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Conserved domains on  [gi|640465218|ref|WP_024909355|]
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MULTISPECIES: pyridoxamine 5'-phosphate oxidase [Enterobacter]

Protein Classification

pyridoxal 5'-phosphate synthase( domain architecture ID 11481478)

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

Gene Ontology:  GO:0010181|GO:0032991|GO:0016491|GO:0008615|GO:0042301|GO:0005829|GO:0042803|GO:1902444|GO:0036001|GO:0004733|GO:0042823
PubMed:  30891451

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
24-218 9.67e-135

pyridoxal 5'-phosphate synthase;


:

Pssm-ID: 235555  Cd Length: 195  Bit Score: 376.10  E-value: 9.67e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  24 RQDLPAEPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLVFYTNLGSRKAHHLENNPRISLLF 103
Cdd:PRK05679   1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218 104 PWHMLERQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKFLELKQKFQQGEIPLPSFWGGFRI 183
Cdd:PRK05679  81 PWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFAQGEVPRPPHWGGYRV 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 640465218 184 PIEQMEFWQGGEHRLHDRFLYQRENGGWKIDRLAP 218
Cdd:PRK05679 161 VPESIEFWQGRPSRLHDRILYRRDDGGWKIERLAP 195
 
Name Accession Description Interval E-value
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
24-218 9.67e-135

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 376.10  E-value: 9.67e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  24 RQDLPAEPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLVFYTNLGSRKAHHLENNPRISLLF 103
Cdd:PRK05679   1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218 104 PWHMLERQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKFLELKQKFQQGEIPLPSFWGGFRI 183
Cdd:PRK05679  81 PWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFAQGEVPRPPHWGGYRV 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 640465218 184 PIEQMEFWQGGEHRLHDRFLYQRENGGWKIDRLAP 218
Cdd:PRK05679 161 VPESIEFWQGRPSRLHDRILYRRDDGGWKIERLAP 195
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 1-218 3.72e-125

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: 352.19  E-value: 3.72e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218   1 MSDndelqqIAHLRREYTKGGLRRQDLPAEPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLV 80
Cdd:COG0259    1 MSD------LADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  81 FYTNLGSRKAHHLENNPRISLLFPWHMLERQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKF 160
Cdd:COG0259   75 FYTNYESRKGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARF 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 640465218 161 LELKQKFQQGEIPLPSFWGGFRIPIEQMEFWQGGEHRLHDRFLYQRENGGWKIDRLAP 218
Cdd:COG0259  155 AELEARFAGGDVPRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGGWTIERLAP 212
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 30-218 2.96e-120

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: 339.09  E-value: 2.96e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218   30 EPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLVFYTNLGSRKAHHLENNPRISLLFPWHMLE 109
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  110 RQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKFLELKQKFQQGEIPLPSFWGGFRIPIEQME 189
Cdd:TIGR00558  81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDGEVPRPEFWGGYRVVPDEIE 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 640465218  190 FWQGGEHRLHDRFLYQRENGG-WKIDRLAP 218
Cdd:TIGR00558 161 FWQGRPSRLHDRFRYRRDGDGsWRIERLAP 190
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
28-218 2.93e-48

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 157.14  E-value: 2.93e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  28 PAEPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLVFYTNLGSRKAHHLENNPRISLLFPWHM 107
Cdd:NF038138  17 PAEPLGLLRRWLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218 108 LERQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKFLELKQkfQQGEIPLPSFWGGFRIPIEQ 187
Cdd:NF038138  97 TSQQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAE--AGGPLPRPARFVGYRLVPEE 174

                        170       180       190
                 ....*....|....*....|....*....|.
gi 640465218 188 MEFWQGGEHRLHDRFLYQRENGGWKIDRLAP 218
Cdd:NF038138 175 VEFWAAGPDRLHRRLRYDRDGDGWTHVRLQP 205
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 39-122 3.02e-28

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: 101.94  E-value: 3.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218   39 LKQACEAKLADPTAMVVATVDENGQPYQRIVLLK-HYDEKGLVFYTNLGSRKAHHLENNPRISLLFPWHMLERQVMVTGK 117
Cdd:pfam01243   1 LTEEIREFLAEPNAVVLATVDKDGRPNVRPVGLKyGFDTVGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGT 80


