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Conserved domains on  [gi|410697556|gb|AFV76624|]
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yjeF-like protein, hydroxyethylthiazole kinase-related protein [Thermus oshimai JL-2]

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 ...
 221-472 4.74e-70

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: 224.23  E-value: 4.74e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 221 TAHKGSVGRVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEGHPP----SPLEAVFHPVP-APSLPPL--KVE 293
Cdd:COG0063   20 DSHKGSRGHVLVIGGSRG----YPGAAVLAARAALRAGAGLVTVAVPESAAPavaaALPELMVIPLPeEDELLELleRAD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 294 ALAVGMGGGPWGAAWALAA---LEAGLPTVLDADALTL--EVAEAYRRRGLPAVLTPHAGEAARLLGTTPEAVAGDPLEA 368
Cdd:COG0063   96 AVVIGPGLGRDEETRELLRallEAADKPLVLDADALNLlaEDPELLAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 369 ARALAERTGLTVVLKGAPTVVAEGD-RLSVNPTGHPALATGGTGDVlsgaiaallaaGLPPFEAARLGVFLHGLAGDLLA 447
Cdd:COG0063  176 AREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVlagiiagllaqGLDPFEAAAAGVYLHGLAGDLAA 255

                        250       260
                 ....*....|....*....|....*
gi 410697556 448 EEKGIGLLAHEVAEALPRARRLLEE 472
Cdd:COG0063  256 EERGRGLLASDLIEALPAALRELLE 280
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 26-173 3.66e-31

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: 118.10  E-value: 3.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556   26 LMEWAGMKAARVYRALF--GEAPAVVLAGKGNNGGDGLVLARHLLLEGVGVRVYA---EEGQKGDALLALKALLAHGVEV 100
Cdd:pfam03853   4 LMENAGRAAARVLKALLspAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLlgpEEKLSEDARRQLDLFKKLGGKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  101 RPLEEASWAEG-----EVLVDALFGTGLKGPLMGFYAGLVERMNASRLPILALDLPSGL------PHAPQVRATATVAFG 169
Cdd:pfam03853  84 VTDNPDEDLEKllspvDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLdadtgaVLGTAVRADHTVTFG 163


                  ....
gi 410697556  170 GLKT 173
Cdd:pfam03853 164 APKP 167
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 221-472 4.74e-70

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: 224.23  E-value: 4.74e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 221 TAHKGSVGRVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEGHPP----SPLEAVFHPVP-APSLPPL--KVE 293
Cdd:COG0063   20 DSHKGSRGHVLVIGGSRG----YPGAAVLAARAALRAGAGLVTVAVPESAAPavaaALPELMVIPLPeEDELLELleRAD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 294 ALAVGMGGGPWGAAWALAA---LEAGLPTVLDADALTL--EVAEAYRRRGLPAVLTPHAGEAARLLGTTPEAVAGDPLEA 368
Cdd:COG0063   96 AVVIGPGLGRDEETRELLRallEAADKPLVLDADALNLlaEDPELLAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 369 ARALAERTGLTVVLKGAPTVVAEGD-RLSVNPTGHPALATGGTGDVlsgaiaallaaGLPPFEAARLGVFLHGLAGDLLA 447
Cdd:COG0063  176 AREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVlagiiagllaqGLDPFEAAAAGVYLHGLAGDLAA 255

                        250       260
                 ....*....|....*....|....*
gi 410697556 448 EEKGIGLLAHEVAEALPRARRLLEE 472
Cdd:COG0063  256 EERGRGLLASDLIEALPAALRELLE 280
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 221-464 3.08e-61

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: 200.53  E-value: 3.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 221 TAHKGSVGRVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEGHPPSPL----EAVFHPVPAPSLPPL-----K 291
Cdd:cd01171    2 DSHKGSRGRVLVIGGSRG----YTGAAYLAALAALRAGAGLVTVATPPEAAAVIKsyspELMVHPLLETDIEELlelleR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 292 VEALAVGMGGG--PWGAAWALAALEAGLPTVLDADALTLEVAEAYRRRGL-PAVLTPHAGEAARLLGTTPEAVAGDPLEA 368
Cdd:cd01171   78 ADAVVIGPGLGrdEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKRYgPVVLTPHPGEFARLLGALVEEIQADRLAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 369 ARALAERTGLTVVLKGAPTVVAEGD-RLSVNPTGHPALATGGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLA 447
Cdd:cd01171  158 AREAAAKLGATVVLKGAVTVIADPDgRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAA 237

                        250
                 ....*....|....*..
gi 410697556 448 EEKGIGLLAHEVAEALP 464
Cdd:cd01171  238 KKKGAGLTAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 4-465 2.61e-57

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 197.98  E-value: 2.61e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556   4 FTPEAMRRADERAAERGYPTLL-LMEWAGMKAARVYRALFGEAPA-VVLAGKGNNGGDGLVLARHLLLEGVGVRVYAEEG 81
Cdd:PRK10565  18 WPADDIRRGEREAADALGLTLYeLMLRAGEAAFQVARSAYPDARHwLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQES 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  82 QK---GDALLALKALLAHGVEVRPlEEASWAEG-EVLVDALFGTGLKGPLMGFYAGLVERMNASRLPILALDLPSGL--- 154
Cdd:PRK10565  98 DKplpEEAALAREAWLNAGGEIHA-ADIVWPESvDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLlae 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 155 -PHAPQ--VRATATVAFGGLKtPHLFQ---REACGRLFLAEIGLPKDLLEDSTLPEVATLEALRPLLPRRPLTAHKGSVG 228
Cdd:PRK10565 177 tGATPGavINADHTVTFIALK-PGLLTgkaRDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPRRPTSHKGDHG 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 229 RVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHlVLPEGHPPSPL-----EAVFHPVPAPSLPP----LKVEALAVGM 299
Cdd:PRK10565 256 RLLIIGGDHG----TAGAIRMAGEAALRSGAGLVR-VLTRSENIAPLltarpELMVHELTPDSLEEslewADVVVIGPGL 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 300 GGGPWGAAWALAALEAGLPTVLDADALTLEVAEAYRRRGlpAVLTPHAGEAARLLGTTPEAVAGDPLEAARALAERTGLT 379
Cdd:PRK10565 331 GQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHN--RVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGGV 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 380 VVLKGAPTVVA-EGDRLSVNPTGHPALATGGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLAEEKGI-GLLAH 457
Cdd:PRK10565 409 VVLKGAGTVIAaEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTrGMLAT 488


                 ....*...
gi 410697556 458 EVAEALPR 465
Cdd:PRK10565 489 DLFSTLQR 496
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 221-466 7.68e-44

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: 155.23  E-value: 7.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  221 TAHKGSVGRVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEG-----HPPSPLEAVF---HPVPAPSLPPLKV 292
Cdd:TIGR00196  18 NSHKGQYGRVLIIGGSDD----YSGAPLLAALAALRAGAGLVTVAAPENvitliNSVSPELIVHrlmWKVDEDEELLERY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  293 EALAVGMGGG--PWGAAWALAALEAGLPTVLDADALTLEVAEAYRRRglPAVLTPHAGEAARLLGTTpeAVAGDPLEAAR 370
Cdd:TIGR00196  94 DVVVIGPGLGqdPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREG--EVILTPHPGEFKRLLGVN--EIQGDRLEAAQ 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  371 ALAERTGLTVVLKGAPTVVAEGD-RLSVNPTGHPALATGGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLAEE 449
Cdd:TIGR00196 170 DIAQKLQAVVVLKGAADVIAAPDgDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDLALKN 249

                         250
                  ....*....|....*...
gi 410697556  450 KGI-GLLAHEVAEALPRA 466
Cdd:TIGR00196 250 HGAyGLTALDLIEKIPRV 267
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 230-465 1.57e-38

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: 140.19  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  230 VGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEG-----HPPSPLEAVfHPVPAPSLPPLKVEALAV-----GM 299
Cdd:pfam01256   1 VLVIGGSKD----YTGAPLLAALAALRSGAGLVSVATDSEaiavlKSPLPEVMV-HPLPETSSILEKLSRYDAvvigpGL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  300 GGGPWGAAWALAALEAGLPTVLDADALTL--EVAEAYRRRGlPAVLTPHAGEAARLLGTtPEAVAGDPLEAARALAERTG 377
Cdd:pfam01256  76 GRDEKGKAALEEVLAKDCPLVIDADALNLlaINNEKPAREG-PTVLTPHPGEFERLCGL-AGILGDDRLEAARELAQKLN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  378 LTVVLKGAPTVVA-EGDRLSVNPTGHPALATGGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLAEEKGIGLLA 456
Cdd:pfam01256 154 GTILLKGNVTVIAaPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGVYMLP 233


                  ....*....
gi 410697556  457 HEVAEALPR 465
Cdd:pfam01256 234 TLLSKIIPR 242
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 26-173 3.66e-31

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: 118.10  E-value: 3.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556   26 LMEWAGMKAARVYRALF--GEAPAVVLAGKGNNGGDGLVLARHLLLEGVGVRVYA---EEGQKGDALLALKALLAHGVEV 100
Cdd:pfam03853   4 LMENAGRAAARVLKALLspAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLlgpEEKLSEDARRQLDLFKKLGGKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  101 RPLEEASWAEG-----EVLVDALFGTGLKGPLMGFYAGLVERMNASRLPILALDLPSGL------PHAPQVRATATVAFG 169
Cdd:pfam03853  84 VTDNPDEDLEKllspvDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLdadtgaVLGTAVRADHTVTFG 163


                  ....
gi 410697556  170 GLKT 173
Cdd:pfam03853 164 APKP 167
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 5-194 1.76e-29

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: 114.43  E-value: 1.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556    5 TPEAMRRADERAAERGYPTLLLMEWAGMKAARVYRALFGEAPAV-VLAGKGNNGGDGLVLARHLLLEGVGVRVYAEEGQK 83
Cdd:TIGR00197   5 SPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHViIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556   84 GDALLALKALLAHGVEVRPLEEASW---AEGEVLVDALFGTGLKGPLMGFYAGLVERMNASRLPILALDLPSGL------ 154
Cdd:TIGR00197  85 ECTEQAEVNLKALKVGGISIDEGNLvkpEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLdvdtga 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 410697556  155 PHAPQVRATATVAFGGLKTPHLFQR-EACGRLFLAEIGLPK 194
Cdd:TIGR00197 165 IEGPAVNADLTITFHAIKPCLLSDRaDVTGELKVGGIGIPP 205
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 13-153 8.83e-11

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 62.20  E-value: 8.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  13 DERAAERGYPTLLLMEWAGMKAAR-VYRALFGEAPA---------VVLAGKGNNGGDGLVLARHLLLEGVGVRV-YAEEG 81
Cdd:PLN03050  19 EELMSTPGFSLEQLMELAGLSVAEaVYEVADGEKASnppgrhprvLLVCGPGNNGGDGLVAARHLAHFGYEVTVcYPKQS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  82 QKGDALLALKALLAHGVEVRPLEEASWAEG-------EVLVDALFGTGLKGPLMGFYAGLVERMN---ASRLPILALDLP 151
Cdd:PLN03050  99 SKPHYENLVTQCEDLGIPFVQAIGGTNDSSkplettyDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPPPIVSVDVP 178


                 ..
gi 410697556 152 SG 153
Cdd:PLN03050 179 SG 180
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 221-472 4.74e-70

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: 224.23  E-value: 4.74e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 221 TAHKGSVGRVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEGHPP----SPLEAVFHPVP-APSLPPL--KVE 293
Cdd:COG0063   20 DSHKGSRGHVLVIGGSRG----YPGAAVLAARAALRAGAGLVTVAVPESAAPavaaALPELMVIPLPeEDELLELleRAD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 294 ALAVGMGGGPWGAAWALAA---LEAGLPTVLDADALTL--EVAEAYRRRGLPAVLTPHAGEAARLLGTTPEAVAGDPLEA 368
Cdd:COG0063   96 AVVIGPGLGRDEETRELLRallEAADKPLVLDADALNLlaEDPELLAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 369 ARALAERTGLTVVLKGAPTVVAEGD-RLSVNPTGHPALATGGTGDVlsgaiaallaaGLPPFEAARLGVFLHGLAGDLLA 447
Cdd:COG0063  176 AREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVlagiiagllaqGLDPFEAAAAGVYLHGLAGDLAA 255

                        250       260
                 ....*....|....*....|....*
gi 410697556 448 EEKGIGLLAHEVAEALPRARRLLEE 472
Cdd:COG0063  256 EERGRGLLASDLIEALPAALRELLE 280
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 221-464 3.08e-61

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: 200.53  E-value: 3.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 221 TAHKGSVGRVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEGHPPSPL----EAVFHPVPAPSLPPL-----K 291
Cdd:cd01171    2 DSHKGSRGRVLVIGGSRG----YTGAAYLAALAALRAGAGLVTVATPPEAAAVIKsyspELMVHPLLETDIEELlelleR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 292 VEALAVGMGGG--PWGAAWALAALEAGLPTVLDADALTLEVAEAYRRRGL-PAVLTPHAGEAARLLGTTPEAVAGDPLEA 368
Cdd:cd01171   78 ADAVVIGPGLGrdEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKRYgPVVLTPHPGEFARLLGALVEEIQADRLAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 369 ARALAERTGLTVVLKGAPTVVAEGD-RLSVNPTGHPALATGGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLA 447
Cdd:cd01171  158 AREAAAKLGATVVLKGAVTVIADPDgRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAA 237

                        250
                 ....*....|....*..
gi 410697556 448 EEKGIGLLAHEVAEALP 464
Cdd:cd01171  238 KKKGAGLTAADLVAEIP 254
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 1-471 1.09e-59

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: 203.95  E-value: 1.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556   1 MRLFTPEAMRRADERAAER-GYPTLLLMEWAGMKAARVYRALFGEAPA--VVLAGKGNNGGDGLVLARHLLLEGVGVRVY 77
Cdd:COG0062    1 MKLLTAAQMRALDRAAIEAlGIPGLVLMERAGRAVARAIRRRFPSAARrvLVLCGPGNNGGDGLVAARLLAEAGYNVTVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  78 A---EEGQKGDALLALKALLAHGVEVRPLEE--ASWAEGEVLVDALFGTGLKGPLMGFYAGLVERMNASRLPILALDLPS 152
Cdd:COG0062   81 LlgdPEKLSGDAAANLERLKAAGIPILELDDelPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 153 GL------PHAPQVRATATVAFGGLKTPHLFQ--REACGRLFLAEIGLPKDLLEDSTLPEVATLEALRPLLPRRPLTAHK 224
Cdd:COG0062  161 GLdadtgeVLGAAVRADLTVTFGAPKPGLLLGpgRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 225 GSVGRVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEGHPPSPLEAVFHPVPAPSLPPLK-------VEALAV 297
Cdd:COG0062  241 GGGGGVLVIGGGGG----GGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEElllllaaAVVVAG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 298 GMGGGPWGAAWALAALEAGLPTVLDADALTLEVAEAYRRRGLPAVLTPHAGEAARLLGTTPEAVAGDPLEAARALAERTG 377
Cdd:COG0062  317 GGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAA 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 378 LTVVLKGAPTVVAEGDRLSVNPTGHPALATGGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLAEEKGIGLLAH 457
Cdd:COG0062  397 AAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAA 476

