[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=1356963 [NCBI, ExPASy, EBI, Israel, Japan] Lam H.-M., Winkler M.E.; "Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations."; J. Bacteriol. 174:6033-6045(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan] Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.; "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."; DNA Res. 3:363-377(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	PROTEIN SEQUENCE OF 2-11, AND CHARACTERIZATION. STRAIN=K12; PubMed=7860596 [NCBI, ExPASy, EBI, Israel, Japan] Zhao G., Winkler M.E.; "Kinetic limitation and cellular amount of pyridoxine (pyridoxamine) 5'-phosphate oxidase of Escherichia coli K-12."; J. Bacteriol. 177:883-891(1995).
[6]	CHARACTERIZATION. DOI=10.1006/prep.1998.0904; PubMed=9693059 [NCBI, ExPASy, EBI, Israel, Japan] di Salvo M., Yang E., Zhao G., Winkler M.E., Schirch V.; "Expression, purification, and characterization of recombinant Escherichia coli pyridoxine 5'-phosphate oxidase."; Protein Expr. Purif. 13:349-356(1998).
[7]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-218 IN COMPLEX WITH FMN, AND SUBUNIT. DOI=10.1016/S0969-2126(00)00162-3; PubMed=10903950 [NCBI, ExPASy, EBI, Israel, Japan] Safo M.K., Mathews I., Musayev F.N., di Salvo M.L., Thiel D.J., Abraham D.J., Schirch V.; "X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8-A resolution."; Structure 8:751-762(2000).
[8]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL 5'-PHOSPHATE AND FMN, AND SUBUNIT. DOI=10.1006/jmbi.2001.4734; PubMed=11453690 [NCBI, ExPASy, EBI, Israel, Japan] Safo M.K., Musayev F.N., di Salvo M.L., Schirch V.; "X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with pyridoxal 5'-phosphate at 2.0 A resolution."; J. Mol. Biol. 310:817-826(2001).
[9]	X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL 5'-PHOSPHATE AND FMN, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-14; TYR-17; ASP-49; ARG-197 AND HIS-199. DOI=10.1006/jmbi.2001.5254; PubMed=11786019 [NCBI, ExPASy, EBI, Israel, Japan] di Salvo M.L., Ko T.-P., Musayev F.N., Raboni S., Schirch V., Safo M.K.; "Active site structure and stereospecificity of Escherichia coli pyridoxine-5'-phosphate oxidase."; J. Mol. Biol. 315:385-397(2002).
[10]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL 5'-PHOSPHATE AND FMN, AND SUBUNIT. DOI=10.1107/S0907444905005512; PubMed=15858270 [NCBI, ExPASy, EBI, Israel, Japan] Safo M.K., Musayev F.N., Schirch V.; "Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a tetragonal crystal form: insights into the mechanistic pathway of the enzyme."; Acta Crystallogr. D 61:599-604(2005).

Comments

FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H₂O + O₂ = pyridoxal 5'-phosphate + NH₃ + H₂O₂.
CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O₂ = pyridoxal 5'-phosphate + H₂O₂.
COFACTOR: Binds 1 FMN per subunit.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=0.3 µM for pyridoxamine 5'-phosphate;
PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1 .
PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1 .
SUBUNIT: Homodimer.
MISCELLANEOUS: Can bind a second molecule of pyridoxamine 5'-phosphate at a non-catalytic site in a cleft at the protein surface.
SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M92351; AAA24709.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74710.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15399.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B43261; B43261.

RefSeq

AP_002260.1; -.
NP_416155.1; -.

3D structure databases

PDB

1DNL; X-ray; 1.80 A; A=20-218.	[ExPASy / RCSB / EBI]
1G76; X-ray; 2.20 A; A=1-218.	[ExPASy / RCSB / EBI]
1G77; X-ray; 2.10 A; A=1-218.	[ExPASy / RCSB / EBI]
1G78; X-ray; 2.20 A; A=1-218.	[ExPASy / RCSB / EBI]
1G79; X-ray; 2.00 A; A=1-218.	[ExPASy / RCSB / EBI]
1JNW; X-ray; 2.07 A; A=1-218.	[ExPASy / RCSB / EBI]
1WV4; X-ray; 2.60 A; A/B=1-218.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DNL; -.
1G76; -.
1G77; -.
1G78; -.
1G79; -.
1JNW; -.
1WV4; -.

ModBase

P0AFI7.

Enzyme and pathway databases

BioCyc

EcoCyc:PDXH-MON; -.
MetaCyc:PDXH-MON; -.

