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Conserved domains on  [gi|692316970|ref|WP_032127805|]
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MULTISPECIES: pyridoxamine 5'-phosphate oxidase [Stenotrophomonas]

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;
1-199 7.36e-113

pyridoxal 5'-phosphate synthase;


:

Pssm-ID: 235555  Cd Length: 195  Bit Score: 319.86  E-value: 7.36e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   1 MSDLYAEALSTFAGLFDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLF 80
Cdd:PRK05679   1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  81 LWRSLREagiQVRIEGRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEARFEGKDVPRPDGWSG 160
Cdd:PRK05679  81 PWKSLER---QVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFAQGEVPRPPHWGG 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 692316970 161 LRVVPDRIEFWYGAQFRLHERWCYEAGAeGRWSKRLLYP 199
Cdd:PRK05679 158 YRVVPESIEFWQGRPSRLHDRILYRRDD-GGWKIERLAP 195
 
Name Accession Description Interval E-value
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
1-199 7.36e-113

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 319.86  E-value: 7.36e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   1 MSDLYAEALSTFAGLFDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLF 80
Cdd:PRK05679   1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  81 LWRSLREagiQVRIEGRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEARFEGKDVPRPDGWSG 160
Cdd:PRK05679  81 PWKSLER---QVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFAQGEVPRPPHWGG 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 692316970 161 LRVVPDRIEFWYGAQFRLHERWCYEAGAeGRWSKRLLYP 199
Cdd:PRK05679 158 YRVVPESIEFWQGRPSRLHDRILYRRDD-GGWKIERLAP 195
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 7-199 6.95e-107

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: 304.42  E-value: 6.95e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970    7 EALSTFAGLFDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLFLWRSLR 86
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   87 EagiQVRIEGRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEARFEGKDVPRPDGWSGLRVVPD 166
Cdd:TIGR00558  81 R---QVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDGEVPRPEFWGGYRVVPD 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 692316970  167 RIEFWYGAQFRLHERWCYEAGAEGRWSKRLLYP 199
Cdd:TIGR00558 158 EIEFWQGRPSRLHDRFRYRRDGDGSWRIERLAP 190
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 2-199 4.89e-104

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: 298.26  E-value: 4.89e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   2 SDLYAEALSTFAGLFDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLFL 81
Cdd:COG0259   19 SDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESRKGRELAANPRAALTFF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  82 WRSLREagiQVRIEGRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEARFEGKDVPRPDGWSGL 161
Cdd:COG0259   99 WPELER---QVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFAGGDVPRPPHWGGY 175

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 692316970 162 RVVPDRIEFWYGAQFRLHERWCYEAgAEGRWSKRLLYP 199
Cdd:COG0259  176 RVVPDRIEFWQGRPSRLHDRLRYTR-EDGGWTIERLAP 212
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
16-199 1.48e-51

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 164.85  E-value: 1.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  16 FDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLFLWRslrEAGIQVRIE 95
Cdd:NF038138  28 LEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWR---ETSQQISLS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  96 GRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEArfEGKDVPRPDGWSGLRVVPDRIEFWYGAQ 175
Cdd:NF038138 105 GPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAE--AGGPLPRPARFVGYRLVPEEVEFWAAGP 182

                        170       180
                 ....*....|....*....|....
gi 692316970 176 FRLHERWCYEAGAEGrWSKRLLYP 199
Cdd:NF038138 183 DRLHRRLRYDRDGDG-WTHVRLQP 205
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 26-105 3.47e-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: 90.77  E-value: 3.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   26 EPNAMTVATADTQGRPSARTVLLKA-FDERGFVFYTHLDSHKGQELQANPQAALLFLWRSLReagIQVRIEGRVEQVADA 104
Cdd:pfam01243  11 EPNAVVLATVDKDGRPNVRPVGLKYgFDTVGILFATNTDSRKARNLEENPRVALLFGDPELR---RGVRIEGTAEIVTDG 87


                  .
gi 692316970  105 E 105
Cdd:pfam01243  88 E 88
 
Name Accession Description Interval E-value
PRK05679 PRK05679
pyridoxal 5'-phosphate synthase;
1-199 7.36e-113

pyridoxal 5'-phosphate synthase;


