLPEEAALAREAWLNAG----GEIHAADIVWPESV----DLIVDA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 128 IFGSGLARNIDGIYKEVIKSINKSGMYILSIDVPSGMLCDSFGILGSCVKANKTVSFEVYKKGFLDYESDKYTGEIVVES 207
Cdd:PRK10565  137 LLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDS 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 208 IGIPEYVVNK---------FHLKEYLvqkkeiksiiKKREKYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVT 278
Cdd:PRK10565  217 LGLDSWLAGQeapiqrfdaEQLSQWL----------KPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVR 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 279 LCTEKSVVEILQSKTIETMIMSYENNDFKELILNSDSIAIGPGMGNNENTFNIIKDILSKDGcPLVLDADALNVLQHNLD 358
Cdd:PRK10565  287 VLTRSENIAPLLTARPELMVHELTPDSLEESLEWADVVVIGPGLGQQEWGKKALQKVENFRK-PMLWDADALNLLAINPD 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 359 LLKNSkrkiVITPHIGEMGRLTGIDSKNIIKNRIDIARDFSKKYGIIVLLKGYNTIITN-GEEVYINSTGNSKMASGGMG 437
Cdd:PRK10565  366 KRHNR----VITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAAePDALAIIDVGNAGMASGGMG 441

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1938575349 438 DILTGIIASFIGQGYEPLKATILSAFIHGYVGDILS 473
Cdd:PRK10565  442 DVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLA 477
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 237-492 9.40e-64

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: 208.01  E-value: 9.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 237 REKYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSY-ENNDFKELILNS-D 314
Cdd:TIGR00196  15 RDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmWKVDEDEELLERyD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 315 SIAIGPGMGNNENTFNIIKDILSKDgCPLVLDADALNVLQHNLDLlknsKRKIVITPHIGEMGRLTGIDSknIIKNRIDI 394
Cdd:TIGR00196  95 VVVIGPGLGQDPSFKKAVEEVLELD-KPVVLDADALNLLTYNQKR----EGEVILTPHPGEFKRLLGVNE--IQGDRLEA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 395 ARDFSKKYGIIVLLKGYNTIITNGE-EVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDILS 473
Cdd:TIGR00196 168 AQDIAQKLQAVVVLKGAADVIAAPDgDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDLAL 247

                         250       260
                  ....*....|....*....|.
gi 1938575349 474 KD--MFCVNASHIVERLPYII 492
Cdd:TIGR00196 248 KNhgAYGLTALDLIEKIPRVC 268
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 249-489 1.60e-60

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: 198.74  E-value: 1.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 249 VSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSY-ENNDFKELILNSDSIAIGPGMGNNEN 327
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLpETSSILEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 328 TFNIIKDILSKDgCPLVLDADALNVL-QHNLDLLKNSKRkiVITPHIGEMGRLTGiDSKNIIKNRIDIARDFSKKYGIIV 406
Cdd:pfam01256  81 GKAALEEVLAKD-CPLVIDADALNLLaINNEKPAREGPT--VLTPHPGEFERLCG-LAGILGDDRLEAARELAQKLNGTI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 407 LLKG-YNTIITNGEEVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDILSKDM-FCVNASHI 484
Cdd:pfam01256 157 LLKGnVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHgVYMLPTLL 236


                  ....*
gi 1938575349 485 VERLP 489
Cdd:pfam01256 237 SKIIP 241
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 24-190 2.23e-46

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: 158.93  E-value: 2.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  24 STVLMENAAL---KVVKNINFEKFNSFTIICGTGNNGGDALAVARQLFSMNMKVDIFIIG-EHSMSKDCLINYNILKNMG 99
Cdd:pfam03853   1 SAVLMENAGRaaaRVLKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGpEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 100 VPIKQIVKTQDiqlLNDILNKNDMIIDGIFGSGLARNIDGIYKEVIKSINKSGMYILSIDVPSGMLCDSFGILGSCVKAN 179
Cdd:pfam03853  81 GKIVTDNPDED---LEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRAD 157

                         170
                  ....*....|.
gi 1938575349 180 KTVSFEVYKKG 190
Cdd:pfam03853 158 HTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 6-212 1.99e-32

