Reviewed, UniProtKB/Swiss-Prot Q1J188 (PDXH_DEIGD)

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:	Dgeo_0443

Organism

Deinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]

Taxonomic identifier

319795 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

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_0000255864
Regions
	Nucleotide binding	80 – 81	2	FMN By similarity
	Nucleotide binding	145 – 146	2	FMN By similarity
	Region	12 – 15	4	Substrate binding By similarity
	Region	197 – 199	3	Substrate binding By similarity
Sites
	Binding site	65	1	FMN By similarity
	Binding site	68	1	FMN; via amide nitrogen By similarity
	Binding site	70	1	Substrate By similarity
	Binding site	87	1	FMN By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	135	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1J188-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 75DC27ADBBA81596	FASTA	218	24,973
	10 20 30 40 50 60 MPDPLPDLSS LRLAYTRAEL RRADLDPDPL RQFQGWLGEA LQAGLREPYA LSLATADASG 70 80 90 100 110 120 RPSVRTVLLR GADERGLTFY TNYESHKGHD LAQNPQAELL FFWADLERQV RAYGPVERVS 130 140 150 160 170 180 EEESTAYFHA RPRESQIAAH ASDPQSAPIA NRGALEAKLA ALQAQYPEGT PVPRPDFWGG 190 200 210 YRVRVREWEF WQGRPSRLHD RFRYTWEGEG WRIERLMP

References

[1]

"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000359 Genomic DNA. Translation: ABF44746.1.
RefSeq	YP_603915.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1J188.
Genome annotation databases
GeneID	4059156.
GenomeReviews	Gene locus Dgeo_0443 in contig CP000359_GR.
KEGG	dge:Dgeo_0443.
NMPDR	fig|68909.1.peg.269.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1J188.
OMA	RKGSELE.
Enzyme and pathway databases
BioCyc	DGEO319795:DGEO_0443-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_DEIGD

Accession

Primary (citable) accession number: Q1J188

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	June 13, 2006
Last modified:	November 3, 2009
This is version 27 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)