Pssm-ID: 235555  Cd Length: 195  Bit Score: 319.86  E-value: 7.36e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   1 MSDLYAEALSTFAGLFDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLF 80
Cdd:PRK05679   1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  81 LWRSLREagiQVRIEGRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEARFEGKDVPRPDGWSG 160
Cdd:PRK05679  81 PWKSLER---QVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFAQGEVPRPPHWGG 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 692316970 161 LRVVPDRIEFWYGAQFRLHERWCYEAGAeGRWSKRLLYP 199
Cdd:PRK05679 158 YRVVPESIEFWQGRPSRLHDRILYRRDD-GGWKIERLAP 195
pdxH TIGR00558
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ...
 7-199 6.95e-107

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: 304.42  E-value: 6.95e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970    7 EALSTFAGLFDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLFLWRSLR 86
Cdd:TIGR00558   1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   87 EagiQVRIEGRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEARFEGKDVPRPDGWSGLRVVPD 166
Cdd:TIGR00558  81 R---QVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDGEVPRPEFWGGYRVVPD 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 692316970  167 RIEFWYGAQFRLHERWCYEAGAEGRWSKRLLYP 199
Cdd:TIGR00558 158 EIEFWQGRPSRLHDRFRYRRDGDGSWRIERLAP 190
PdxH COG0259
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ...
 2-199 4.89e-104

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: 298.26  E-value: 4.89e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   2 SDLYAEALSTFAGLFDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLFL 81
Cdd:COG0259   19 SDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESRKGRELAANPRAALTFF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  82 WRSLREagiQVRIEGRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEARFEGKDVPRPDGWSGL 161
Cdd:COG0259   99 WPELER---QVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFAGGDVPRPPHWGGY 175

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 692316970 162 RVVPDRIEFWYGAQFRLHERWCYEAgAEGRWSKRLLYP 199
Cdd:COG0259  176 RVVPDRIEFWQGRPSRLHDRLRYTR-EDGGWTIERLAP 212
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 6-184 1.77e-63

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 203.16  E-value: 1.77e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   6 AEALSTFAGLFDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLFLWRSL 85
Cdd:PLN03049 268 ADPIDQFKEWFDDAVAAGLREPNAMTLATAGEDGRPSARIVLLKGVDKRGFVWYTNYDSRKAHELSANPKASLVFYWDGL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  86 REagiQVRIEGRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEARF-EGKDVPRPDGWSGLRVV 164
Cdd:PLN03049 348 HR---QVRVEGSVEKVSEEESDQYFHSRPRGSQIGALVSKQSTVIPGRHILDQSYKELEAKYaDSSAIPKPKHWGGYRLK 424

                        170       180
                 ....*....|....*....|
gi 692316970 165 PDRIEFWYGAQFRLHERWCY 184
Cdd:PLN03049 425 PELIEFWQGRESRLHDRLQY 444
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 12-184 2.80e-55

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 183.60  E-value: 2.80e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  12 FAGLFDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLFLWRSLREagiQ 91
Cdd:PLN02918 356 FRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNGFVWYTNYESQKGSDLSENPSAALLFYWEELNR---Q 432

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  92 VRIEGRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEARF-EGKDVPRPDGWSGLRVVPDRIEF 170
Cdd:PLN02918 433 VRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQEYKELEKKYsDGSVIPKPKNWGGYRLKPNLFEF 512

                        170
                 ....*....|....
gi 692316970 171 WYGAQFRLHERWCY 184
Cdd:PLN02918 513 WQGQQSRLHDRLQY 526
phena_PhzG NF038138
phenazine biosynthesis FMN-dependent oxidase PhzG;
16-199 1.48e-51

phenazine biosynthesis FMN-dependent oxidase PhzG;


Pssm-ID: 468380  Cd Length: 205  Bit Score: 164.85  E-value: 1.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  16 FDEAKQSREVEPNAMTVATADTQGRPSARTVLLKAFDERGFVFYTHLDSHKGQELQANPQAALLFLWRslrEAGIQVRIE 95
Cdd:NF038138  28 LEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWR---ETSQQISLS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  96 GRVEQVADAEADAYFASRPRMSQIGAWASQQSKTLATREEFDARVAEIEArfEGKDVPRPDGWSGLRVVPDRIEFWYGAQ 175
Cdd:NF038138 105 GPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAE--AGGPLPRPARFVGYRLVPEEVEFWAAGP 182