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: 122.91  E-value: 1.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349   6 SQLIKNIDNYCINDLDIPSTVLMENAALKVVKNINFEKFNS--FTIICGTGNNGGDALAVARQLfsMNMKVDIFIIGEHS 83
Cdd:TIGR00197   5 SPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAghVIIFCGPGNNGGDGFVVARHL--KGFGVEVFLLKKEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  84 ---MSKDCLINYNILKNMGVPIKqivktqDIQLLNDIlnKNDMIIDGIFGSGLARNIDGIYKEVIKSINKSGMYILSIDV 160
Cdd:TIGR00197  83 rieCTEQAEVNLKALKVGGISID------EGNLVKPE--DCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1938575349 161 PSGMLCDSFGILGSCVKANKTVSFEVYKKGFLDYESDkYTGEIVVESIGIPE 212
Cdd:TIGR00197 155 PSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRAD-VTGELKVGGIGIPP 205
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 12-221 1.24e-10

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 63.33  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  12 IDNYCINDLDIPSTVLMENAALKVVKNI----NFEKFNSFTIICGTGNNGGDALAVARQLFSMNMKVDIfiigehsmskd 87
Cdd:PLN03049   23 IDEHLMGPLGFSVDQLMELAGLSVASAIaevySPSEYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSI----------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  88 CLIN------YN----ILKNMGVPikqIVKTQDIQLlnDILNKNDMIIDGIFG---SGLARN-IDGIYKEVIKSINKSGm 153
Cdd:PLN03049   92 CYPKrtdkplYNglvtQLESLSVP---FLSVEDLPS--DLSSQFDIVVDAMFGfsfHGAPRPpFDDLIQKLVRAAGPPP- 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938575349 154 yILSIDVPSGMLCDSFGILGSCVKANKTVSFEVYKkgfldYESDKYTGEivVESIG---IPEYVVNKFHLK 221
Cdd:PLN03049  166 -IVSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPK-----LCAKMFKGP--HHFLGgrfVPPAIVEKFKLH 228
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 237-495 1.21e-110

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: 329.01  E-value: 1.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 237 REKYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSYENND-FKELILNSDS 315
Cdd:COG0063    17 RPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPEEDeLLELLERADA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 316 IAIGPGMGNNENTFNIIKDILSKDGCPLVLDADALNVLQHNLDLLKNSKRKIVITPHIGEMGRLTGIDSKNIIKNRIDIA 395
Cdd:COG0063    97 VVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEAA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 396 RDFSKKYGIIVLLKGYNTIITNGE-EVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDILSK 474
Cdd:COG0063   177 REAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAGVYLHGLAGDLAAE 256

                         250       260
                  ....*....|....*....|..
gi 1938575349 475 D-MFCVNASHIVERLPYIIENL 495
Cdd:COG0063   257 ErGRGLLASDLIEALPAALREL 278
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 239-489 5.59e-97

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: 293.36  E-value: 5.59e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 239 KYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSYENND---FKELILNSDS 315
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 316 IAIGPGMGNNENTFNIIKDILSKDgCPLVLDADALNVLQHNLDLLKnSKRKIVITPHIGEMGRLTGIDSKNIIKNRIDIA 395
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKD-KPLVLDADALNLLADEPSLIK-RYGPVVLTPHPGEFARLLGALVEEIQADRLAAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 396 RDFSKKYGIIVLLKGYNTIITNG-EEVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDILSK 474
Cdd:cd01171   159 REAAAKLGATVVLKGAVTVIADPdGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAK 238

                         250
                  ....*....|....*.
gi 1938575349 475 DMFCV-NASHIVERLP 489
Cdd:cd01171   239 KKGAGlTAADLVAEIP 254
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 1-472 1.75e-92

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: 290.23  E-value: 1.75e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349   1 MKIGNSQLIKNIDNYCINDLDIPSTVLMENAALKVVKNInFEKFN----SFTIICGTGNNGGDALAVARQLFSMNMKVDI 76
Cdd:COG0062     1 MKLLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAI-RRRFPsaarRVLVLCGPGNNGGDGLVAARLLAEAGYNVTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  77 FIIGEHS-MSKDCLINYNILKNMGVPIkqivktQDIQLLNDILNKNDMIIDGIFGSGLARNIDGIYKEVIKSINKSGMYI 155
Cdd:COG0062    80 FLLGDPEkLSGDAAANLERLKAAGIPI------LELDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 156 LSIDVPSGMLCDSFGILGSCVKANKTVSFEVYKKGFLDYESDKYTGEIVVESIGIPEyVVNKFHLKEYLVQKKEIKSIIK 235
Cdd:COG0062   154 LAVDIPSGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI-PAAAEAPAALLLLADLLALLLP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 236 KREKYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSYENNDFKELILNSDS 315
Cdd:COG0062   233 PRRRSHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 316 IAIGPGMGNNENTFNIIKDILSKDGCPLVLDADALNVLQHNLDLLKNSKRKIVITPHIGEMGRLT--GIDSKNIIKNRID 393
Cdd:COG0062   313 VVAGGGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLteLLELRAAAAALLA 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1938575349 394 IARDFSKKYGIIVLLKGYNTIITNGEEVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDIL 472
Cdd:COG0062   393 AAAAAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAA 471
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 49-473 9.14e-65