                  ....*
gi 640465218  118 AERLS 122
Cdd:pfam01243  81 AEIVT 85
 
Name Accession Description Interval E-value
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
24-218 9.67e-135

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 376.10  E-value: 9.67e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  24 RQDLPAEPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLVFYTNLGSRKAHHLENNPRISLLF 103
Cdd:PRK05679   1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218 104 PWHMLERQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKFLELKQKFQQGEIPLPSFWGGFRI 183
Cdd:PRK05679  81 PWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFAQGEVPRPPHWGGYRV 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 640465218 184 PIEQMEFWQGGEHRLHDRFLYQRENGGWKIDRLAP 218
Cdd:PRK05679 161 VPESIEFWQGRPSRLHDRILYRRDDGGWKIERLAP 195
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 1-218 3.72e-125

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: 352.19  E-value: 3.72e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218   1 MSDndelqqIAHLRREYTKGGLRRQDLPAEPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLV 80
Cdd:COG0259    1 MSD------LADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  81 FYTNLGSRKAHHLENNPRISLLFPWHMLERQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKF 160
Cdd:COG0259   75 FYTNYESRKGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARF 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 640465218 161 LELKQKFQQGEIPLPSFWGGFRIPIEQMEFWQGGEHRLHDRFLYQRENGGWKIDRLAP 218
Cdd:COG0259  155 AELEARFAGGDVPRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGGWTIERLAP 212
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 30-218 2.96e-120

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: 339.09  E-value: 2.96e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218   30 EPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLVFYTNLGSRKAHHLENNPRISLLFPWHMLE 109
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  110 RQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKFLELKQKFQQGEIPLPSFWGGFRIPIEQME 189
Cdd:TIGR00558  81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDGEVPRPEFWGGYRVVPDEIE 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 640465218  190 FWQGGEHRLHDRFLYQRENGG-WKIDRLAP 218
Cdd:TIGR00558 161 FWQGRPSRLHDRFRYRRDGDGsWRIERLAP 190
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 10-218 4.71e-76

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 236.29  E-value: 4.71e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  10 IAHLRREYTKGGLRRQDLPAEPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLVFYTNLGSRK 89
Cdd:PLN03049 249 IAALRENYVGPELLEEQVNADPIDQFKEWFDDAVAAGLREPNAMTLATAGEDGRPSARIVLLKGVDKRGFVWYTNYDSRK 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  90 AHHLENNPRISLLFPWHMLERQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKFLELKQKFQQ 169
Cdd:PLN03049 329 AHELSANPKASLVFYWDGLHRQVRVEGSVEKVSEEESDQYFHSRPRGSQIGALVSKQSTVIPGRHILDQSYKELEAKYAD 408

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 640465218 170 GE-IPLPSFWGGFRIPIEQMEFWQGGEHRLHDRFLYQRENGG----WKIDRLAP 218
Cdd:PLN03049 409 SSaIPKPKHWGGYRLKPELIEFWQGRESRLHDRLQYTREEINgksvWKIDRLAP 462
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 10-218 3.08e-67

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 215.57  E-value: 3.08e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  10 IAHLRREYTKGGLRRQDLPAEPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLVFYTNLGSRK 89
Cdd:PLN02918 331 ISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNGFVWYTNYESQK 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  90 AHHLENNPRISLLFPWHMLERQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKFLELKQKFQQ 169
Cdd:PLN02918 411 GSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQEYKELEKKYSD 490

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 640465218 170 GE-IPLPSFWGGFRIPIEQMEFWQGGEHRLHDRFLY--QRENGG--WKIDRLAP 218
Cdd:PLN02918 491 GSvIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYslQEVNGKpvWKIHRLAP 544
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
28-218 2.93e-48

