NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2666736860|ref|WP_329980978|]
View 

NAD(P)H-hydrate dehydratase [Dialister invisus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 220-507 7.78e-107

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: 319.76  E-value: 7.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 220 SVKLVEEKDIYEFLPVRSFAAHKGTNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSS 299
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 300 CGDAPCFTEDISDkavkqtgmYDVVALGPGLGRNERTQTFVADMLEHCRKTMVVDADALFAVGHQKINLRNCPADVVLTP 379
Cdd:COG0063    81 LPEEDELLELLER--------ADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 380 HVGEFAFLTGLTAKDVEAGRIDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQ 459
Cdd:COG0063   153 HPGEFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQ 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2666736860 460 GLSAEEAAVAGVYLHGLAGDLLAEKMPVGYTASDVARMIPLARKKVIE 507
Cdd:COG0063   233 GLDPFEAAAAGVYLHGLAGDLAAEERGRGLLASDLIEALPAALRELLE 280
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 26-191 2.88e-50

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: 169.33  E-value: 2.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  26 VLMENAGASVVQLMKEKISWEDARVVIVCGSGNNGGDGFVTARYALSEGADVAVLVMGDASHMGENSLLYKNIAAKMGIP 105
Cdd:pfam03853   3 VLMENAGRAAARVLKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 106 VISVAGADDAKEYLAGADIIVDALIGTGLKHHVKGSTAELITAMNDSEAVIVSVDVPSGMFSDSGCAAGAVVNADYTVAL 185
Cdd:pfam03853  83 IVTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTF 162


                  ....*.
gi 2666736860 186 GSVKRG 191
Cdd:pfam03853 163 GAPKPG 168
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 220-507 7.78e-107

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: 319.76  E-value: 7.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 220 SVKLVEEKDIYEFLPVRSFAAHKGTNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSS 299
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 300 CGDAPCFTEDISDkavkqtgmYDVVALGPGLGRNERTQTFVADMLEHCRKTMVVDADALFAVGHQKINLRNCPADVVLTP 379
Cdd:COG0063    81 LPEEDELLELLER--------ADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 380 HVGEFAFLTGLTAKDVEAGRIDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQ 459
Cdd:COG0063   153 HPGEFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQ 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2666736860 460 GLSAEEAAVAGVYLHGLAGDLLAEKMPVGYTASDVARMIPLARKKVIE 507
Cdd:COG0063   233 GLDPFEAAAAGVYLHGLAGDLAAEERGRGLLASDLIEALPAALRELLE 280
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 240-499 1.31e-85

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: 264.47  E-value: 1.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 240 AHKGTNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSSCGDAPCFTEDISDKAvkqtg 319
Cdd:cd01171     3 SHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLER----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 320 mYDVVALGPGLGRNERTQTFVADMLEHCrKTMVVDADALFAVGHQKInLRNCPADVVLTPHVGEFAFLTGLTAKDVEAGR 399
Cdd:cd01171    78 -ADAVVIGPGLGRDEEAAEILEKALAKD-KPLVLDADALNLLADEPS-LIKRYGPVVLTPHPGEFARLLGALVEEIQADR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 400 IDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQGLSAEEAAVAGVYLHGLAGD 479
Cdd:cd01171   155 LAAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGD 234

                         250       260
                  ....*....|....*....|
gi 2666736860 480 LLAEKMPVGYTASDVARMIP 499
Cdd:cd01171   235 LAAKKKGAGLTAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 7-500 4.06e-80