Organism-specific databases

EchoBASE

EB1450; -.

EcoGene

EG11487; pdxH.

Ontologies

GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from HAMAP).
GO:0004733;	Molecular function: pyridoxamine-phosphate oxidase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0008615;	Biological process: pyridoxine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_01629; -; 1.
PBIL [Tree]

InterPro

IPR011576; PNPOx_rel_FMN_bd_core.
IPR000659; Pyridox_oxidase.
IPR012349; Split_barrel_FMN_bd.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.110.10; PNPOx_FMN_bd; 1.

PANTHER

PTHR10851; Pyridox_oxidase; 1.

Pfam

PF01243; Pyridox_oxidase; 1.
Pfam graphical view of domain structure.

ProDom

PD006312; Pyridox_oxidase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00558; pdxH; 1.

PROSITE

PS01064; PYRIDOX_OXIDASE; 1.

Genome annotation databases

GeneID

946806; -.

GenomeReviews

AP009048_GR; JW1630.
U00096_GR; b1638.

KEGG

ecj:JW1630; -.
eco:b1638; -.

Phylogenomic databases

HOGENOM

P0AFI7; -.

Genome annotation databases

CMR

P0AFI7; b1638.

Other

ProtoNet

P0AFI7.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Direct protein sequencing; Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 218`	`217`	`Pyridoxine/pyridoxamine 5'-phosphate oxidase.`	`PRO_0000167706`
`NP_BIND`	`82 83`	`2`	`FMN.`
`NP_BIND`	`146 147`	`2`	`FMN.`
`REGION`	`14 17`	`4`	`Substrate binding.`
`REGION`	`197 199`	`3`	`Substrate binding.`
`BINDING`	`67 67`		`FMN.`
`BINDING`	`70 70`		`FMN; via amide nitrogen.`
`BINDING`	`72 72`		`Substrate.`
`BINDING`	`89 89`		`FMN.`
`BINDING`	`129 129`		`Substrate.`
`BINDING`	`133 133`		`Substrate.`
`BINDING`	`137 137`		`Substrate.`
`MUTAGEN`	`14 14`		`R->E: Reduces affinity for substrate about 7-fold, but has no effect on catalytic activity.`
`MUTAGEN`	`14 14`		`R->M: Reduces affinity for substrate about 9-fold, but has no effect on catalytic activity.`
`MUTAGEN`	`17 17`		`Y->F: Reduces affinity for substrate 3-fold, but has about 5-fold increase in catalytic activity.`
`MUTAGEN`	`49 49`		`D->A: Reduces affinity for substrate 3-fold and catalytic activity 2-fold.`
`MUTAGEN`	`197 197`		`R->E: Reduces affinity for substrate 8000-fold and catalytic activity 16-fold.`
`MUTAGEN`	`197 197`		`R->M: Reduces affinity for substrate 300-fold and catalytic activity about 4-fold.`
`MUTAGEN`	`199 199`		`H->A: Reduces affinity for substrate 230-fold, but has no effect on catalytic activity.`
`MUTAGEN`	`199 199`		`H->N: Reduces catalytic activity about 4-fold, but has no effect on affinity for substrate.`
`HELIX`	`9 12`	`4`
`HELIX`	`24 26`	`3`
`HELIX`	`31 44`	`14`
`STRAND`	`52 58`	`7`
`STRAND`	`64 70`	`7`
`STRAND`	`73 75`	`3`
`STRAND`	`78 84`	`7`
`HELIX`	`88 95`	`8`
`STRAND`	`98 103`	`6`
`HELIX`	`106 108`	`3`
`STRAND`	`110 120`	`11`
`HELIX`	`123 130`	`8`
`HELIX`	`135 143`	`9`
`STRAND`	`148 151`	`4`
`HELIX`	`154 166`	`13`
`STRAND`	`178 183`	`6`
`STRAND`	`186 192`	`7`
`HELIX`	`195 197`	`3`
`STRAND`	`200 206`	`7`
`STRAND`	`208 216`	`9`

Sequence information

Length: 218 AA [This is the length of the unprocessed precursor]

Molecular weight: 25545 Da [This is the MW of the unprocessed precursor]

CRC64: 8B47CEEEA6CEF5F9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP TAMVVATVDE 

        70         80         90        100        110        120 
HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS LLFPWHTLER QVMVIGKAER 

       130        140        150        160        170        180 
LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG 

       190        200        210 
FRVSLEQIEF WQGGEHRLHD RFLYQRENDA WKIDRLAP

P0AFI7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools