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Conserved domains on  [gi|21430394|gb|AAM50875|]
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LP04163p [Drosophila melanogaster]

Protein Classification

pyridoxal 5'-phosphate synthase( domain architecture ID 11489231)

pyridoxal 5'-phosphate synthase catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 42-246 1.64e-96

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: 280.15  E-value: 1.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394    42 NPFCVFRDWLELALKTpEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNYGSRKAEDIKSNPYVAISFYWLPL 121
Cdd:TIGR00558   1 DPIEQFERWFEEAIEA-ELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   122 RRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVEAAIKLELgPDGEVPLP-NWGGYLVRPDL 200
Cdd:TIGR00558  80 ERQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARF-PDGEVPRPeFWGGYRVVPDE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 21430394   201 IEFWQGQTDRLHDRIRFRRgggvesevdsklvhKGEDGWVYERLAP 246
Cdd:TIGR00558 159 IEFWQGRPSRLHDRFRYRR--------------DGDGSWRIERLAP 190
 
Name Accession Description Interval E-value
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 42-246 1.64e-96

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: 280.15  E-value: 1.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394    42 NPFCVFRDWLELALKTpEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNYGSRKAEDIKSNPYVAISFYWLPL 121
Cdd:TIGR00558   1 DPIEQFERWFEEAIEA-ELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   122 RRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVEAAIKLELgPDGEVPLP-NWGGYLVRPDL 200
Cdd:TIGR00558  80 ERQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARF-PDGEVPRPeFWGGYRVVPDE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 21430394   201 IEFWQGQTDRLHDRIRFRRgggvesevdsklvhKGEDGWVYERLAP 246
Cdd:TIGR00558 159 IEFWQGRPSRLHDRFRYRR--------------DGDGSWRIERLAP 190
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 19-246 1.41e-95

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: 278.61  E-value: 1.41e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394  19 LSALRLKYceRKDAFLEDNIKvKNPFCVFRDWLELALKTpEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNY 98
Cdd:COG0259   4 LADLRREY--TKGGLDESDLP-ADPLALFARWLEEAEAA-GVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394  99 GSRKAEDIKSNPYVAISFYWLPLRRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVEAAIKL 178
Cdd:COG0259  80 ESRKGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEA 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21430394 179 ELgPDGEVPLP-NWGGYLVRPDLIEFWQGQTDRLHDRIRFRRGGGvesevdsklvhkgedGWVYERLAP 246
Cdd:COG0259 160 RF-AGGDVPRPpHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDG---------------GWTIERLAP 212
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
42-246 5.84e-87

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 256.30  E-value: 5.84e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   42 NPFCVFRDWLELALKTpEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNYGSRKAEDIKSNPYVAISFYWLPL 121
Cdd:PRK05679   7 EPLALFERWLAEAVKA-ELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLFPWKSL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394  122 RRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVEAAIKLELGpDGEVPLP-NWGGYLVRPDL 200
Cdd:PRK05679  86 ERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFA-QGEVPRPpHWGGYRVVPES 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 21430394  201 IEFWQGQTDRLHDRIRFRRGGGvesevdsklvhkgedGWVYERLAP 246
Cdd:PRK05679 165 IEFWQGRPSRLHDRILYRRDDG---------------GWKIERLAP 195
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
42-246 1.57e-46

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 153.67  E-value: 1.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   42 NPFCVFRDWLELAlKTPEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNYGSRKAEDIKSNPYVAISFYWLPL 121
Cdd:NF038138  19 EPLGLLRRWLEAA-VALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRET 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394  122 RRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRipsrsyLDDVEA--AIKLELGPDGEvPLP---NWGGYLV 196
Cdd:NF038138  98 SQQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEP------LDDEAAlrAEARELAEAGG-PLPrpaRFVGYRL 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 21430394  197 RPDLIEFWQGQTDRLHDRIRFRRGGgvesevdsklvhkgeDGWVYERLAP 246
Cdd:NF038138 171 VPEEVEFWAAGPDRLHRRLRYDRDG---------------DGWTHVRLQP 205
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 59-135 5.02e-24

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: 91.93  E-value: 5.02e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21430394    59 EILEPNAAALATVSAEGRPSNRYVLVKEATAE-GFTFFTNYGSRKAEDIKSNPYVAISFYWLPLRRSVRIEGVAEKIS 135
Cdd:pfam01243   8 FLAEPNAVVLATVDKDGRPNVRPVGLKYGFDTvGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGTAEIVT 85
 
Name Accession Description Interval E-value
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 42-246 1.64e-96

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: 280.15  E-value: 1.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394    42 NPFCVFRDWLELALKTpEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNYGSRKAEDIKSNPYVAISFYWLPL 121
Cdd:TIGR00558   1 DPIEQFERWFEEAIEA-ELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   122 RRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVEAAIKLELgPDGEVPLP-NWGGYLVRPDL 200
Cdd:TIGR00558  80 ERQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARF-PDGEVPRPeFWGGYRVVPDE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 21430394   201 IEFWQGQTDRLHDRIRFRRgggvesevdsklvhKGEDGWVYERLAP 246
Cdd:TIGR00558 159 IEFWQGRPSRLHDRFRYRR--------------DGDGSWRIERLAP 190
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 19-246 1.41e-95

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: 278.61  E-value: 1.41e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394  19 LSALRLKYceRKDAFLEDNIKvKNPFCVFRDWLELALKTpEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNY 98
Cdd:COG0259   4 LADLRREY--TKGGLDESDLP-ADPLALFARWLEEAEAA-GVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394  99 GSRKAEDIKSNPYVAISFYWLPLRRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVEAAIKL 178
Cdd:COG0259  80 ESRKGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEA 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21430394 179 ELgPDGEVPLP-NWGGYLVRPDLIEFWQGQTDRLHDRIRFRRGGGvesevdsklvhkgedGWVYERLAP 246
Cdd:COG0259 160 RF-AGGDVPRPpHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDG---------------GWTIERLAP 212
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
42-246 5.84e-87

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 256.30  E-value: 5.84e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   42 NPFCVFRDWLELALKTpEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNYGSRKAEDIKSNPYVAISFYWLPL 121
Cdd:PRK05679   7 EPLALFERWLAEAVKA-ELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLFPWKSL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394  122 RRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVEAAIKLELGpDGEVPLP-NWGGYLVRPDL 200
Cdd:PRK05679  86 ERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFA-QGEVPRPpHWGGYRVVPES 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 21430394  201 IEFWQGQTDRLHDRIRFRRGGGvesevdsklvhkgedGWVYERLAP 246
Cdd:PRK05679 165 IEFWQGRPSRLHDRILYRRDDG---------------GWKIERLAP 195
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 14-246 1.26e-72

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 228.58  E-value: 1.26e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   14 ASEVPLSALRLKYCERKdaFLEDNIKvKNPFCVFRDWLELALkTPEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFT 93
Cdd:PLN03049 244 TPSVDIAALRENYVGPE--LLEEQVN-ADPIDQFKEWFDDAV-AAGLREPNAMTLATAGEDGRPSARIVLLKGVDKRGFV 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   94 FFTNYGSRKAEDIKSNPYVAISFYWLPLRRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVE 173
Cdd:PLN03049 320 WYTNYDSRKAHELSANPKASLVFYWDGLHRQVRVEGSVEKVSEEESDQYFHSRPRGSQIGALVSKQSTVIPGRHILDQSY 399

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21430394  174 AAIKLELGPDGEVPLP-NWGGYLVRPDLIEFWQGQTDRLHDRIRFRRgggveSEVDSKLVhkgedgWVYERLAP 246
Cdd:PLN03049 400 KELEAKYADSSAIPKPkHWGGYRLKPELIEFWQGRESRLHDRLQYTR-----EEINGKSV------WKIDRLAP 462
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 14-246 2.81e-58

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 193.23  E-value: 2.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   14 ASEVPLSALRLKYCERKdaFLEDNIKVkNPFCVFRDWLELALkTPEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFT 93
Cdd:PLN02918 326 PPSVDISALRENYISPE--LLEEQVET-DPTDQFRKWFDEAV-AAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNGFV 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   94 FFTNYGSRKAEDIKSNPYVAISFYWLPLRRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVE 173
Cdd:PLN02918 402 WYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQEY 481

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21430394  174 AAIKLELGPDGEVPLP-NWGGYLVRPDLIEFWQGQTDRLHDRIRFrrgggVESEVDSKLVhkgedgWVYERLAP 246
Cdd:PLN02918 482 KELEKKYSDGSVIPKPkNWGGYRLKPNLFEFWQGQQSRLHDRLQY-----SLQEVNGKPV------WKIHRLAP 544
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
42-246 1.57e-46

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 153.67  E-value: 1.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394   42 NPFCVFRDWLELAlKTPEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNYGSRKAEDIKSNPYVAISFYWLPL 121
Cdd:NF038138  19 EPLGLLRRWLEAA-VALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRET 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394  122 RRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRipsrsyLDDVEA--AIKLELGPDGEvPLP---NWGGYLV 196
Cdd:NF038138  98 SQQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEP------LDDEAAlrAEARELAEAGG-PLPrpaRFVGYRL 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 21430394  197 RPDLIEFWQGQTDRLHDRIRFRRGGgvesevdsklvhkgeDGWVYERLAP 246
Cdd:NF038138 171 VPEEVEFWAAGPDRLHRRLRYDRDG---------------DGWTHVRLQP 205
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 59-135 5.02e-24

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: 91.93  E-value: 5.02e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21430394    59 EILEPNAAALATVSAEGRPSNRYVLVKEATAE-GFTFFTNYGSRKAEDIKSNPYVAISFYWLPLRRSVRIEGVAEKIS 135
Cdd:pfam01243   8 FLAEPNAVVLATVDKDGRPNVRPVGLKYGFDTvGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGTAEIVT 85
PNP_phzG_C pfam10590
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of ...
 191-246 3.84e-20

Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of the two dimerization regions of the protein, located at the edge of the dimer interface, at the C-terminus, being the last three beta strands, S6, S7, and S8 along with the last three residues to the end. In Swiss:P21159, S6 runs from residues 178-192, S7 from 200-206 and S8 from 211-215. the extended loop, of residues 167-177 may well be involved in the pocket formed between the two dimers that positions the FMN molecule.To date, the only time functional oxidase or phenazine biosynthesis activities have been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. It is unknown the role performed by each domain in bringing about molecular functions of either oxidase or phenazine activity.


Pssm-ID: 463161  Cd Length: 42  Bit Score: 80.24  E-value: 3.84e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 21430394   191 WGGYLVRPDLIEFWQGQTDRLHDRIRFRRgggvesevdsklvhKGEDGWVYERLAP 246
Cdd:pfam10590   1 WGGYRLVPEEIEFWQGRPSRLHDRIRYTR--------------EGDGGWTIERLAP 42
YzzA COG3871
General stress protein 26 (function unknown) [Function unknown];
59-132 7.93e-09

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


Pssm-ID: 443080 [Multi-domain]  Cd Length: 132  Bit Score: 52.63  E-value: 7.93e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21430394  59 EILE-PNAAALATVSAEGRPSNRYVLVKEATAEG-FTFFTNYGSRKAEDIKSNPYVAISFYWLPLRRSVRIEGVAE 132
Cdd:COG3871  13 ELLEdIRTAMLATVDADGRPHSRPMWFQVDVDDGtLWFFTSRDSAKVRNIRRDPRVSLSFADPGDDRYVSVEGTAE 88
COG5135 COG5135
Uncharacterized conserved protein [Function unknown];
68-203 2.01e-06

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 444058  Cd Length: 193  Bit Score: 46.87  E-value: 2.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394  68 LATVSAEGRPSNRYVLVKeataeGFT-------FFTNYGSRKAEDIKSNPYVAISFYWLPLRRSVRIEGVAEKISVEDSL 140
Cdd:COG5135  27 LATVTGDGRPANRTVVFR-----GFLedsnqlkFITDARSEKVDQIQQQPWAEICWYFPKTREQFRLSGKLTLVTADDPD 101

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21430394 141 KYFHQ---------RPRASQIGAAASPQSQRipsrsylDDVEAAIKLELgPDGEVPLPNWGGYLVRPDLIEF 203
Cdd:COG5135 102 PDLQKarqqtwqelSDAARLQFAWPAPGAPR-------EEPEAAFSPPP-PDPDQPLPNFCLLLLEPDQVDH 165
Pyridox_oxase_2 pfam12766
Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase catalyzes the oxidation ...
 48-135 8.40e-04

Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase catalyzes the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP), the terminal step in the de novo biosynthesis of PLP in Escherichia coli and part of the salvage pathway of this coenzyme in both E. coli and mammalian cells. This region is the flavoprotein FMN-binding domain.


Pssm-ID: 432768 [Multi-domain]  Cd Length: 99  Bit Score: 37.61  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21430394    48 RDWLELALKTPEILEP-NAAALATV-SAEGRPSNRYV-----LVKEATAEGFTFFTNYGSRKAEDIKSNPYVAISFyWLP 120
Cdd:pfam12766   5 RPLLESALSNNRKLPPsTYFQLATVdPPEGRPRVRTVvfrgfLFNDYESDVLTFTTDVRSEKVEQLEGNPAFEACF-WFP 83

                          90
                  ....*....|....*.
gi 21430394   121 -LRRSVRIEGVAEKIS 135
Cdd:pfam12766  84 kTREQFRIRGTAFVIG 99
 
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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