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 258.84  E-value: 4.06e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860   7 EESRLLDQRAMTEYGLPESVLMENAGASVVQLMKEkiSWEDAR-VVIVCGSGNNGGDGFVTARYALSEGADVAVL-VMGD 84
Cdd:PRK10565   21 DDIRRGEREAADALGLTLYELMLRAGEAAFQVARS--AYPDARhWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLaQESD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  85 ASHMGENSLLYKNIAAKMGipviSVAGADDAkeYLAGADIIVDALIGTGLKHHVKGSTAELITAMNDSEAVIVSVDVPSG 164
Cdd:PRK10565   99 KPLPEEAALAREAWLNAGG----EIHAADIV--WPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 165 MFSDSGCAAGAVVNADYTVALGSVKRGHVLYPGNGYTGTVLYSPIGI-PNGAREHFSVKLVEEKDIYEFLPVRSFAAHKG 243
Cdd:PRK10565  173 LLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLdSWLAGQEAPIQRFDAEQLSQWLKPRRPTSHKG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 244 TNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKI-ALASVGNAAFQLAGKiPEVMVsscgdapcftEDISDKAVKQTGMY- 321
Cdd:PRK10565  253 DHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVrVLTRSENIAPLLTAR-PELMV----------HELTPDSLEESLEWa 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 322 DVVALGPGLGRNERTQTFVAdMLEHCRKTMVVDADAL--FAVGHQKINLRncpadvVLTPHVGEFAFLTGLTAKDVEAGR 399
Cdd:PRK10565  322 DVVVIGPGLGQQEWGKKALQ-KVENFRKPMLWDADALnlLAINPDKRHNR------VITPHPGEAARLLGCSVAEIESDR 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 400 IDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQGLSAEEAAVAGVYLHGLAGD 479
Cdd:PRK10565  395 LLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAAD 474

                         490       500
                  ....*....|....*....|..
gi 2666736860 480 LLAEKMPV-GYTASDVARMIPL 500
Cdd:PRK10565  475 VLAARFGTrGMLATDLFSTLQR 496
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 223-499 1.50e-60

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: 199.92  E-value: 1.50e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 223 LVEEKDIyEFLPVRSFAAHKGTNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSSCGD 302
Cdd:TIGR00196   3 FLGEGDL-LTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 303 APCFTEDISDKavkqtgmYDVVALGPGLGRNERTQTFVADMLEHCRKtMVVDADALFAVGHQkiNLRNCPadVVLTPHVG 382
Cdd:TIGR00196  82 KVDEDEELLER-------YDVVVIGPGLGQDPSFKKAVEEVLELDKP-VVLDADALNLLTYN--QKREGE--VILTPHPG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 383 EFAFLTGltAKDVEAGRIDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQGLS 462
Cdd:TIGR00196 150 EFKRLLG--VNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLD 227

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2666736860 463 AEEAAVAGVYLHGLAGDLLAEKMPV-GYTASDVARMIP 499
Cdd:TIGR00196 228 PFDAACNAAFAHGLAGDLALKNHGAyGLTALDLIEKIP 265
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 248-500 7.41e-52

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: 176.40  E-value: 7.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 248 IGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSSCGDAPCFTEDISdkavkqtgMYDVVALG 327
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILEKLS--------RYDAVVIG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 328 PGLGRNERTQTFVADMLEHcRKTMVVDADALFAVG-HQKINLRNCPadVVLTPHVGEFAFLTGLtAKDVEAGRIDEAIRY 406
Cdd:pfam01256  73 PGLGRDEKGKAALEEVLAK-DCPLVIDADALNLLAiNNEKPAREGP--TVLTPHPGEFERLCGL-AGILGDDRLEAAREL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 407 AKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQGLSAEEAAVAGVYLHGLAGDLLAEKMP 486
Cdd:pfam01256 149 AQKLNGTILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG 228

                         250
                  ....*....|....
gi 2666736860 487 VGYTASDVARMIPL 500
Cdd:pfam01256 229 VYMLPTLLSKIIPR 242
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 26-191 2.88e-50

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: 169.33  E-value: 2.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  26 VLMENAGASVVQLMKEKISWEDARVVIVCGSGNNGGDGFVTARYALSEGADVAVLVMGDASHMGENSLLYKNIAAKMGIP 105
Cdd:pfam03853   3 VLMENAGRAAARVLKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 106 VISVAGADDAKEYLAGADIIVDALIGTGLKHHVKGSTAELITAMNDSEAVIVSVDVPSGMFSDSGCAAGAVVNADYTVAL 185
Cdd:pfam03853  83 IVTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTF 162


