UniProt Accession

 PDXH_ECOLI; P0AFI7; P28225 

Genbank Protein ID

 M92351; U00096; AP009048 

Genbank Nucleotide ID

 AAA24709.1; AAC74710.1; BAA15399.1 

Protein Name

 Pyridoxine/pyridoxamine 5'-phosphate oxidase 

Protein Synonyms/Alias

 PNP/PMP oxidase; PNPOx; Pyridoxal 5'-phosphate synthase 

Gene Name

 pdxH 

Gene Synonyms/Alias

 b1638; JW1630 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
19	HLRREYTKGGLRRRD	acetylation	[1]
46	LSQACEAKLADPTAM	acetylation	[1]
72	YQRIVLLKHYDEKGM	acetylation	[1]
77	LLKHYDEKGMVFYTN	acetylation	[1]
117	RQVMVIGKAERLSTL	acetylation	[1]
128	LSTLEVMKYFHSRPR	acetylation	[1]
145	QIGAWVSKQSSRISA	acetylation	[1]
159	ARGILESKFLELKQK	acetylation	[1]
164	ESKFLELKQKFQQGE	acetylation	[1]
166	KFLELKQKFQQGEVP	acetylation	[1]
212	QRENDAWKIDRLAP*	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 

Functional Description

 Catalyzes the oxidation of either pyridoxine 5'- phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). 

Sequence Annotation

 NP_BIND 82 83 FMN.
 NP_BIND 146 147 FMN.
 REGION 14 17 Substrate binding.
 REGION 197 199 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.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 218 AA 

Protein Sequence

Gene Ontology

 GO:0010181; F:FMN binding; IDA:EcoCyc.
 GO:0004733; F:pyridoxamine-phosphate oxidase activity; IDA:EcoCyc.
 GO:0009443; P:pyridoxal 5'-phosphate salvage; EXP:EcoCyc.
 GO:0008615; P:pyridoxine biosynthetic process; IDA:EcoCyc. 

Interpro

 IPR000659; Pyridox_Oxase.
 IPR019740; Pyridox_Oxase_CS.
 IPR011576; Pyridox_Oxase_FMN-bd.
 IPR019576; Pyridoxamine_oxidase_dimer_C.
 IPR012349; Split_barrel_FMN-bd. 

Pfam

 PF10590; PNPOx_C
 PF01243; Pyridox_oxidase 

SMART

  

PROSITE

 PS01064; PYRIDOX_OXIDASE 

PRINTS