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Conserved domains on  [gi|1153867282|ref|WP_078388321|]
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MULTISPECIES: pyridoxamine 5'-phosphate oxidase [Acinetobacter]

Protein Classification

pyridoxal 5'-phosphate synthase( domain architecture ID 11415719)

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 COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 7-218 8.39e-105

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: 300.96  E-value: 8.39e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282   7 DLSELRLSYQKGELREDRVETNPHTQFLLWFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQ 86
Cdd:COG0259     3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  87 KGNDLAENPYAELLFYWQEQERQIRIGGKVVKISEAESTDYYHKRPRDSQIAAHIStPQSGVIESREVLQQRFEQLQSQV 166
Cdd:COG0259    83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWAS-PQSQPIASREELEARFAELEARF 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1153867282 167 EGKsELNKPLFWGGYRIEPDYYEFWQGRPNRLHDRLSYEKQQDVWMLKRLMP 218
Cdd:COG0259   162 AGG-DVPRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGGWTIERLAP 212
 
Name Accession Description Interval E-value
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 7-218 8.39e-105

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: 300.96  E-value: 8.39e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282   7 DLSELRLSYQKGELREDRVETNPHTQFLLWFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQ 86
Cdd:COG0259     3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  87 KGNDLAENPYAELLFYWQEQERQIRIGGKVVKISEAESTDYYHKRPRDSQIAAHIStPQSGVIESREVLQQRFEQLQSQV 166
Cdd:COG0259    83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWAS-PQSQPIASREELEARFAELEARF 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1153867282 167 EGKsELNKPLFWGGYRIEPDYYEFWQGRPNRLHDRLSYEKQQDVWMLKRLMP 218
Cdd:COG0259   162 AGG-DVPRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGGWTIERLAP 212
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 28-218 2.02e-102

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: 294.02  E-value: 2.02e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  28 NPHTQFLLWFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQKGNDLAENPYAELLFYWQEQE 107
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282 108 RQIRIGGKVVKISEAESTDYYHKRPRDSQIAAHIStPQSGVIESREVLQQRFEQLQSQVEGKsELNKPLFWGGYRIEPDY 187
Cdd:TIGR00558  81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWAS-QQSRPIASREELEARFAELKARFPDG-EVPRPEFWGGYRVVPDE 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1153867282 188 YEFWQGRPNRLHDRLSYEKQQD-VWMLKRLMP 218
Cdd:TIGR00558 159 IEFWQGRPSRLHDRFRYRRDGDgSWRIERLAP 190
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
22-218 6.66e-85

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 249.75  E-value: 6.66e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  22 EDRVETNPHTQFLLWFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQKGNDLAENPYAELLF 101
Cdd:PRK05679    1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282 102 YWQEQERQIRIGGKVVKISEAESTDYYHKRPRDSQIAAHIStPQSGVIESREVLQQRFEQLQSQVEGKsELNKPLFWGGY 181
Cdd:PRK05679   81 PWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWAS-KQSRPISSRAALEAKFAEVKAKFAQG-EVPRPPHWGGY 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1153867282 182 RIEPDYYEFWQGRPNRLHDRLSYEKQQDVWMLKRLMP 218
Cdd:PRK05679  159 RVVPESIEFWQGRPSRLHDRILYRRDDGGWKIERLAP 195
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
36-218 6.35e-49

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 158.68  E-value: 6.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  36 WFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQKGNDLAENPYAELLFYWQEQERQIRIGGK 115
Cdd:NF038138   27 WLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRETSQQISLSGP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282 116 VVKISEAESTDYYHKRPrdsqIAAHISTP---QSGVIESREVLQQRFEQLqsqVEGKSELNKPLFWGGYRIEPDYYEFWQ 192
Cdd:NF038138  107 VERLPDAESDALWAARP----VATHAMTAasrQSEPLDDEAALRAEAREL---AEAGGPLPRPARFVGYRLVPEEVEFWA 179

                         170       180
                  ....*....|....*....|....*.
gi 1153867282 193 GRPNRLHDRLSYEKQQDVWMLKRLMP 218
Cdd:NF038138  180 AGPDRLHRRLRYDRDGDGWTHVRLQP 205
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 37-123 4.23e-25

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: 93.85  E-value: 4.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  37 FNHALEAQLHEPYAMSLATATAQGRPHVRTVLL-RGATEAGYDFYTNYDSQKGNDLAENPYAELLFYWQEQERQIRIGGK 115
Cdd:pfam01243   1 LTEEIREFLAEPNAVVLATVDKDGRPNVRPVGLkYGFDTVGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGT 80


                  ....*...
gi 1153867282 116 VVKISEAE 123
Cdd:pfam01243  81 AEIVTDGE 88
 
Name Accession Description Interval E-value
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 7-218 8.39e-105

