Reviewed, UniProtKB/Swiss-Prot Q8X647 (PDXH_ECO57)

Names and origin

Protein names

Recommended name:
    Pyridoxine/pyridoxamine 5'-phosphate oxidase
    EC=1.4.3.5
Alternative name(s):
    PNP/PMP oxidase
      Short name=PNPOx
    Pyridoxal 5'-phosphate synthase

Gene names

Name:	pdxH
Ordered Locus Names:	Z2652, ECs2347

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity.
Catalytic activity	Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP MF_01629 Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP MF_01629
Cofactor	Binds 1 FMN per subunit By similarity.
Pathway	Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP MF_01629 Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: HAMAP pyridoxamine-phosphate oxidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 218	218	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000167707
Regions
	Nucleotide binding	82 – 83	2	FMN By similarity
	Nucleotide binding	146 – 147	2	FMN By similarity
	Region	14 – 17	4	Substrate binding By similarity
	Region	197 – 199	3	Substrate binding By similarity
Sites
	Binding site	67	1	FMN By similarity
	Binding site	70	1	FMN; via amide nitrogen By similarity
	Binding site	72	1	Substrate By similarity
	Binding site	89	1	FMN By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	133	1	Substrate By similarity
	Binding site	137	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X647-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 95582F0EA6D83923	FASTA	218	25,561
	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 SWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG 190 200 210 FRVSLEQIEF WQGGEHRLHD RFLYQRENDA WKIDRLAP

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG56627.1. BA000007 Genomic DNA. Translation: BAB35770.1.
PIR	C90922. G85770.
RefSeq	NP_288074.1. NP_310374.1.
3D structure databases
HSSP	HSSP built from PDB template 1G79 based on UniProtKB P28225.
SMR	Q8X647. Positions 5-218.
ModBase	Search...
Genome annotation databases
GeneID	912730. 961593.
GenomeReviews	Gene locus Z2652 in contig AE005174_GR. Gene locus ECs2347 in contig BA000007_GR.
KEGG	ece:Z2652. ecs:ECs2347.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8X647.
OMA	FTFFTNY.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS2347-MON.
Family and domain databases
HAMAP	MF_01629. [Tree]
InterPro	IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR011576. PyridoxamineP_oxidase_FMN-bd. IPR012349. Split_barrel_FMN_bd. [Graphical view]
Gene3D	G3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
PANTHER	PTHR10851. Pyridox_oxidase. 1 hit.
Pfam	PF10590. PNPOx_C. 1 hit. PF01243. Pyridox_oxidase. 1 hit. [Graphical view]
ProDom	PD006312. Pyridox_oxidase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_ECO57

Accession

Primary (citable) accession number: Q8X647
Secondary accession number(s): Q7ADK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	March 1, 2002
Last modified:	November 3, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)