                        170       180
                 ....*....|....*....|....
gi 692316970 176 FRLHERWCYEAGAEGrWSKRLLYP 199
Cdd:NF038138 183 DRLHRRLRYDRDGDG-WTHVRLQP 205
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 26-105 3.47e-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: 90.77  E-value: 3.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   26 EPNAMTVATADTQGRPSARTVLLKA-FDERGFVFYTHLDSHKGQELQANPQAALLFLWRSLReagIQVRIEGRVEQVADA 104
Cdd:pfam01243  11 EPNAVVLATVDKDGRPNVRPVGLKYgFDTVGILFATNTDSRKARNLEENPRVALLFGDPELR---RGVRIEGTAEIVTDG 87


                  .
gi 692316970  105 E 105
Cdd:pfam01243  88 E 88
PNP_phzG_C pfam10590
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of ...
 158-199 3.68e-15

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: 66.38  E-value: 3.68e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 692316970  158 WSGLRVVPDRIEFWYGAQFRLHERWCYEAGAEGRWSKRLLYP 199
Cdd:pfam10590   1 WGGYRLVPEEIEFWQGRPSRLHDRIRYTREGDGGWTIERLAP 42
YzzA COG3871
General stress protein 26 (function unknown) [Function unknown];
2-171 8.60e-09

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


Pssm-ID: 443080 [Multi-domain]  Cd Length: 132  Bit Score: 51.86  E-value: 8.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970   2 SDLYAEALSTFAGLFDEAKqsrevepNAMtVATADTQGRPSAR--TVLLKAFDERgFVFYTHLDSHKGQELQANPQAALL 79
Cdd:COG3871    1 TTDDEELEEKLWELLEDIR-------TAM-LATVDADGRPHSRpmWFQVDVDDGT-LWFFTSRDSAKVRNIRRDPRVSLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  80 FlwrSLREAGIQVRIEGRVEQVADaeadayfasrprmsqigawasqqsktlatREEFDARVAEIEARF--EGKDVPRpdg 157
Cdd:COG3871   72 F---ADPGDDRYVSVEGTAEIVDD-----------------------------RAKIDELWNPLAEAWfpDGPDDPD--- 116

                        170
                 ....*....|....
gi 692316970 158 WSGLRVVPDRIEFW 171
Cdd:COG3871  117 LVLLRVTPERAEYW 130
COG5135 COG5135
Uncharacterized conserved protein [Function unknown];
32-199 1.83e-08

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 444058  Cd Length: 193  Bit Score: 51.88  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970  32 VATADTQGRPSARTVLLKAFDE--RGFVFYTHLDSHKGQELQANPQAALLFLWRSLREagiQVRIEGRVEQVADAEADAY 109
Cdd:COG5135   27 LATVTGDGRPANRTVVFRGFLEdsNQLKFITDARSEKVDQIQQQPWAEICWYFPKTRE---QFRLSGKLTLVTADDPDPD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692316970 110 FASRpRMSQigaWasqQSKTLATREEFDA------RVAEIEARfegkDVPRPDGWSG------LRVVPDRIEfWYGAQFR 177
Cdd:COG5135  104 LQKA-RQQT---W---QELSDAARLQFAWpapgapREEPEAAF----SPPPPDPDQPlpnfclLLLEPDQVD-HLELRGE 171

                        170       180
                 ....*....|....*....|..
gi 692316970 178 LHERWCYEAGAEGRWSKRLLYP 199
Cdd:COG5135  172 PQNRALYHLDDDGEWSGQWVNP 193
Pyridox_oxase_2 pfam12766
Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase catalyzes the oxidation ...
 30-98 3.55e-03

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: 35.68  E-value: 3.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692316970   30 MTVAT-ADTQGRPSARTVLLKAFDERGF-----VFYTHLDSHKGQELQANPQAALLFlWrsLREAGIQVRIEGRV 98
Cdd:pfam12766  24 FQLATvDPPEGRPRVRTVVFRGFLFNDYesdvlTFTTDVRSEKVEQLEGNPAFEACF-W--FPKTREQFRIRGTA 95
 
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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