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: 300.96  E-value: 8.39e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282   7 DLSELRLSYQKGELREDRVETNPHTQFLLWFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQ 86
Cdd:COG0259     3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  87 KGNDLAENPYAELLFYWQEQERQIRIGGKVVKISEAESTDYYHKRPRDSQIAAHIStPQSGVIESREVLQQRFEQLQSQV 166
Cdd:COG0259    83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWAS-PQSQPIASREELEARFAELEARF 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1153867282 167 EGKsELNKPLFWGGYRIEPDYYEFWQGRPNRLHDRLSYEKQQDVWMLKRLMP 218
Cdd:COG0259   162 AGG-DVPRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGGWTIERLAP 212
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 28-218 2.02e-102

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: 294.02  E-value: 2.02e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  28 NPHTQFLLWFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQKGNDLAENPYAELLFYWQEQE 107
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282 108 RQIRIGGKVVKISEAESTDYYHKRPRDSQIAAHIStPQSGVIESREVLQQRFEQLQSQVEGKsELNKPLFWGGYRIEPDY 187
Cdd:TIGR00558  81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWAS-QQSRPIASREELEARFAELKARFPDG-EVPRPEFWGGYRVVPDE 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1153867282 188 YEFWQGRPNRLHDRLSYEKQQD-VWMLKRLMP 218
Cdd:TIGR00558 159 IEFWQGRPSRLHDRFRYRRDGDgSWRIERLAP 190
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
22-218 6.66e-85

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 249.75  E-value: 6.66e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  22 EDRVETNPHTQFLLWFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQKGNDLAENPYAELLF 101
Cdd:PRK05679    1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282 102 YWQEQERQIRIGGKVVKISEAESTDYYHKRPRDSQIAAHIStPQSGVIESREVLQQRFEQLQSQVEGKsELNKPLFWGGY 181
Cdd:PRK05679   81 PWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWAS-KQSRPISSRAALEAKFAEVKAKFAQG-EVPRPPHWGGY 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1153867282 182 RIEPDYYEFWQGRPNRLHDRLSYEKQQDVWMLKRLMP 218
Cdd:PRK05679  159 RVVPESIEFWQGRPSRLHDRILYRRDDGGWKIERLAP 195
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 7-218 7.59e-80

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 245.92  E-value: 7.59e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282   7 DLSELRLSYQKGELREDRVETNPHTQFLLWFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQ 86
Cdd:PLN03049  248 DIAALRENYVGPELLEEQVNADPIDQFKEWFDDAVAAGLREPNAMTLATAGEDGRPSARIVLLKGVDKRGFVWYTNYDSR 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  87 KGNDLAENPYAELLFYWQEQERQIRIGGKVVKISEAESTDYYHKRPRDSQIAAHISTpQSGVIESREVLQQRFEQLQSQV 166
Cdd:PLN03049  328 KAHELSANPKASLVFYWDGLHRQVRVEGSVEKVSEEESDQYFHSRPRGSQIGALVSK-QSTVIPGRHILDQSYKELEAKY 406

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1153867282 167 EGKSELNKPLFWGGYRIEPDYYEFWQGRPNRLHDRLSYEKQ----QDVWMLKRLMP 218
Cdd:PLN03049  407 ADSSAIPKPKHWGGYRLKPELIEFWQGRESRLHDRLQYTREeingKSVWKIDRLAP 462
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 7-218 4.01e-79

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 246.39  E-value: 4.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282   7 DLSELRLSYQKGELREDRVETNPHTQFLLWFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQ 86
Cdd:PLN02918  330 DISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNGFVWYTNYESQ 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  87 KGNDLAENPYAELLFYWQEQERQIRIGGKVVKISEAESTDYYHKRPRDSQIAAhISTPQSGVIESREVLQQRFEQLQSQV 166
Cdd:PLN02918  410 KGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGA-IVSKQSSVVPGRHVLYQEYKELEKKY 488

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1153867282 167 EGKSELNKPLFWGGYRIEPDYYEFWQGRPNRLHDRLSYEKQQ----DVWMLKRLMP 218
Cdd:PLN02918  489 SDGSVIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYSLQEvngkPVWKIHRLAP 544
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
36-218 6.35e-49

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 158.68  E-value: 6.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  36 WFNHALEAQLHEPYAMSLATATAQGRPHVRTVLLRGATEAGYDFYTNYDSQKGNDLAENPYAELLFYWQEQERQIRIGGK 115
Cdd:NF038138   27 WLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRETSQQISLSGP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282 116 VVKISEAESTDYYHKRPrdsqIAAHISTP---QSGVIESREVLQQRFEQLqsqVEGKSELNKPLFWGGYRIEPDYYEFWQ 192
Cdd:NF038138  107 VERLPDAESDALWAARP----VATHAMTAasrQSEPLDDEAALRAEAREL---AEAGGPLPRPARFVGYRLVPEEVEFWA 179

                         170       180
                  ....*....|....*....|....*.
gi 1153867282 193 GRPNRLHDRLSYEKQQDVWMLKRLMP 218
Cdd:NF038138  180 AGPDRLHRRLRYDRDGDGWTHVRLQP 205
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 37-123 4.23e-25