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 218.01  E-value: 9.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  49 IICGTGNNGGDALAVARQLFSMNMKVDIFII-GEHSMSKDCLINYNILKNMGvpikQIVKTQDIQLLNDIlnknDMIIDG 127
Cdd:PRK10565   65 VLCGHGNNGGDGYVVARLAQAAGIDVTLLAQeSDKPLPEEAALAREAWLNAG----GEIHAADIVWPESV----DLIVDA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 128 IFGSGLARNIDGIYKEVIKSINKSGMYILSIDVPSGMLCDSFGILGSCVKANKTVSFEVYKKGFLDYESDKYTGEIVVES 207
Cdd:PRK10565  137 LLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDS 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 208 IGIPEYVVNK---------FHLKEYLvqkkeiksiiKKREKYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVT 278
Cdd:PRK10565  217 LGLDSWLAGQeapiqrfdaEQLSQWL----------KPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVR 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 279 LCTEKSVVEILQSKTIETMIMSYENNDFKELILNSDSIAIGPGMGNNENTFNIIKDILSKDGcPLVLDADALNVLQHNLD 358
Cdd:PRK10565  287 VLTRSENIAPLLTARPELMVHELTPDSLEESLEWADVVVIGPGLGQQEWGKKALQKVENFRK-PMLWDADALNLLAINPD 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 359 LLKNSkrkiVITPHIGEMGRLTGIDSKNIIKNRIDIARDFSKKYGIIVLLKGYNTIITN-GEEVYINSTGNSKMASGGMG 437
Cdd:PRK10565  366 KRHNR----VITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAAePDALAIIDVGNAGMASGGMG 441

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1938575349 438 DILTGIIASFIGQGYEPLKATILSAFIHGYVGDILS 473
Cdd:PRK10565  442 DVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLA 477
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 237-492 9.40e-64

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: 208.01  E-value: 9.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 237 REKYSYKGDFGRVSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSY-ENNDFKELILNS-D 314
Cdd:TIGR00196  15 RDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmWKVDEDEELLERyD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 315 SIAIGPGMGNNENTFNIIKDILSKDgCPLVLDADALNVLQHNLDLlknsKRKIVITPHIGEMGRLTGIDSknIIKNRIDI 394
Cdd:TIGR00196  95 VVVIGPGLGQDPSFKKAVEEVLELD-KPVVLDADALNLLTYNQKR----EGEVILTPHPGEFKRLLGVNE--IQGDRLEA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 395 ARDFSKKYGIIVLLKGYNTIITNGE-EVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDILS 473
Cdd:TIGR00196 168 AQDIAQKLQAVVVLKGAADVIAAPDgDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDLAL 247

                         250       260
                  ....*....|....*....|.
gi 1938575349 474 KD--MFCVNASHIVERLPYII 492
Cdd:TIGR00196 248 KNhgAYGLTALDLIEKIPRVC 268
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 249-489 1.60e-60

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: 198.74  E-value: 1.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 249 VSVIAGSKKYTGAAYLTSQGAVRSGAGLVTLCTEKSVVEILQSKTIETMIMSY-ENNDFKELILNSDSIAIGPGMGNNEN 327
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLpETSSILEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 328 TFNIIKDILSKDgCPLVLDADALNVL-QHNLDLLKNSKRkiVITPHIGEMGRLTGiDSKNIIKNRIDIARDFSKKYGIIV 406
Cdd:pfam01256  81 GKAALEEVLAKD-CPLVIDADALNLLaINNEKPAREGPT--VLTPHPGEFERLCG-LAGILGDDRLEAARELAQKLNGTI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 407 LLKG-YNTIITNGEEVYINSTGNSKMASGGMGDILTGIIASFIGQGYEPLKATILSAFIHGYVGDILSKDM-FCVNASHI 484
Cdd:pfam01256 157 LLKGnVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHgVYMLPTLL 236


