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Conserved domains on  [gi|2103738851|gb|UBI76864|]
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NAD(P)H-hydrate dehydratase [Ensifer canadensis]

Protein Classification

NAD(P)H-hydrate epimerase( domain architecture ID 10000547)

NAD(P)H-hydrate epimerase catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
9-484 1.28e-71

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: 235.92  E-value: 1.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851   9 LITPAEMAAID-LAAAQSGIDSFLLMRRAGLAVAAAVLRLFP-QAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAF 86
Cdd:COG0062     3 LLTAAQMRALDrAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  87 GDPAAaLSGDADRARQLW---DGAIDPLASLVPHLG--DVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSG 161
Cdd:COG0062    83 GDPEK-LSGDAAANLERLkaaGIPILELDDELPELAeaDLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 162 VDGRTGQIRRAAFAASHTITFMARKPGHLLLPGRSLSGALDVVDIGIPArIVQAQGGGWRLNTPALWSDQASRLDASTHK 241
Cdd:COG0062   162 LDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI-PAAAEAPAALLLLADLLALLLPPRRRSHHK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 242 FRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDTRLGAFVLGP 321
Cdd:COG0062   241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 322 GFGVGDRACDFALQLCDRALVLDADGITSFQERRSELFERLAVAAGRVVMTPHEGEFARLFPEIARDEKLSKIEKAQAAA 401
Cdd:COG0062   321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 402 RishATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRHGAAGARAGPGLTA 481
Cdd:COG0062   401 A---AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477

                  ...
gi 2103738851 482 ETL 484
Cdd:COG0062   478 LLA 480
 
Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
9-484 1.28e-71

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: 235.92  E-value: 1.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851   9 LITPAEMAAID-LAAAQSGIDSFLLMRRAGLAVAAAVLRLFP-QAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAF 86
Cdd:COG0062     3 LLTAAQMRALDrAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  87 GDPAAaLSGDADRARQLW---DGAIDPLASLVPHLG--DVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSG 161
Cdd:COG0062    83 GDPEK-LSGDAAANLERLkaaGIPILELDDELPELAeaDLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 162 VDGRTGQIRRAAFAASHTITFMARKPGHLLLPGRSLSGALDVVDIGIPArIVQAQGGGWRLNTPALWSDQASRLDASTHK 241
Cdd:COG0062   162 LDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI-PAAAEAPAALLLLADLLALLLPPRRRSHHK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 242 FRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDTRLGAFVLGP 321
Cdd:COG0062   241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 322 GFGVGDRACDFALQLCDRALVLDADGITSFQERRSELFERLAVAAGRVVMTPHEGEFARLFPEIARDEKLSKIEKAQAAA 401
Cdd:COG0062   321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 402 RishATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRHGAAGARAGPGLTA 481
Cdd:COG0062   401 A---AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477

                  ...
gi 2103738851 482 ETL 484
Cdd:COG0062   478 LLA 480
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
237-468 2.32e-53

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: 180.12  E-value: 2.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 237 ASTHKFRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDTRLGA 316
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLERADA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 317 FVLGPGFGVGDRACDFALQLCDRA--LVLDADGITSFQERRSelferLAVAAGRVVMTPHEGEFARLFPEIARDEKLSKI 394
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDkpLVLDADALNLLADEPS-----LIKRYGPVVLTPHPGEFARLLGALVEEIQADRL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2103738851 395 EKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:cd01171   156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLH 229
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
21-468 2.20e-51

