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Conserved domains on  [gi|1856727381|ref|WP_174616559|]
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pyridoxamine 5'-phosphate oxidase family protein [Bacillus subtilis]

Protein Classification

pyridoxamine 5'-phosphate oxidase family protein( domain architecture ID 10472314)

pyridoxamine 5'-phosphate oxidase family protein similar to Desulfovibrio vulgaris FMN-binding protein which functions as a redox protein

EC:  1.4.3.5|1.-.-.-
Gene Ontology:  GO:0008615|GO:0004733|GO:0010181
PubMed:  26327315|12686112

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 7-93 1.65e-03

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: 35.69  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856727381   7 MSDRLFELLdgsclneKQHEAFVLQTVSEDGWPHAAMISAGEIIALSRTDIRIAlwKNTMTSANILRTGKAQFTAWWKGA 86
Cdd:pfam01243   1 LTEEIREFL-------AEPNAVVLATVDKDGRPNVRPVGLKYGFDTVGILFATN--TDSRKARNLEENPRVALLFGDPEL 71


                  ....*..
gi 1856727381  87 AYYVKFE 93
Cdd:pfam01243  72 RRGVRIE 78
 
Name Accession Description Interval E-value
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 7-93 1.65e-03

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: 35.69  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856727381   7 MSDRLFELLdgsclneKQHEAFVLQTVSEDGWPHAAMISAGEIIALSRTDIRIAlwKNTMTSANILRTGKAQFTAWWKGA 86
Cdd:pfam01243   1 LTEEIREFL-------AEPNAVVLATVDKDGRPNVRPVGLKYGFDTVGILFATN--TDSRKARNLEENPRVALLFGDPEL 71


                  ....*..
gi 1856727381  87 AYYVKFE 93
Cdd:pfam01243  72 RRGVRIE 78
 
Name Accession Description Interval E-value
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 7-93 1.65e-03

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: 35.69  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856727381   7 MSDRLFELLdgsclneKQHEAFVLQTVSEDGWPHAAMISAGEIIALSRTDIRIAlwKNTMTSANILRTGKAQFTAWWKGA 86
Cdd:pfam01243   1 LTEEIREFL-------AEPNAVVLATVDKDGRPNVRPVGLKYGFDTVGILFATN--TDSRKARNLEENPRVALLFGDPEL 71


                  ....*..
gi 1856727381  87 AYYVKFE 93
Cdd:pfam01243  72 RRGVRIE 78
 
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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