                  ....*.
gi 2666736860 186 GSVKRG 191
Cdd:pfam03853 163 GAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 6-213 7.72e-37

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: 134.85  E-value: 7.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860   6 SEESRLLDQRAMTEYGLPESVLMENAGASVVQLMKEKISWEdARVVIVCGSGNNGGDGFVTARYALSEGADVAVLVMGDA 85
Cdd:TIGR00197   5 SPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLA-GHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  86 SHMGENSLLYKNIAAKMGIPVISVAGADDAKeylagADIIVDALIGTGLKHHVKGSTAELITAMNDSEAVIVSVDVPSGM 165
Cdd:TIGR00197  84 IECTEQAEVNLKALKVGGISIDEGNLVKPED-----CDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2666736860 166 FSDSGCAAGAVVNADYTVALGSVKRGhVLYPGNGYTGTVLYSPIGIPN 213
Cdd:TIGR00197 159 DVDTGAIEGPAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIPP 205
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 12-202 1.32e-20

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 91.09  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  12 LDQRAMTEYGLPESVLMENAGASVVQLMKEKISWEDA--------RVVIVCGSGNNGGDGFVTARYALSEGADVAVLVMG 83
Cdd:PLN03050   17 LDEELMSTPGFSLEQLMELAGLSVAEAVYEVADGEKAsnppgrhpRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  84 DASHMgenslLYKNIAAK---MGIPVISVAGADDAKEYL--AGADIIVDALIGTGLKHHVKGSTAELITAMN---DSEAV 155
Cdd:PLN03050   97 QSSKP-----HYENLVTQcedLGIPFVQAIGGTNDSSKPleTTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPPP 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2666736860 156 IVSVDVPSGMFSDSGCAAGAVVNADYTVALGSVKRGHVLYPGNGYTG 202
Cdd:PLN03050  172 IVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 220-507 7.78e-107

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: 319.76  E-value: 7.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 220 SVKLVEEKDIYEFLPVRSFAAHKGTNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSS 299
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 300 CGDAPCFTEDISDkavkqtgmYDVVALGPGLGRNERTQTFVADMLEHCRKTMVVDADALFAVGHQKINLRNCPADVVLTP 379
Cdd:COG0063    81 LPEEDELLELLER--------ADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 380 HVGEFAFLTGLTAKDVEAGRIDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQ 459
Cdd:COG0063   153 HPGEFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQ 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2666736860 460 GLSAEEAAVAGVYLHGLAGDLLAEKMPVGYTASDVARMIPLARKKVIE 507
Cdd:COG0063   233 GLDPFEAAAAGVYLHGLAGDLAAEERGRGLLASDLIEALPAALRELLE 280
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 1-501 1.15e-90

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: 285.99  E-value: 1.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860   1 MILTTSEESRLLDQRAMTEYGLPESVLMENAGASVVQLMKEKISWEDARVVIVCGSGNNGGDGFVTARYALSEGADVAVL 80
Cdd:COG0062     1 MKLLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  81 VMGDASHMGENSLLYKNIAAKMGIPVISVagaDDAKEYLAGADIIVDALIGTGLKHHVKGSTAELITAMNDSEAVIVSVD 160
Cdd:COG0062    81 LLGDPEKLSGDAAANLERLKAAGIPILEL---DDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 161 VPSGMFSDSGCAAGAVVNADYTVALGSVKRGHVLYPGNGYTGTVLYSPIGIPNGA-REHFSVKLVEEKDIYEFLPVRSFA 239
Cdd:COG0062   158 IPSGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAaAEAPAALLLLADLLALLLPPRRRS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 240 AHKGTNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSSCGDAPCFTEDISDKavkqtg 319
Cdd:COG0062   238 HHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAA------ 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 320 myDVVALGPGLGRNERTQTFVADMLEHCRKTMVVDADALFAVGHQKINLRNCPADVVLTPHVGEFAFLTGLTAKDVEAGR 399
Cdd:COG0062   312 --VVVAGGGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAA 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 400 IDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQGLSAEEAAVAGVYLHGLAGD 479
Cdd:COG0062   390 LLAAAAAAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAA 469