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 182.18  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  21 AAAQSGIDSFLLMRRAGLAVAAAVLRLFPQAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAFgDPAAALSGDADRA 100
Cdd:PRK10565   30 AADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQ-ESDKPLPEEAALA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 101 RQLW---DGAIDPLASLVPHLGDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAAS 177
Cdd:PRK10565  109 REAWlnaGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINAD 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 178 HTITFMARKPGHLLLPGRSLSGALDVVDIGIPARIVQAQGGGWRLNTPALWSDQASRlDASTHKFRRGHLVVFSGGAQAT 257
Cdd:PRK10565  189 HTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR-RPTSHKGDHGRLLIIGGDHGTA 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 258 GAARLSAAAGLAAGAGLVTVASPKSALdinAAQLTA---VMLREIDD---RQDLEhWlrdtrLGAFVLGPGFGVGDRACD 331
Cdd:PRK10565  268 GAIRMAGEAALRSGAGLVRVLTRSENI---APLLTArpeLMVHELTPdslEESLE-W-----ADVVVIGPGLGQQEWGKK 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 332 fALQL---CDRALVLDADGITsfqerrselfeRLAVAAGRV---VMTPHEGEFARLF----PEIARDEKLSkiekAQAAA 401
Cdd:PRK10565  339 -ALQKvenFRKPMLWDADALN-----------LLAINPDKRhnrVITPHPGEAARLLgcsvAEIESDRLLS----ARRLV 402
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2103738851 402 RISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:PRK10565  403 KRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAH 469
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
7-209 4.19e-36

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: 132.92  E-value: 4.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851   7 DVLITPAEMAAIDLAAAQSGIDSFLLMRRAGLAVAAAVLRLFPQAQRYVVLCGPGNNGGDGYVAASALAecGANVAVFAF 86
Cdd:TIGR00197   1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLK--GFGVEVFLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  87 GDPAA-ALSGDADRARQLW---DGAIDPLASLVPHLGDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGV 162
Cdd:TIGR00197  79 KKEKRiECTEQAEVNLKALkvgGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2103738851 163 DGRTGQIRRAAFAASHTITFMARKPGhLLLPGRSLSGALDVVDIGIP 209
Cdd:TIGR00197 159 DVDTGAIEGPAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIP 204
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
46-188 1.51e-35

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: 130.04  E-value: 1.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  46 RLFPQAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAFGDPAAaLSGDADRARQLWDGAIDPLASLVPHL------- 118
Cdd:pfam03853  19 LLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEK-LSEDARRQLDLFKKLGGKIVTDNPDEdleklls 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2103738851 119 -GDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAASHTITFMARKPG 188
Cdd:pfam03853  98 pVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
 
Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
9-484 1.28e-71

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: 235.92  E-value: 1.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851   9 LITPAEMAAID-LAAAQSGIDSFLLMRRAGLAVAAAVLRLFP-QAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAF 86
Cdd:COG0062     3 LLTAAQMRALDrAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  87 GDPAAaLSGDADRARQLW---DGAIDPLASLVPHLG--DVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSG 161
Cdd:COG0062    83 GDPEK-LSGDAAANLERLkaaGIPILELDDELPELAeaDLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 162 VDGRTGQIRRAAFAASHTITFMARKPGHLLLPGRSLSGALDVVDIGIPArIVQAQGGGWRLNTPALWSDQASRLDASTHK 241
Cdd:COG0062   162 LDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI-PAAAEAPAALLLLADLLALLLPPRRRSHHK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 242 FRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDTRLGAFVLGP 321
Cdd:COG0062   241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 322 GFGVGDRACDFALQLCDRALVLDADGITSFQERRSELFERLAVAAGRVVMTPHEGEFARLFPEIARDEKLSKIEKAQAAA 401
Cdd:COG0062   321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 402 RishATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRHGAAGARAGPGLTA 481
Cdd:COG0062   401 A---AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477

                  ...
gi 2103738851 482 ETL 484
Cdd:COG0062   478 LLA 480
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
220-491 3.54e-65

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: 211.90  E-value: 3.54e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 220 WRLNTPALWSDQASRLDASTHKFRRGHLVVFSGGAQATgaarlsaaaglaagaglVTVASPKSALDINAAQLTAVMLREI 299
Cdd:COG0063     2 ARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPgaavlaaraalragaglVTVAVPESAAPAVAAALPELMVIPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 300 DDRQDLEHWLRdtRLGAFVLGPGFGVGDRACDF---ALQLCDRALVLDADGITSFQERRSELFERlavaAGRVVMTPHEG 376
Cdd:COG0063    82 PEEDELLELLE--RADAVVIGPGLGRDEETRELlraLLEAADKPLVLDADALNLLAEDPELLAAL----PAPTVLTPHPG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 377 EFARLFPEIARDEKLSKIEKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMP 456
Cdd:COG0063   156 EFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLD 235
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2103738851 457 AFEAAAAGVWRH----GAAGARAGPGLTAETLVTSIPPL 491
Cdd:COG0063   236 PFEAAAAGVYLHglagDLAAEERGRGLLASDLIEALPAA 274
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
237-468 2.32e-53

