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Conserved domains on  [gi|378729563|gb|EHY56022|]
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hypothetical protein HMPREF1120_04128 [Exophiala dermatitidis NIH/UT8656]

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

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 ...
26-102 2.44e-11

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: 58.41  E-value: 2.44e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378729563   26 LPPEVSQCLQNSRFLHLATISAtessQPTPHVSLMNYTFLPsyKEHGPVIImtTNAQSIKTRNLLHNPKVSLLVHDW 102
Cdd:pfam01243   1 LTEEIREFLAEPNAVVLATVDK----DGRPNVRPVGLKYGF--DTVGILFA--TNTDSRKARNLEENPRVALLFGDP 69
 
Name Accession Description Interval E-value
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
26-102 2.44e-11

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: 58.41  E-value: 2.44e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378729563   26 LPPEVSQCLQNSRFLHLATISAtessQPTPHVSLMNYTFLPsyKEHGPVIImtTNAQSIKTRNLLHNPKVSLLVHDW 102
Cdd:pfam01243   1 LTEEIREFLAEPNAVVLATVDK----DGRPNVRPVGLKYGF--DTVGILFA--TNTDSRKARNLEENPRVALLFGDP 69
Rv1155_F420 TIGR03618
PPOX class probable F420-dependent enzyme; A Genome Properties metabolic reconstruction for ...
34-101 2.60e-07

PPOX class probable F420-dependent enzyme; A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomyces, make F420. The Partial Phylogenetic Profiling algorithm identifies this members of this protein family as high-scoring proteins to the F420 biosynthesis profile. A member of this family, Rv1155, was crytallized after expression in Escherichia coli, which does not synthesize F420; the crystal structure shown to resemble FMN-binding proteins, but with a recognizable empty cleft corresponding to, yet differing profounding from, the FMN site of pyridoxine 5'-phosphate oxidase. We propose that this protein family consists of F420-binding enzymes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274679 [Multi-domain]  Cd Length: 126  Bit Score: 48.44  E-value: 2.60e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378729563   34 LQNSRFLHLATISATESsqptPHVSLMNYTFlpsykeHGPVIIMTTNAQSIKTRNLLHNPKVSLLVHD 101
Cdd:TIGR03618   5 LSERRLAVLATIRPDGR----PQLSPVWFAL------DGDELVFSTTAGRAKARNLRRDPRVSLSVLD 62
HugZ COG0748
Putative heme iron utilization protein, contains PNPOx domain [Inorganic ion transport and ...
20-101 2.77e-07

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


Pssm-ID: 440511 [Multi-domain]  Cd Length: 221  Bit Score: 49.96  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378729563  20 RIVSSTLPPEVSQCLQNSRFLHLATISAtessQPTPHVSLMNYTFLPsykEHGPVIIMTTNAQsiKTRNLLHNPKVSLLV 99
Cdd:COG0748    2 EEADEEAAEEARTLLRSARSGALATLDA----DGYPFASYAPFALDD---DGSPYILISGLAE--HTRNLLADPRASLLL 72

                 ..
gi 378729563 100 HD 101
Cdd:COG0748   73 IE 74
 
Name Accession Description Interval E-value
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
26-102 2.44e-11

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: 58.41  E-value: 2.44e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378729563   26 LPPEVSQCLQNSRFLHLATISAtessQPTPHVSLMNYTFLPsyKEHGPVIImtTNAQSIKTRNLLHNPKVSLLVHDW 102
Cdd:pfam01243   1 LTEEIREFLAEPNAVVLATVDK----DGRPNVRPVGLKYGF--DTVGILFA--TNTDSRKARNLEENPRVALLFGDP 69
Rv1155_F420 TIGR03618
PPOX class probable F420-dependent enzyme; A Genome Properties metabolic reconstruction for ...
34-101 2.60e-07

PPOX class probable F420-dependent enzyme; A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomyces, make F420. The Partial Phylogenetic Profiling algorithm identifies this members of this protein family as high-scoring proteins to the F420 biosynthesis profile. A member of this family, Rv1155, was crytallized after expression in Escherichia coli, which does not synthesize F420; the crystal structure shown to resemble FMN-binding proteins, but with a recognizable empty cleft corresponding to, yet differing profounding from, the FMN site of pyridoxine 5'-phosphate oxidase. We propose that this protein family consists of F420-binding enzymes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274679 [Multi-domain]  Cd Length: 126  Bit Score: 48.44  E-value: 2.60e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378729563   34 LQNSRFLHLATISATESsqptPHVSLMNYTFlpsykeHGPVIIMTTNAQSIKTRNLLHNPKVSLLVHD 101
Cdd:TIGR03618   5 LSERRLAVLATIRPDGR----PQLSPVWFAL------DGDELVFSTTAGRAKARNLRRDPRVSLSVLD 62
HugZ COG0748
Putative heme iron utilization protein, contains PNPOx domain [Inorganic ion transport and ...
20-101 2.77e-07

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


Pssm-ID: 440511 [Multi-domain]  Cd Length: 221  Bit Score: 49.96  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378729563  20 RIVSSTLPPEVSQCLQNSRFLHLATISAtessQPTPHVSLMNYTFLPsykEHGPVIIMTTNAQsiKTRNLLHNPKVSLLV 99
Cdd:COG0748    2 EEADEEAAEEARTLLRSARSGALATLDA----DGYPFASYAPFALDD---DGSPYILISGLAE--HTRNLLADPRASLLL 72

                 ..
gi 378729563 100 HD 101
Cdd:COG0748   73 IE 74
YzzA COG3871
General stress protein 26 (function unknown) [Function unknown];
34-104 3.89e-07

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


Pssm-ID: 443080 [Multi-domain]  Cd Length: 132  Bit Score: 48.01  E-value: 3.89e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378729563  34 LQNSRFLHLATISATESsqptPHVSLMnytfLPSYKEHGPVIIMTTNAQSIKTRNLLHNPKVSLLVHD-----WVS 104
Cdd:COG3871   15 LEDIRTAMLATVDADGR----PHSRPM----WFQVDVDDGTLWFFTSRDSAKVRNIRRDPRVSLSFADpgddrYVS 82
NimA COG3467
Nitroimidazole reductase NimA or a related FMN-containing flavoprotein, pyridoxamine 5 ...
34-116 1.69e-06

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: 46.45  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378729563  34 LQNSRFLHLATISATEssqptPHVSLMNYTFlpsykeHGPVIIMTTNAQSIKTRNLLHNPKVSLLVHDWVSHRPPTASSV 113
Cdd:COG3467   17 LDEARVGRLATVDDGR-----PYVVPVNYVY------DGDTIYFHTAKEGRKLDNLRRNPRVCFEVDELDGLHSTNYRSV 85

                 ...
gi 378729563 114 VGE 116
Cdd:COG3467   86 VVF 88
 
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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