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: 93.85  E-value: 4.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  37 FNHALEAQLHEPYAMSLATATAQGRPHVRTVLL-RGATEAGYDFYTNYDSQKGNDLAENPYAELLFYWQEQERQIRIGGK 115
Cdd:pfam01243   1 LTEEIREFLAEPNAVVLATVDKDGRPNVRPVGLkYGFDTVGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGT 80


                  ....*...
gi 1153867282 116 VVKISEAE 123
Cdd:pfam01243  81 AEIVTDGE 88
PNP_phzG_C pfam10590
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of ...
 178-218 5.64e-18

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: 74.08  E-value: 5.64e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1153867282 178 WGGYRIEPDYYEFWQGRPNRLHDRLSYEKQQD-VWMLKRLMP 218
Cdd:pfam10590   1 WGGYRLVPEEIEFWQGRPSRLHDRIRYTREGDgGWTIERLAP 42
COG5135 COG5135
Uncharacterized conserved protein [Function unknown];
39-124 3.38e-13

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 444058  Cd Length: 193  Bit Score: 65.36  E-value: 3.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  39 HALEAQLHEPYA--MSLATATAQGRPHVRTVLLRGATEAGY--DFYTNYDSQKGNDLAENPYAELLFYWQEQERQIRIGG 114
Cdd:COG5135    11 RALHRNRSPPYSryLQLATVTGDGRPANRTVVFRGFLEDSNqlKFITDARSEKVDQIQQQPWAEICWYFPKTREQFRLSG 90

                          90
                  ....*....|
gi 1153867282 115 KVVKISEAES 124
Cdd:COG5135    91 KLTLVTADDP 100
Pyridox_oxase_2 pfam12766
Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase catalyzes the oxidation ...
 37-120 7.71e-11

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: 56.87  E-value: 7.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153867282  37 FNHALEAQLHEPYA--MSLAT-ATAQGRPHVRTVLLRGATEAGY-----DFYTNYDSQKGNDLAENPYAELLFYWQEQER 108
Cdd:pfam12766   8 LESALSNNRKLPPStyFQLATvDPPEGRPRVRTVVFRGFLFNDYesdvlTFTTDVRSEKVEQLEGNPAFEACFWFPKTRE 87

                          90
                  ....*....|..
gi 1153867282 109 QIRIGGKVVKIS 120
Cdd:pfam12766  88 QFRIRGTAFVIG 99
PPOX_FMN_cyano TIGR04026
PPOX class probable FMN-dependent enzyme, alr4036 family; Members of the PPOX family (see ...
 53-124 6.91e-09

PPOX class probable FMN-dependent enzyme, alr4036 family; Members of the PPOX family (see pfam01243) may contain either FMN or F420 as cofactor. This subfamily described here is widespread in Cyanobacteria and plants, and is named for alr4036 from Nostoc sp. PCC 7120. The family consists mostly of proteins from species that lack the capability to synthesize F420, so it is probable that all members bind FMN rather than F420. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274927  Cd Length: 185  Bit Score: 53.47  E-value: 6.91e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1153867282  53 LATATAQGRPHVRTVLLRGATEAG-YDFYTNYDSQKGNDLAENPYAELLFYWQEQERQIRIGGKVVKISEAES 124
Cdd:TIGR04026  26 LATVTSDGTPRNRTVVFRGWEDSNqLELITDSRSEKIEQLAQNPAAEICWYFPKTREQFRLRGKATLVTADDS 98
COG5015 COG5015
Pyridoxamine 5'-phosphate oxidase (PNPOx-like) family protein [General function prediction ...
 53-123 1.53e-05

Pyridoxamine 5'-phosphate oxidase (PNPOx-like) family protein [General function prediction only];


Pssm-ID: 444039 [Multi-domain]  Cd Length: 130  Bit Score: 42.90  E-value: 1.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1153867282  53 LATaTAQGRPHVRTVLLRGATEAGYDFYTNydSQKG--NDLAENPYAELLFYWQEQErQIRIGGKVVKISEAE 123
Cdd:COG5015    15 LAT-VDGGQPRVRPFGFVFEDEGKLYFCTS--NQKDvyKQLKANPKVEICAMKKDGE-WIRLSGKAVFVDDRE 83
YzzA COG3871
General stress protein 26 (function unknown) [Function unknown];
49-101 6.03e-05

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


Pssm-ID: 443080 [Multi-domain]  Cd Length: 132  Bit Score: 41.46  E-value: 6.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1153867282  49 YAMsLATATAQGRPHVRTVLLRGATEAG--YdFYTNYDSQKGNDLAENPYAELLF 101
Cdd:COG3871    20 TAM-LATVDADGRPHSRPMWFQVDVDDGtlW-FFTSRDSAKVRNIRRDPRVSLSF 72
 
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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