                         490       500
                  ....*....|....*....|..
gi 2666736860 480 LLAEKMPVGYTASDVARMIPLA 501
Cdd:COG0062   470 AAAALAAALLAAAAALIALLLA 491
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 240-499 1.31e-85

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: 264.47  E-value: 1.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 240 AHKGTNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSSCGDAPCFTEDISDKAvkqtg 319
Cdd:cd01171     3 SHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLER----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 320 mYDVVALGPGLGRNERTQTFVADMLEHCrKTMVVDADALFAVGHQKInLRNCPADVVLTPHVGEFAFLTGLTAKDVEAGR 399
Cdd:cd01171    78 -ADAVVIGPGLGRDEEAAEILEKALAKD-KPLVLDADALNLLADEPS-LIKRYGPVVLTPHPGEFARLLGALVEEIQADR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 400 IDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQGLSAEEAAVAGVYLHGLAGD 479
Cdd:cd01171   155 LAAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGD 234

                         250       260
                  ....*....|....*....|
gi 2666736860 480 LLAEKMPVGYTASDVARMIP 499
Cdd:cd01171   235 LAAKKKGAGLTAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 7-500 4.06e-80

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 258.84  E-value: 4.06e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860   7 EESRLLDQRAMTEYGLPESVLMENAGASVVQLMKEkiSWEDAR-VVIVCGSGNNGGDGFVTARYALSEGADVAVL-VMGD 84
Cdd:PRK10565   21 DDIRRGEREAADALGLTLYELMLRAGEAAFQVARS--AYPDARhWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLaQESD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  85 ASHMGENSLLYKNIAAKMGipviSVAGADDAkeYLAGADIIVDALIGTGLKHHVKGSTAELITAMNDSEAVIVSVDVPSG 164
Cdd:PRK10565   99 KPLPEEAALAREAWLNAGG----EIHAADIV--WPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 165 MFSDSGCAAGAVVNADYTVALGSVKRGHVLYPGNGYTGTVLYSPIGI-PNGAREHFSVKLVEEKDIYEFLPVRSFAAHKG 243
Cdd:PRK10565  173 LLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLdSWLAGQEAPIQRFDAEQLSQWLKPRRPTSHKG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 244 TNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKI-ALASVGNAAFQLAGKiPEVMVsscgdapcftEDISDKAVKQTGMY- 321
Cdd:PRK10565  253 DHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVrVLTRSENIAPLLTAR-PELMV----------HELTPDSLEESLEWa 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 322 DVVALGPGLGRNERTQTFVAdMLEHCRKTMVVDADAL--FAVGHQKINLRncpadvVLTPHVGEFAFLTGLTAKDVEAGR 399
Cdd:PRK10565  322 DVVVIGPGLGQQEWGKKALQ-KVENFRKPMLWDADALnlLAINPDKRHNR------VITPHPGEAARLLGCSVAEIESDR 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 400 IDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQGLSAEEAAVAGVYLHGLAGD 479
Cdd:PRK10565  395 LLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAAD 474

                         490       500
                  ....*....|....*....|..
gi 2666736860 480 LLAEKMPV-GYTASDVARMIPL 500
Cdd:PRK10565  475 VLAARFGTrGMLATDLFSTLQR 496
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 223-499 1.50e-60

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: 199.92  E-value: 1.50e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 223 LVEEKDIyEFLPVRSFAAHKGTNGFIGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSSCGD 302
Cdd:TIGR00196   3 FLGEGDL-LTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 303 APCFTEDISDKavkqtgmYDVVALGPGLGRNERTQTFVADMLEHCRKtMVVDADALFAVGHQkiNLRNCPadVVLTPHVG 382
Cdd:TIGR00196  82 KVDEDEELLER-------YDVVVIGPGLGQDPSFKKAVEEVLELDKP-VVLDADALNLLTYN--QKREGE--VILTPHPG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 383 EFAFLTGltAKDVEAGRIDEAIRYAKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQGLS 462
Cdd:TIGR00196 150 EFKRLLG--VNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLD 227

