Reviewed, UniProtKB/Swiss-Prot Q2IHV2 (PDXH_ANADE)

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:	Adeh_1455

Organism

Anaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]

Taxonomic identifier

290397 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
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. HAMAP MF_01629
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. HAMAP MF_01629
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. HAMAP MF_01629
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 – 198	198	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000255851
Regions
	Nucleotide binding	62 – 63	2	FMN By similarity
	Nucleotide binding	126 – 127	2	FMN By similarity
	Region	177 – 179	3	Substrate binding By similarity
Sites
	Binding site	47	1	FMN By similarity
	Binding site	50	1	FMN; via amide nitrogen By similarity
	Binding site	52	1	Substrate By similarity
	Binding site	69	1	FMN By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	113	1	Substrate By similarity
	Binding site	117	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2IHV2-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 3A32F2623434D844	FASTA	198	21,612
	10 20 30 40 50 60 MPLPPSAAPD PIARFRDALA RAAAASPHDA TAAALATADA RGAPSVRMVL VKSADARGFA 70 80 90 100 110 120 FFTNRESRKA RDLAANPRAA LCFHWPALEE QVRVEGAVTP LPDAEADAYF RSRPRESRVG 130 140 150 160 170 180 AWASRQSAPL GDRAELEAAV REVEARFPGD EIPRPPFWGG YLVAPERIEF WRSGPGRLHH 190 RTVYVRRGDG WEVGALQP

References

[1]

"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000251 Genomic DNA. Translation: ABC81228.1.
RefSeq	YP_464665.1.
3D structure databases
SMR	Q2IHV2. Positions 8-198.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2IHV2.
Genome annotation databases
GeneID	3887698.
GenomeReviews	Gene locus Adeh_1455 in contig CP000251_GR.
KEGG	ade:Adeh_1455.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HBG327559.
OMA	HWSGFRI.
PhylomeDB	Q2IHV2.
Enzyme and pathway databases
BioCyc	ADEH290397:ADEH_1455-MONOMER.
Family and domain databases
HAMAP	MF_01629. PdxH. [Tree]
InterPro	IPR000659. Pyridoxamine_oxidase. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR011576. PyridoxamineP_oxidase_FMN-bd. IPR009002. Split_barrel_FMN-bd_related. 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]
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_ANADE

Accession

Primary (citable) accession number: Q2IHV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	March 7, 2006
Last modified:	February 9, 2010
This is version 32 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)