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: 180.12  E-value: 2.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 237 ASTHKFRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDTRLGA 316
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLERADA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 317 FVLGPGFGVGDRACDFALQLCDRA--LVLDADGITSFQERRSelferLAVAAGRVVMTPHEGEFARLFPEIARDEKLSKI 394
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDkpLVLDADALNLLADEPS-----LIKRYGPVVLTPHPGEFARLLGALVEEIQADRL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2103738851 395 EKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:cd01171   156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLH 229
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
21-468 2.20e-51

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 182.18  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  21 AAAQSGIDSFLLMRRAGLAVAAAVLRLFPQAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAFgDPAAALSGDADRA 100
Cdd:PRK10565   30 AADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQ-ESDKPLPEEAALA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 101 RQLW---DGAIDPLASLVPHLGDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAAS 177
Cdd:PRK10565  109 REAWlnaGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINAD 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 178 HTITFMARKPGHLLLPGRSLSGALDVVDIGIPARIVQAQGGGWRLNTPALWSDQASRlDASTHKFRRGHLVVFSGGAQAT 257
Cdd:PRK10565  189 HTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR-RPTSHKGDHGRLLIIGGDHGTA 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 258 GAARLSAAAGLAAGAGLVTVASPKSALdinAAQLTA---VMLREIDD---RQDLEhWlrdtrLGAFVLGPGFGVGDRACD 331
Cdd:PRK10565  268 GAIRMAGEAALRSGAGLVRVLTRSENI---APLLTArpeLMVHELTPdslEESLE-W-----ADVVVIGPGLGQQEWGKK 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 332 fALQL---CDRALVLDADGITsfqerrselfeRLAVAAGRV---VMTPHEGEFARLF----PEIARDEKLSkiekAQAAA 401
Cdd:PRK10565  339 -ALQKvenFRKPMLWDADALN-----------LLAINPDKRhnrVITPHPGEAARLLgcsvAEIESDRLLS----ARRLV 402
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2103738851 402 RISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:PRK10565  403 KRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAH 469
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
7-209 4.19e-36

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: 132.92  E-value: 4.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851   7 DVLITPAEMAAIDLAAAQSGIDSFLLMRRAGLAVAAAVLRLFPQAQRYVVLCGPGNNGGDGYVAASALAecGANVAVFAF 86
Cdd:TIGR00197   1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLK--GFGVEVFLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  87 GDPAA-ALSGDADRARQLW---DGAIDPLASLVPHLGDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGV 162
Cdd:TIGR00197  79 KKEKRiECTEQAEVNLKALkvgGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2103738851 163 DGRTGQIRRAAFAASHTITFMARKPGhLLLPGRSLSGALDVVDIGIP 209
Cdd:TIGR00197 159 DVDTGAIEGPAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIP 204
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
46-188 1.51e-35

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: 130.04  E-value: 1.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  46 RLFPQAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAFGDPAAaLSGDADRARQLWDGAIDPLASLVPHL------- 118
Cdd:pfam03853  19 LLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEK-LSEDARRQLDLFKKLGGKIVTDNPDEdleklls 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2103738851 119 -GDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAASHTITFMARKPG 188
Cdd:pfam03853  98 pVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
235-491 1.26e-29

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: 117.10  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 235 LDASTHKFRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDtRL 314
Cdd:TIGR00196  15 RDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMWKVDEDEELLE-RY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 315 GAFVLGPGFG---VGDRACDFALQLCdRALVLDADGItsfqerrsELFERLAVAAGRVVMTPHEGEFARLFPEIarDEKL 391
Cdd:TIGR00196  94 DVVVIGPGLGqdpSFKKAVEEVLELD-KPVVLDADAL--------NLLTYNQKREGEVILTPHPGEFKRLLGVN--EIQG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 392 SKIEKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRHGAA 471
Cdd:TIGR00196 163 DRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLA 242
                         250       260
                  ....*....|....*....|....*
gi 2103738851 472 GAR-----AGPGLTAETLVTSIPPL 491
Cdd:TIGR00196 243 GDLalknhGAYGLTALDLIEKIPRV 267
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
313-468 3.66e-26