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2666736860 463 AEEAAVAGVYLHGLAGDLLAEKMPV-GYTASDVARMIP 499
Cdd:TIGR00196 228 PFDAACNAAFAHGLAGDLALKNHGAyGLTALDLIEKIP 265
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 248-500 7.41e-52

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: 176.40  E-value: 7.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 248 IGIFAGSEGMAGAGLLAAQGALYGGGGKIALASVGNAAFQLAGKIPEVMVSSCGDAPCFTEDISdkavkqtgMYDVVALG 327
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILEKLS--------RYDAVVIG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 328 PGLGRNERTQTFVADMLEHcRKTMVVDADALFAVG-HQKINLRNCPadVVLTPHVGEFAFLTGLtAKDVEAGRIDEAIRY 406
Cdd:pfam01256  73 PGLGRDEKGKAALEEVLAK-DCPLVIDADALNLLAiNNEKPAREGP--TVLTPHPGEFERLCGL-AGILGDDRLEAAREL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 407 AKENHVVLVLKGAPTVIAVPDGRAWVNSTGNPGMAAGGMGDTLTGIIAAFIGQGLSAEEAAVAGVYLHGLAGDLLAEKMP 486
Cdd:pfam01256 149 AQKLNGTILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG 228

                         250
                  ....*....|....
gi 2666736860 487 VGYTASDVARMIPL 500
Cdd:pfam01256 229 VYMLPTLLSKIIPR 242
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 26-191 2.88e-50

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: 169.33  E-value: 2.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  26 VLMENAGASVVQLMKEKISWEDARVVIVCGSGNNGGDGFVTARYALSEGADVAVLVMGDASHMGENSLLYKNIAAKMGIP 105
Cdd:pfam03853   3 VLMENAGRAAARVLKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 106 VISVAGADDAKEYLAGADIIVDALIGTGLKHHVKGSTAELITAMNDSEAVIVSVDVPSGMFSDSGCAAGAVVNADYTVAL 185
Cdd:pfam03853  83 IVTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTF 162


                  ....*.
gi 2666736860 186 GSVKRG 191
Cdd:pfam03853 163 GAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 6-213 7.72e-37

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: 134.85  E-value: 7.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860   6 SEESRLLDQRAMTEYGLPESVLMENAGASVVQLMKEKISWEdARVVIVCGSGNNGGDGFVTARYALSEGADVAVLVMGDA 85
Cdd:TIGR00197   5 SPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLA-GHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  86 SHMGENSLLYKNIAAKMGIPVISVAGADDAKeylagADIIVDALIGTGLKHHVKGSTAELITAMNDSEAVIVSVDVPSGM 165
Cdd:TIGR00197  84 IECTEQAEVNLKALKVGGISIDEGNLVKPED-----CDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2666736860 166 FSDSGCAAGAVVNADYTVALGSVKRGhVLYPGNGYTGTVLYSPIGIPN 213
Cdd:TIGR00197 159 DVDTGAIEGPAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIPP 205
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 12-202 1.32e-20

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 91.09  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  12 LDQRAMTEYGLPESVLMENAGASVVQLMKEKISWEDA--------RVVIVCGSGNNGGDGFVTARYALSEGADVAVLVMG 83
Cdd:PLN03050   17 LDEELMSTPGFSLEQLMELAGLSVAEAVYEVADGEKAsnppgrhpRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  84 DASHMgenslLYKNIAAK---MGIPVISVAGADDAKEYL--AGADIIVDALIGTGLKHHVKGSTAELITAMN---DSEAV 155
Cdd:PLN03050   97 QSSKP-----HYENLVTQcedLGIPFVQAIGGTNDSSKPleTTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPPP 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2666736860 156 IVSVDVPSGMFSDSGCAAGAVVNADYTVALGSVKRGHVLYPGNGYTG 202
Cdd:PLN03050  172 IVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 5-189 2.03e-17

