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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532589  16 GLCVFSTVRRDGSIQSSVVNAGVLqhplTGVPVVGLVAigGSRKLAHLRADPRAT--IVAKAGW-QWAAVEGSADLI-GP 91
Cdd:TIGR03618   9 RLAVLATIRPDGRPQLSPVWFALD----GDELVFSTTA--GRAKARNLRRDPRVSlsVLDPDGPyRYVEIEGTAEVSpDP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063532589  92 DDPHPEVDAerlrglLREIFTAAGGThddwDTYDRVMREQRRTAVLIPPARVYA 145
Cdd:TIGR03618  83 DAVRDLVDR------LAERYRGAAGE----DEYRRPMVDPRRVVVRVTPERVYG 126

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532589  16 GLCVFSTVRRDGSIQSSVVNAGVLqhplTGVPVVGLVAigGSRKLAHLRADPRAT--IVAKAGW-QWAAVEGSADLI-GP 91
Cdd:TIGR03618   9 RLAVLATIRPDGRPQLSPVWFALD----GDELVFSTTA--GRAKARNLRRDPRVSlsVLDPDGPyRYVEIEGTAEVSpDP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063532589  92 DDPHPEVDAerlrglLREIFTAAGGThddwDTYDRVMREQRRTAVLIPPARVYA 145
Cdd:TIGR03618  83 DAVRDLVDR------LAERYRGAAGE----DEYRRPMVDPRRVVVRVTPERVYG 126

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532589  13 ADQGLCVFSTVRRDGSIQSSVVnaGVLQHPLTGVPVVGlvAIGGSRKLAHLRADPRATI--VAKAGWQWAAVEGSADLIG 90
Cdd:pfam01243  10 AEPNAVVLATVDKDGRPNVRPV--GLKYGFDTVGILFA--TNTDSRKARNLEENPRVALlfGDPELRRGVRIEGTAEIVT 85

                  ...
gi 1063532589  91 PDD 93
Cdd:pfam01243  86 DGE 88

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532589  16 GLCVFSTVRRDGSIQSSVVNAGVLqhplTGVPVVGLVAigGSRKLAHLRADPRAT--IVAKAGW-QWAAVEGSADLI-GP 91
Cdd:TIGR03618   9 RLAVLATIRPDGRPQLSPVWFALD----GDELVFSTTA--GRAKARNLRRDPRVSlsVLDPDGPyRYVEIEGTAEVSpDP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063532589  92 DDPHPEVDAerlrglLREIFTAAGGThddwDTYDRVMREQRRTAVLIPPARVYA 145
Cdd:TIGR03618  83 DAVRDLVDR------LAERYRGAAGE----DEYRRPMVDPRRVVVRVTPERVYG 126

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532589  13 ADQGLCVFSTVRRDGSIQSSVVnaGVLQHPLTGVPVVGlvAIGGSRKLAHLRADPRATI--VAKAGWQWAAVEGSADLIG 90
Cdd:pfam01243  10 AEPNAVVLATVDKDGRPNVRPV--GLKYGFDTVGILFA--TNTDSRKARNLEENPRVALlfGDPELRRGVRIEGTAEIVT 85

                  ...
gi 1063532589  91 PDD 93
Cdd:pfam01243  86 DGE 88