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: 106.68  E-value: 3.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 313 RLGAFVLGPGFG---VGDRACDFALqLCDRALVLDADGITsFQERRSELFERlavaAGRVVMTPHEGEFARLFPEIARDE 389
Cdd:pfam01256  65 RYDAVVIGPGLGrdeKGKAALEEVL-AKDCPLVIDADALN-LLAINNEKPAR----EGPTVLTPHPGEFERLCGLAGILG 138
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2103738851 390 KlSKIEKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:pfam01256 139 D-DRLEAARELAQKLNGTILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLH 216
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
49-201 2.51e-10

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 60.66  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  49 PQAQ-RYVVLCGPGNNGGDGYVAASALAECGANVAVFAfgdPAAAlsgdadrARQLWDGAIDPLASL-VPHLG------- 119
Cdd:PLN03050   57 PGRHpRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCY---PKQS-------SKPHYENLVTQCEDLgIPFVQaiggtnd 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 120 ---------DVVVDALFG---AGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAASHTITFMARK- 186
Cdd:PLN03050  127 sskplettyDVIVDAIFGfsfHGAPRAPFDTLLAQMVQQQKSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKl 206
                         170       180
                  ....*....|....*....|
gi 2103738851 187 -----PGHLLLPGRSLSGAL 201
Cdd:PLN03050  207 sakkfEGRHFVGGRFLPPAI 226
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
53-169 1.79e-09

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 59.86  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  53 RYVVLCGPGNNGGDGYVAASALAEcganvavfaFG-DPAAALSGDADRArqLWDGAIDPLASL-VPHLG----------- 119
Cdd:PLN03049   61 RVLALCGPGNNGGDGLVAARHLHH---------FGyKPSICYPKRTDKP--LYNGLVTQLESLsVPFLSvedlpsdlssq 129
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2103738851 120 -DVVVDALFG---AGLSRDLPEQVVQVIerINAKGVPVI-AVDLPSGVDGRTGQI 169
Cdd:PLN03049  130 fDIVVDAMFGfsfHGAPRPPFDDLIQKL--VRAAGPPPIvSVDIPSGWHVEEGDV 182
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
53-191 1.69e-07

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 53.79  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851  53 RYVVLCGPGNNGGDGYVAASALAECGANVAVFAfgdPAAAlsgdadrARQLWDGAIDPLASL-VPHLG------------ 119
Cdd:PLN02918  137 RVLAICGPGNNGGDGLVAARHLHHFGYKPFVCY---PKRT-------AKPLYTGLVTQLESLsVPFVSvedlpadlskdf 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 120 DVVVDALFG---AGLSR----DLPEQVVQVIERINAKGVPVI-AVDLPSGVDGRTGQIRRAAFAASHTITFMARK----- 186
Cdd:PLN02918  207 DIIVDAMFGfsfHGAPRppfdDLIRRLVSLQNYEQTLKHPVIvSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKlcakk 286

                  ....*...
gi 2103738851 187 ---PGHLL 191
Cdd:PLN02918  287 frgPHHFL 294
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
388-465 6.33e-03

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 38.63  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 388 DEKLSKIEKAQAAARISHATIVYKGADTVIAgaDG-KVAVNANAPPSLAT-AGSGDVLAGIVGAHLAQGMPAFEAAAAGV 465
Cdd:PRK09355  140 DGSADAVEIAKAAAKKYGTVVVVTGEVDYIT--DGeRVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAAC 217
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
394-465 6.98e-03

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: 38.29  E-value: 6.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2103738851 394 IEKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPpsLATA--GSGDVLAGIVGAHLAQGMPAFEAAAAGV 465
Cdd:cd01170   142 LELAKALARKYGAVVVVTGEVDYITDGERVVVVKNGHP--LLTKitGTGCLLGAVIAAFLAVGDDPLEAAVSAV 213
 
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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