                  ....*
gi 1938575349 485 VERLP 489
Cdd:pfam01256 237 SKIIP 241
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 24-190 2.23e-46

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: 158.93  E-value: 2.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  24 STVLMENAAL---KVVKNINFEKFNSFTIICGTGNNGGDALAVARQLFSMNMKVDIFIIG-EHSMSKDCLINYNILKNMG 99
Cdd:pfam03853   1 SAVLMENAGRaaaRVLKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGpEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 100 VPIKQIVKTQDiqlLNDILNKNDMIIDGIFGSGLARNIDGIYKEVIKSINKSGMYILSIDVPSGMLCDSFGILGSCVKAN 179
Cdd:pfam03853  81 GKIVTDNPDED---LEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRAD 157

                         170
                  ....*....|.
gi 1938575349 180 KTVSFEVYKKG 190
Cdd:pfam03853 158 HTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 6-212 1.99e-32

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: 122.91  E-value: 1.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349   6 SQLIKNIDNYCINDLDIPSTVLMENAALKVVKNINFEKFNS--FTIICGTGNNGGDALAVARQLfsMNMKVDIFIIGEHS 83
Cdd:TIGR00197   5 SPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAghVIIFCGPGNNGGDGFVVARHL--KGFGVEVFLLKKEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  84 ---MSKDCLINYNILKNMGVPIKqivktqDIQLLNDIlnKNDMIIDGIFGSGLARNIDGIYKEVIKSINKSGMYILSIDV 160
Cdd:TIGR00197  83 rieCTEQAEVNLKALKVGGISID------EGNLVKPE--DCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1938575349 161 PSGMLCDSFGILGSCVKANKTVSFEVYKKGFLDYESDkYTGEIVVESIGIPE 212
Cdd:TIGR00197 155 PSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRAD-VTGELKVGGIGIPP 205
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 298-459 1.03e-13

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: 70.65  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 298 IMSYENNDFKELILNSDS--IAIGPGMGNNENTFNIIKDILSKDGCPLVLDADALNVLQHNLDL---LKNSKRKIVITPH 372
Cdd:cd01170    35 IMSDAPEEVEELAKIAGAlvINIGTLTSEQIEAMLKAGKAANQLGKPVVLDPVGVGATSFRTEVakeLLAEGQPTVIRGN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 373 IGEMGRLTGIDSKNI--------IKNRIDIARDFSKKYGIIVLLKGYNTIITNGEEVYINSTGNSKMAS-GGMGDILTGI 443
Cdd:cd01170   115 ASEIAALAGLTGLGKgvdssssdEEDALELAKALARKYGAVVVVTGEVDYITDGERVVVVKNGHPLLTKiTGTGCLLGAV 194

                         170
                  ....*....|....*.
gi 1938575349 444 IASFIGQGYEPLKATI 459
Cdd:cd01170   195 IAAFLAVGDDPLEAAV 210
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 373-459 7.90e-12

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 65.59  E-value: 7.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 373 IGEMGRLTGIDSKNIIKNRIDIARDFSKKYGIIVLLKGYNTIITNGEEVYINSTGNSKMAS-GGMGDILTGIIASFIGQG 451
Cdd:PRK09355  127 AGEAAETKGVDSTDGSADAVEIAKAAAKKYGTVVVVTGEVDYITDGERVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVE 206


                  ....*...
gi 1938575349 452 YEPLKATI 459
Cdd:PRK09355  207 KDYLEAAA 214
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 12-221 1.24e-10

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 63.33  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  12 IDNYCINDLDIPSTVLMENAALKVVKNI----NFEKFNSFTIICGTGNNGGDALAVARQLFSMNMKVDIfiigehsmskd 87
Cdd:PLN03049   23 IDEHLMGPLGFSVDQLMELAGLSVASAIaevySPSEYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSI----------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  88 CLIN------YN----ILKNMGVPikqIVKTQDIQLlnDILNKNDMIIDGIFG---SGLARN-IDGIYKEVIKSINKSGm 153
Cdd:PLN03049   92 CYPKrtdkplYNglvtQLESLSVP---FLSVEDLPS--DLSSQFDIVVDAMFGfsfHGAPRPpFDDLIQKLVRAAGPPP- 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938575349 154 yILSIDVPSGMLCDSFGILGSCVKANKTVSFEVYKkgfldYESDKYTGEivVESIG---IPEYVVNKFHLK 221
Cdd:PLN03049  166 -IVSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPK-----LCAKMFKGP--HHFLGgrfVPPAIVEKFKLH 228
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 49-201 8.26e-09