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 84.52  E-value: 2.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860   5 TSEESRLLDQRAMTEYGLPESVLMENAGASVVQLMKEKISWED-ARVVIVCGSGNNGGDGFVTARYALSEGADVAVLVMG 83
Cdd:PLN03049   16 SQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSPSEyRRVLALCGPGNNGGDGLVAARHLHHFGYKPSICYPK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  84 DAshmgeNSLLYKNIAAK---MGIPVISVagADDAKEYLAGADIIVDALIGTGLKHHVKGSTAELITAMNDSEA--VIVS 158
Cdd:PLN03049   96 RT-----DKPLYNGLVTQlesLSVPFLSV--EDLPSDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKLVRAAGppPIVS 168

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2666736860 159 VDVPSGMFSDSGCAAGAVVNADYTVALGSVK 189
Cdd:PLN03049  169 VDIPSGWHVEEGDVNGEGLKPDMLVSLTAPK 199
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 5-189 2.66e-12

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 68.81  E-value: 2.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860   5 TSEESRLLDQRAMTEYGLPESVLMENAGASVVQLMKE--KISwEDARVVIVCGSGNNGGDGFVTARYALSEGADVAVLVM 82
Cdd:PLN02918   92 TQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEvyKPG-EYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFVCYP 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860  83 GDASHMGENSLLYKniAAKMGIPVISVAG--ADDAKEYlagaDIIVDALIGTGLKHHVKGSTAELITAM--------NDS 152
Cdd:PLN02918  171 KRTAKPLYTGLVTQ--LESLSVPFVSVEDlpADLSKDF----DIIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeqTLK 244

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2666736860 153 EAVIVSVDVPSGMFSDSGCAAGAVVNADYTVALGSVK 189
Cdd:PLN02918  245 HPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPK 281
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 382-488 7.37e-08

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 53.65  E-value: 7.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 382 GEFAFLTGLTA--KDVEAGRIDE-----AIRYAKENHVVLVLKGAPTVIAVpDGRAWVNSTGNPGMAA-GGMGDTLTGII 453
Cdd:PRK09355  121 SEIAALAGEAAetKGVDSTDGSAdaveiAKAAAKKYGTVVVVTGEVDYITD-GERVVSVHNGHPLMTKvTGTGCLLSAVV 199

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2666736860 454 AAFIGQGLSAEEAAVAGVYLHGLAGDLLAEKMPVG 488
Cdd:PRK09355  200 AAFAAVEKDYLEAAAAACAVYGIAGELAAERSEKG 234
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 382-484 3.64e-06

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


Pssm-ID: 238575 [Multi-domain]  Cd Length: 242  Bit Score: 48.30  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 382 GEFAFLTGLTAK----DVEAGRIDEAIR----YAKENHVVLVLKGAPTVIAvpDG-RAWVNSTGNPGMAA-GGMGDTLTG 451
Cdd:cd01170   116 SEIAALAGLTGLgkgvDSSSSDEEDALElakaLARKYGAVVVVTGEVDYIT--DGeRVVVVKNGHPLLTKiTGTGCLLGA 193

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2666736860 452 IIAAFIGQGLSAEEAAVAGVYLHGLAGDLLAEK 484
Cdd:cd01170   194 VIAAFLAVGDDPLEAAVSAVLVYGIAGELAAER 226
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 373-472 1.65e-03

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 40.52  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666736860 373 ADVvLTPHVGEFAFLTGLTAKDVEAgrIDEAIR--YAKENHVVLVlKGAPT---------VIAVPDGRAWVNSTGNPGMA 441
Cdd:COG2240   139 ADI-ITPNLTELALLTGRPYETLEE--ALAAARalLALGPKIVVV-TSVPLddtpadkigNLAVTADGAWLVETPLLPFS 214

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2666736860 442 AGGMGDTLTGIIAAFIGQGLSAEEA---AVAGVY 472
Cdd:COG2240   215 PNGTGDLFAALLLAHLLRGKSLEEAlerAAAFVY 248
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH