NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|42573644|ref|NP_974918|]
View 

pyridoxin (pyrodoxamine) 5'-phosphate oxidase [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02918 super family cl29141
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 4-466 0e+00

pyridoxine (pyridoxamine) 5'-phosphate oxidase


The actual alignment was detected with superfamily member PLN02918:

Pssm-ID: 356017 [Multi-domain]  Cd Length: 544  Bit Score: 903.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644    4 VIRRVTTMTFTFLLQSPPLPISP-SPPQFSLSSSPLSKTQRFITPSQG----SRLRTLCTKV-------------IIPNM 65
Cdd:PLN02918   1 NIKSTATMTFTFLLQSLLPLPISpPPPHSSSLSSSPSPTQRFLTPSQGsrlpPRRRALCTKSqdprwrramaslaVIPNM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   66 QDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHH 145
Cdd:PLN02918  81 QDSGSPPLSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  146 FGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 225
Cdd:PLN02918 161 FGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  226 QTLqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDML-----------RFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSM 294
Cdd:PLN02918 241 QTL-KHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLvsltapklcakKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSM 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  295 CVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENG 374
Cdd:PLN02918 320 CVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNG 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  375 FVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYD 454
Cdd:PLN02918 400 FVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQ 479

                        490
                 ....*....|..
gi 42573644  455 EYEELTKQYSDG 466
Cdd:PLN02918 480 EYKELEKKYSDG 491
 
Name Accession Description Interval E-value
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 4-466 0e+00

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 903.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644    4 VIRRVTTMTFTFLLQSPPLPISP-SPPQFSLSSSPLSKTQRFITPSQG----SRLRTLCTKV-------------IIPNM 65
Cdd:PLN02918   1 NIKSTATMTFTFLLQSLLPLPISpPPPHSSSLSSSPSPTQRFLTPSQGsrlpPRRRALCTKSqdprwrramaslaVIPNM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   66 QDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHH 145
Cdd:PLN02918  81 QDSGSPPLSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  146 FGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 225
Cdd:PLN02918 161 FGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  226 QTLqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDML-----------RFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSM 294
Cdd:PLN02918 241 QTL-KHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLvsltapklcakKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSM 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  295 CVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENG 374
Cdd:PLN02918 320 CVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNG 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  375 FVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYD 454
Cdd:PLN02918 400 FVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQ 479

                        490
                 ....*....|..
gi 42573644  455 EYEELTKQYSDG 466
Cdd:PLN02918 480 EYKELEKKYSDG 491
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 305-466 5.93e-84

Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440029  Cd Length: 212  Bit Score: 257.04  E-value: 5.93e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644 305 DISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESK 384
Cdd:COG0259   3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644 385 KGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYS 464
Cdd:COG0259  83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFA 162


                ..
gi 42573644 465 DG 466
Cdd:COG0259 163 GG 164
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 326-466 4.08e-81

pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273138  Cd Length: 190  Bit Score: 248.95  E-value: 4.08e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   326 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 405
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42573644   406 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDG 466
Cdd:TIGR00558  81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDG 141
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 97-259 2.11e-36

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 131.97  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644    97 DQLMELAGLSVAASIAEVYKPEEySRVLAICGPGNNGGDGLVAARHLHHFGYK--PFICYPkrtaKPLYTGLV-TQLDSL 173
Cdd:pfam03853   2 AVLMENAGRAAARVLKALLSPAG-PKVLILCGPGNNGGDGLAAARHLANRGAKvtVLLLGP----EEKLSEDArRQLDLF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   174 S------VPFVSVEDLPDDLSkDFDVIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeqtLQKHPVIVSVDIPSGWHVEE 247
Cdd:pfam03853  77 KklggkiVTDNPDEDLEKLLS-PVDLIIDALLGTGLSGPLRGEYAALIEWI---------NQSGAPVLAVDIPSGLDADT 146

                         170
                  ....*....|..
gi 42573644   248 GDHEDGGIKPDM 259
Cdd:pfam03853 147 GAVLGTAVRADH 158
 
Name Accession Description Interval E-value
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 4-466 0e+00

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 903.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644    4 VIRRVTTMTFTFLLQSPPLPISP-SPPQFSLSSSPLSKTQRFITPSQG----SRLRTLCTKV-------------IIPNM 65
Cdd:PLN02918   1 NIKSTATMTFTFLLQSLLPLPISpPPPHSSSLSSSPSPTQRFLTPSQGsrlpPRRRALCTKSqdprwrramaslaVIPNM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   66 QDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHH 145
Cdd:PLN02918  81 QDSGSPPLSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  146 FGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 225
Cdd:PLN02918 161 FGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  226 QTLqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDML-----------RFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSM 294
Cdd:PLN02918 241 QTL-KHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLvsltapklcakKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSM 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  295 CVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENG 374
Cdd:PLN02918 320 CVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNG 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  375 FVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYD 454
Cdd:PLN02918 400 FVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQ 479

                        490
                 ....*....|..
gi 42573644  455 EYEELTKQYSDG 466
Cdd:PLN02918 480 EYKELEKKYSDG 491
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 60-466 0e+00

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 728.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   60 VIIPNMQDSGSppLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVA 139
Cdd:PLN03049   1 VAVQHLHNPDS--ISYLSQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSPSEYRRVLALCGPGNNGGDGLVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  140 ARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLV 219
Cdd:PLN03049  79 ARHLHHFGYKPSICYPKRTDKPLYNGLVTQLESLSVPFLSVEDLPSDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKLV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  220 SLQNyeqtlqkHPVIVSVDIPSGWHVEEGDHEDGGIKPDML-----------RFRGPHHFLGGRFVPPSVAEKYKLELPS 288
Cdd:PLN03049 159 RAAG-------PPPIVSVDIPSGWHVEEGDVNGEGLKPDMLvsltapklcakMFKGPHHFLGGRFVPPAIVEKFKLHLPP 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  289 YPGTSMCVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLK 368
Cdd:PLN03049 232 YPGTSMCVRIGKTPSVDIAALRENYVGPELLEEQVNADPIDQFKEWFDDAVAAGLREPNAMTLATAGEDGRPSARIVLLK 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  369 GFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPG 448
Cdd:PLN03049 312 GVDKRGFVWYTNYDSRKAHELSANPKASLVFYWDGLHRQVRVEGSVEKVSEEESDQYFHSRPRGSQIGALVSKQSTVIPG 391

                        410
                 ....*....|....*...
gi 42573644  449 RHVLYDEYEELTKQYSDG 466
Cdd:PLN03049 392 RHILDQSYKELEAKYADS 409
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 65-298 1.31e-102

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 306.42  E-value: 1.31e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   65 MQDSGsppLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYK-------PEEYSRVLAICGPGNNGGDGL 137
Cdd:PLN03050   1 MSNIQ---TGYLNAQDAAALDEELMSTPGFSLEQLMELAGLSVAEAVYEVADgekasnpPGRHPRVLLVCGPGNNGGDGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  138 VAARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSV----EDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDD 213
Cdd:PLN03050  78 VAARHLAHFGYEVTVCYPKQSSKPHYENLVTQCEDLGIPFVQAiggtNDSSKPLETTYDVIVDAIFGFSFHGAPRAPFDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  214 LIRRLVSLQNyeqtlqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDML-----------RFRGpHHFLGGRFVPPSVAEKY 282
Cdd:PLN03050 158 LLAQMVQQQK------SPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLvsltapklsakKFEG-RHFVGGRFLPPAIAEKY 230

                        250
                 ....*....|....*.
gi 42573644  283 KLELPSYPGTSMCVRI 298
Cdd:PLN03050 231 GLQKPPYPGVSQVMEV 246
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 305-466 5.93e-84

Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440029  Cd Length: 212  Bit Score: 257.04  E-value: 5.93e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644 305 DISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESK 384
Cdd:COG0259   3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644 385 KGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYS 464
Cdd:COG0259  83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFA 162


                ..
gi 42573644 465 DG 466
Cdd:COG0259 163 GG 164
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 326-466 4.08e-81

pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273138  Cd Length: 190  Bit Score: 248.95  E-value: 4.08e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   326 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 405
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42573644   406 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDG 466
Cdd:TIGR00558  81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDG 141
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
320-466 1.53e-70

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 222.02  E-value: 1.53e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  320 EEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLF 399
Cdd:PRK05679   1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573644  400 YWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDG 466
Cdd:PRK05679  81 PWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFAQG 147
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 76-259 3.21e-39

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: 148.09  E-value: 3.21e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  76 LTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYkPEEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFICYP 155
Cdd:COG0062   4 LTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRF-PSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644 156 KRTAKplYTGL----VTQLDSLSVPFVSVEDLPDDLSkDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYeqtlqkh 231
Cdd:COG0062  83 GDPEK--LSGDaaanLERLKAAGIPILELDDELPELA-EADLIVDALFGTGLSRPLRGPYAELIEAINASGAP------- 152

                       170       180
                ....*....|....*....|....*...
gi 42573644 232 pvIVSVDIPSGWHVEEGDHEDGGIKPDM 259
Cdd:COG0062 153 --VLAVDIPSGLDADTGEVLGAAVRADL 178
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 81-276 1.52e-38

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: 138.70  E-value: 1.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644    81 AAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEysRVLAICGPGNNGGDGLVAARHLHhfGYKPFICYPKRTAK 160
Cdd:TIGR00197   8 DMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAG--HVIIFCGPGNNGGDGFVVARHLK--GFGVEVFLLKKEKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   161 -PLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIrrlvslqnyeQTLQKHPV-IVSVD 238
Cdd:TIGR00197  84 iECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIV----------ESINELPApIVSVD 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42573644   239 IPSGWHVEEGDHEDGGIKPD-----------MLRFRGPH---HFLGGRFVPP 276
Cdd:TIGR00197 154 IPSGLDVDTGAIEGPAVNADltitfhaikpcLLSDRADVtgeLKVGGIGIPP 205
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 97-259 2.11e-36

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 131.97  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644    97 DQLMELAGLSVAASIAEVYKPEEySRVLAICGPGNNGGDGLVAARHLHHFGYK--PFICYPkrtaKPLYTGLV-TQLDSL 173
Cdd:pfam03853   2 AVLMENAGRAAARVLKALLSPAG-PKVLILCGPGNNGGDGLAAARHLANRGAKvtVLLLGP----EEKLSEDArRQLDLF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   174 S------VPFVSVEDLPDDLSkDFDVIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeqtLQKHPVIVSVDIPSGWHVEE 247
Cdd:pfam03853  77 KklggkiVTDNPDEDLEKLLS-PVDLIIDALLGTGLSGPLRGEYAALIEWI---------NQSGAPVLAVDIPSGLDADT 146

                         170
                  ....*....|..
gi 42573644   248 GDHEDGGIKPDM 259
Cdd:pfam03853 147 GAVLGTAVRADH 158
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 335-421 5.02e-26

Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family members were predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, such as Swiss:Q06199 and its paralogs, do not possess this activity, nor do they bind to flavin mononucleotide (FMN). To date, the only time functional oxidase activity has been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. Moreover, some of the family members that contain both domains have been shown to be involved in phenazine biosynthesis. While some molecular function has been experimentally validated for the proteins containing both domains, the role performed by each domain on its own is unknown.


Pssm-ID: 426149 [Multi-domain]  Cd Length: 88  Bit Score: 101.17  E-value: 5.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   335 FDEAVAAGLRETNAMALSTANKDKKPSSRMVLLK-GFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGP 413
Cdd:pfam01243   1 LTEEIREFLAEPNAVVLATVDKDGRPNVRPVGLKyGFDTVGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGT 80


                  ....*...
gi 42573644   414 VERIPESE 421
Cdd:pfam01243  81 AEIVTDGE 88
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 72-248 6.99e-12

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 67.39  E-value: 6.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644   72 PLSYLTQREAAEIDEtlmgpLGFSIDQLMELAGLSvAASIAEVYKPEEySRVLAICGPGNNGGDGLVAARhlhhfgykpf 151
Cdd:PRK10565  19 PADDIRRGEREAADA-----LGLTLYELMLRAGEA-AFQVARSAYPDA-RHWLVLCGHGNNGGDGYVVAR---------- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644  152 icypkrtakplytglVTQLDSLSVPFVSVED---LPDD---------------------LSKDFDVIVDAMFGFSFHGAP 207
Cdd:PRK10565  82 ---------------LAQAAGIDVTLLAQESdkpLPEEaalareawlnaggeihaadivWPESVDLIVDALLGTGLRQAP 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 42573644  208 RPPFDDLIRRlvslqnyeqtLQKHPV-IVSVDIPSGWHVEEG 248
Cdd:PRK10565 147 REPYAALIDQ----------ANAHPApVVALDIPSGLLAETG 178
YzzA COG3871
General stress protein 26 (function unknown) [Function unknown];
337-417 7.16e-04

General stress protein 26 (function unknown) [Function unknown];


Pssm-ID: 443080 [Multi-domain]  Cd Length: 132  Bit Score: 39.53  E-value: 7.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573644 337 EAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWF-TNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVE 415
Cdd:COG3871   9 EKLWELLEDIRTAMLATVDADGRPHSRPMWFQVDVDDGTLWFfTSRDSAKVRNIRRDPRVSLSFADPGDDRYVSVEGTAE 88


                ..
gi 42573644 416 RI 417
Cdd:COG3871  89 IV 90
 
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