                        490
                 ....*....|....
gi 410697556 458 EVAEALPRARRLLE 471
Cdd:COG0062  477 ALLAAAAALIALLL 490
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 4-465 2.61e-57

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 197.98  E-value: 2.61e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556   4 FTPEAMRRADERAAERGYPTLL-LMEWAGMKAARVYRALFGEAPA-VVLAGKGNNGGDGLVLARHLLLEGVGVRVYAEEG 81
Cdd:PRK10565  18 WPADDIRRGEREAADALGLTLYeLMLRAGEAAFQVARSAYPDARHwLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQES 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  82 QK---GDALLALKALLAHGVEVRPlEEASWAEG-EVLVDALFGTGLKGPLMGFYAGLVERMNASRLPILALDLPSGL--- 154
Cdd:PRK10565  98 DKplpEEAALAREAWLNAGGEIHA-ADIVWPESvDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLlae 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 155 -PHAPQ--VRATATVAFGGLKtPHLFQ---REACGRLFLAEIGLPKDLLEDSTLPEVATLEALRPLLPRRPLTAHKGSVG 228
Cdd:PRK10565 177 tGATPGavINADHTVTFIALK-PGLLTgkaRDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPRRPTSHKGDHG 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 229 RVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHlVLPEGHPPSPL-----EAVFHPVPAPSLPP----LKVEALAVGM 299
Cdd:PRK10565 256 RLLIIGGDHG----TAGAIRMAGEAALRSGAGLVR-VLTRSENIAPLltarpELMVHELTPDSLEEslewADVVVIGPGL 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 300 GGGPWGAAWALAALEAGLPTVLDADALTLEVAEAYRRRGlpAVLTPHAGEAARLLGTTPEAVAGDPLEAARALAERTGLT 379
Cdd:PRK10565 331 GQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHN--RVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGGV 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 380 VVLKGAPTVVA-EGDRLSVNPTGHPALATGGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLAEEKGI-GLLAH 457
Cdd:PRK10565 409 VVLKGAGTVIAaEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTrGMLAT 488


                 ....*...
gi 410697556 458 EVAEALPR 465
Cdd:PRK10565 489 DLFSTLQR 496
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 221-466 7.68e-44

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: 155.23  E-value: 7.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  221 TAHKGSVGRVGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEG-----HPPSPLEAVF---HPVPAPSLPPLKV 292
Cdd:TIGR00196  18 NSHKGQYGRVLIIGGSDD----YSGAPLLAALAALRAGAGLVTVAAPENvitliNSVSPELIVHrlmWKVDEDEELLERY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  293 EALAVGMGGG--PWGAAWALAALEAGLPTVLDADALTLEVAEAYRRRglPAVLTPHAGEAARLLGTTpeAVAGDPLEAAR 370
Cdd:TIGR00196  94 DVVVIGPGLGqdPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREG--EVILTPHPGEFKRLLGVN--EIQGDRLEAAQ 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  371 ALAERTGLTVVLKGAPTVVAEGD-RLSVNPTGHPALATGGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLAEE 449
Cdd:TIGR00196 170 DIAQKLQAVVVLKGAADVIAAPDgDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDLALKN 249

                         250
                  ....*....|....*...
gi 410697556  450 KGI-GLLAHEVAEALPRA 466
Cdd:TIGR00196 250 HGAyGLTALDLIEKIPRV 267
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 230-465 1.57e-38