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 157.14  E-value: 2.93e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  28 PAEPLVLFERWLKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKGLVFYTNLGSRKAHHLENNPRISLLFPWHM 107
Cdd:NF038138  17 PAEPLGLLRRWLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218 108 LERQVMVTGKAERLSTLEVVKYFHSRPRDSQIGAWVSKQSSRISARGVLESKFLELKQkfQQGEIPLPSFWGGFRIPIEQ 187
Cdd:NF038138  97 TSQQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAE--AGGPLPRPARFVGYRLVPEE 174

                        170       180       190
                 ....*....|....*....|....*....|.
gi 640465218 188 MEFWQGGEHRLHDRFLYQRENGGWKIDRLAP 218
Cdd:NF038138 175 VEFWAAGPDRLHRRLRYDRDGDGWTHVRLQP 205
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 39-122 3.02e-28

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: 101.94  E-value: 3.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218   39 LKQACEAKLADPTAMVVATVDENGQPYQRIVLLK-HYDEKGLVFYTNLGSRKAHHLENNPRISLLFPWHMLERQVMVTGK 117
Cdd:pfam01243   1 LTEEIREFLAEPNAVVLATVDKDGRPNVRPVGLKyGFDTVGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGT 80


                  ....*
gi 640465218  118 AERLS 122
Cdd:pfam01243  81 AEIVT 85
PNP_phzG_C pfam10590
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of ...
 178-218 1.34e-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: 75.62  E-value: 1.34e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 640465218  178 WGGFRIPIEQMEFWQGGEHRLHDRFLYQRE-NGGWKIDRLAP 218
Cdd:pfam10590   1 WGGYRLVPEEIEFWQGRPSRLHDRIRYTREgDGGWTIERLAP 42
YzzA COG3871
General stress protein 26 (function unknown) [Function unknown];
39-119 3.36e-10

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


Pssm-ID: 443080 [Multi-domain]  Cd Length: 132  Bit Score: 56.10  E-value: 3.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  39 LKQACEAKLADPTAMVVATVDENGQPYQRIVLLKHYDEKG-LVFYTNLGSRKAHHLENNPRISLLF--PWHMleRQVMVT 115
Cdd:COG3871    7 LEEKLWELLEDIRTAMLATVDADGRPHSRPMWFQVDVDDGtLWFFTSRDSAKVRNIRRDPRVSLSFadPGDD--RYVSVE 84


                 ....
gi 640465218 116 GKAE 119
Cdd:COG3871   85 GTAE 88
NimA COG3467
Nitroimidazole reductase NimA or a related FMN-containing flavoprotein, pyridoxamine 5 ...
 40-125 3.47e-07

Nitroimidazole reductase NimA or a related FMN-containing flavoprotein, pyridoxamine 5'-phosphate oxidase superfamily [Defense mechanisms];


Pssm-ID: 442690 [Multi-domain]  Cd Length: 144  Bit Score: 47.99  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640465218  40 KQACEAKLADPTAMVVATVDeNGQPYqrIVLLKH-YDEKGLVFYTNLGSRKAHHLENNPRISLLF-----PWHMLERQVM 113
Cdd:COG3467   10 REEIRALLDEARVGRLATVD-DGRPY--VVPVNYvYDGDTIYFHTAKEGRKLDNLRRNPRVCFEVdeldgLHSTNYRSVV 86

                         90
                 ....*....|..
gi 640465218 114 VTGKAERLSTLE 125
Cdd:COG3467   87 VFGRAEEVEDPE 98
HugZ COG0748
Putative heme iron utilization protein, contains PNPOx domain [Inorganic ion transport and ...
 53-121 4.13e-03

Putative heme iron utilization protein, contains PNPOx domain [Inorganic ion transport and metabolism];


Pssm-ID: 440511 [Multi-domain]  Cd Length: 221  Bit Score: 37.25  E-value: 4.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640465218  53 MVVATVDENGQPYQRIVLLKHYDEKGLVFYTnlgSRKAHH---LENNPRISLLF------PWHMLERQ-VMVTGKAERL 121
Cdd:COG0748   22 GALATLDADGYPFASYAPFALDDDGSPYILI---SGLAEHtrnLLADPRASLLLiedeskAGDPLARPrLTLQGRAERV 97
 
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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