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 56.42  E-value: 8.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  49 IICGTGNNGGDALAVARQLFSMNMKVDifIIGEHSMSKDCLINY-NILKNMGVPIKQIVKTqDIQLLNDILNKNDMIIDG 127
Cdd:PLN03050   65 LVCGPGNNGGDGLVAARHLAHFGYEVT--VCYPKQSSKPHYENLvTQCEDLGIPFVQAIGG-TNDSSKPLETTYDVIVDA 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938575349 128 IFG---SGLARNIDGIYKEVIKSINKSGMYILSIDVPSGMLCDSFGILGSCVKANKTVSFEVYKKGFLDYESDKYTG 201
Cdd:PLN03050  142 IFGfsfHGAPRAPFDTLLAQMVQQQKSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 12-188 1.03e-07

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 54.56  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  12 IDNYCINDLDIPSTVLMENAALKVVKNI----NFEKFNSFTIICGTGNNGGDALAVARQLFSMNMKVdiFIIGEHSMSKD 87
Cdd:PLN02918   99 IDETLMGPLGFSVDQLMELAGLSVAASIaevyKPGEYSRVLAICGPGNNGGDGLVAARHLHHFGYKP--FVCYPKRTAKP 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349  88 ClinYN----ILKNMGVPikqIVKTQDiqLLNDILNKNDMIIDGIFG---SGLARNI--DGIYKEV-IKSINKSGMY--I 155
Cdd:PLN02918  177 L---YTglvtQLESLSVP---FVSVED--LPADLSKDFDIIVDAMFGfsfHGAPRPPfdDLIRRLVsLQNYEQTLKHpvI 248

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1938575349 156 LSIDVPSGMLCDSFGILGSCVKANKTVSFEVYK 188
Cdd:PLN02918  249 VSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPK 281
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 321-466 9.20e-04

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 40.93  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 321 GMGNNENTFNIIKDILSKDGCPLVLD-------------ADALNVLQHNLdllknSKRKIVITPHIGEMGRLTGIDSKNi 387
Cdd:pfam08543  67 GMLGSAEIIEAVAEKLDKYGVPVVLDpvmvaksgdslldDEAIEALKEEL-----LPLATLITPNLPEAEALTGRKIKT- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 388 IKNRIDIARDFSKKYGIIVLLKG----------YNTIITNGEEV-----YINSTGNSkmasgGMGDILTGIIASFIGQGY 452
Cdd:pfam08543 141 LEDMKEAAKKLLALGAKAVLIKGghlegeeavvTDVLYDGGGFYtleapRIPTKNTH-----GTGCTLSAAIAANLAKGL 215

                         170
                  ....*....|....*
gi 1938575349 453 EPLKATILS-AFIHG 466
Cdd:pfam08543 216 SLPEAVREAkEYVTE 230
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 368-457 7.58e-03

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 38.33  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 368 VITPHIGEMGRLTGIDSKNiIKNRIDIARDFSKKYGIIVLLKG--------YNTIITNGEEVYINSTGNSKMASG--GMG 437
Cdd:cd01173   139 IITPNQFELELLTGKKIND-LEDAKAAARALHAKGPKTVVVTSveladddrIEMLGSTATEAWLVQRPKIPFPAYfnGTG 217

                          90       100
                  ....*....|....*....|
gi 1938575349 438 DILTGIIASFIGQGYEPLKA 457
Cdd:cd01173   218 DLFAALLLARLLKGKSLAEA 237
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 337-466 9.02e-03

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 38.10  E-value: 9.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938575349 337 SKDGCPLvLDADALNVLQHnlDLLKNSKrkiVITPHIGEMGRLTGIDSKNiIKNRIDIARDFSKKYGIIVLLKG------ 410
Cdd:COG0351   104 AKSGDRL-LDEDAVEALRE--LLLPLAT---VVTPNLPEAEALLGIEITT-LDDMREAAKALLELGAKAVLVKGghlpgd 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1938575349 411 --YNTIITNGEEVYINS----TGNskmaSGGMGDILTGIIASFIGQGYEPLKATILS-AFIHG 466
Cdd:COG0351   177 eaVDVLYDGDGVREFSApridTGN----THGTGCTLSSAIAALLAKGLDLEEAVREAkEYVTQ 235
 
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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