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: 140.19  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  230 VGVLGGYRGegllYAGAPLLAALGAYRMGAGLVHLVLPEG-----HPPSPLEAVfHPVPAPSLPPLKVEALAV-----GM 299
Cdd:pfam01256   1 VLVIGGSKD----YTGAPLLAALAALRSGAGLVSVATDSEaiavlKSPLPEVMV-HPLPETSSILEKLSRYDAvvigpGL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  300 GGGPWGAAWALAALEAGLPTVLDADALTL--EVAEAYRRRGlPAVLTPHAGEAARLLGTtPEAVAGDPLEAARALAERTG 377
Cdd:pfam01256  76 GRDEKGKAALEEVLAKDCPLVIDADALNLlaINNEKPAREG-PTVLTPHPGEFERLCGL-AGILGDDRLEAARELAQKLN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  378 LTVVLKGAPTVVA-EGDRLSVNPTGHPALATGGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLAEEKGIGLLA 456
Cdd:pfam01256 154 GTILLKGNVTVIAaPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGVYMLP 233


                  ....*....
gi 410697556  457 HEVAEALPR 465
Cdd:pfam01256 234 TLLSKIIPR 242
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 26-173 3.66e-31

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: 118.10  E-value: 3.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556   26 LMEWAGMKAARVYRALF--GEAPAVVLAGKGNNGGDGLVLARHLLLEGVGVRVYA---EEGQKGDALLALKALLAHGVEV 100
Cdd:pfam03853   4 LMENAGRAAARVLKALLspAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLlgpEEKLSEDARRQLDLFKKLGGKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  101 RPLEEASWAEG-----EVLVDALFGTGLKGPLMGFYAGLVERMNASRLPILALDLPSGL------PHAPQVRATATVAFG 169
Cdd:pfam03853  84 VTDNPDEDLEKllspvDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLdadtgaVLGTAVRADHTVTFG 163


                  ....
gi 410697556  170 GLKT 173
Cdd:pfam03853 164 APKP 167
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 5-194 1.76e-29

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: 114.43  E-value: 1.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556    5 TPEAMRRADERAAERGYPTLLLMEWAGMKAARVYRALFGEAPAV-VLAGKGNNGGDGLVLARHLLLEGVGVRVYAEEGQK 83
Cdd:TIGR00197   5 SPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHViIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556   84 GDALLALKALLAHGVEVRPLEEASW---AEGEVLVDALFGTGLKGPLMGFYAGLVERMNASRLPILALDLPSGL------ 154
Cdd:TIGR00197  85 ECTEQAEVNLKALKVGGISIDEGNLvkpEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLdvdtga 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 410697556  155 PHAPQVRATATVAFGGLKTPHLFQR-EACGRLFLAEIGLPK 194
Cdd:TIGR00197 165 IEGPAVNADLTITFHAIKPCLLSDRaDVTGELKVGGIGIPP 205
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 13-153 8.83e-11

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 62.20  E-value: 8.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  13 DERAAERGYPTLLLMEWAGMKAAR-VYRALFGEAPA---------VVLAGKGNNGGDGLVLARHLLLEGVGVRV-YAEEG 81
Cdd:PLN03050  19 EELMSTPGFSLEQLMELAGLSVAEaVYEVADGEKASnppgrhprvLLVCGPGNNGGDGLVAARHLAHFGYEVTVcYPKQS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  82 QKGDALLALKALLAHGVEVRPLEEASWAEG-------EVLVDALFGTGLKGPLMGFYAGLVERMN---ASRLPILALDLP 151
Cdd:PLN03050  99 SKPHYENLVTQCEDLGIPFVQAIGGTNDSSkplettyDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPPPIVSVDVP 178


                 ..
gi 410697556 152 SG 153
Cdd:PLN03050 179 SG 180
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 26-153 6.66e-09

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 57.94  E-value: 6.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  26 LMEWAGMKAA----RVYRALfGEAPAVVLAGKGNNGGDGLVLARHLLLEGVGVRV-YAEEGQKGDALLALKALLAHGVEV 100
Cdd:PLN03049  38 LMELAGLSVAsaiaEVYSPS-EYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSIcYPKRTDKPLYNGLVTQLESLSVPF 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 410697556 101 RPLEE--ASWAEG-EVLVDALFGTGLKGPLMGFYAGLVERMNASRL--PILALDLPSG 153
Cdd:PLN03049 117 LSVEDlpSDLSSQfDIVVDAMFGFSFHGAPRPPFDDLIQKLVRAAGppPIVSVDIPSG 174
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 318-463 2.07e-07

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: 51.77  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 318 PTVLD-----ADALTLEVAEAYRRRGLPAVLTPHAGEAARLLGTT--------PEAVAGDPLEAARALAERTGLTVVLKG 384
Cdd:cd01170   81 PVVLDpvgvgATSFRTEVAKELLAEGQPTVIRGNASEIAALAGLTglgkgvdsSSSDEEDALELAKALARKYGAVVVVTG 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 385 APTVVAEGDRLSVNPTGHPALA--TGgTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLAE-EKGIGLLAHEVAE 461
Cdd:cd01170  161 EVDYITDGERVVVVKNGHPLLTkiTG-TGCLLGAVIAAFLAVGDDPLEAAVSAVLVYGIAGELAAErAKGPGSFRVALLD 239


                 ..
gi 410697556 462 AL 463
Cdd:cd01170  240 EL 241
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 318-453 1.58e-06

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 49.41  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 318 PTVLD---ADALTL--EVAEAYRRRGLPAVLTPHAGEAARLLGTTPEA-------VAGDPLEAARALAERTGLTVVLKGA 385
Cdd:PRK09355  86 PVVLDpvgVGATSYrtEFALELLAEVKPAVIRGNASEIAALAGEAAETkgvdstdGSADAVEIAKAAAKKYGTVVVVTGE 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410697556 386 PTVVAEGDRLSVNPTGHPALAT-GGTGDVLSGAIAALLAAGLPPFEAARLGVFLHGLAGDLLAEEKGIG 453
Cdd:PRK09355 166 VDYITDGERVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAACAVYGIAGELAAERSEKG 234
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 20-153 5.12e-05

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 45.70  E-value: 5.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556  20 GYPTLLLMEWAGMKAA----RVYRAlfGEAPAV-VLAGKGNNGGDGLVLARHLLLEGVGVRV-YAEEGQK---GDALLAL 90
Cdd:PLN02918 108 GFSVDQLMELAGLSVAasiaEVYKP--GEYSRVlAICGPGNNGGDGLVAARHLHHFGYKPFVcYPKRTAKplyTGLVTQL 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410697556  91 KALLAHGVEVRPLEEASWAEGEVLVDALFGTGLKGPLMGFYAGLVERM-------NASRLP-ILALDLPSG 153
Cdd:PLN02918 186 ESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeQTLKHPvIVSVDIPSG 256
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
324-408 1.36e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 41.31  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 324 DALTLEVAEAYRRRGLP--AVLTPHAGEAARLLGTTPEAVAGDPLEAARALAERTGLTVVLKGAPTVVAEGDRLSVNPTG 401
Cdd:PRK14713 140 DRLLEEDAEAALRELVPraDLITPNLPELAVLLGEPPATTWEEALAQARRLAAETGTTVLVKGGHLDGQRAPDALVGPDG 219


                 ....*..
gi 410697556 402 HPALATG 408
Cdd:PRK14713 220 AVTEVPG 226
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 329-413 4.06e-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: 39.10  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410697556 329 EVAEAYRRRGLPA--VLTPHAGEAARLLGTTPEAVAgDPLEAARALAERTGLTVVLKGAPtvVAEGDRL--------SVN 398
Cdd:cd01173  124 EIVPVYRDLLVPLadIITPNQFELELLTGKKINDLE-DAKAAARALHAKGPKTVVVTSVE--LADDDRIemlgstatEAW 200

                         90
                 ....*....|....*....
gi 410697556 399 PTGHPALATG----GTGDV 413
Cdd:cd01173  201 LVQRPKIPFPayfnGTGDL 219
 
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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