Reviewed, UniProtKB/Swiss-Prot Q5PBF2 (PDXH_ANAMM)

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:	AM281

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

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_0000167680
Regions
	Nucleotide binding	145 – 146	2	FMN By similarity
	Region	196 – 198	3	Substrate binding By similarity
Sites
	Binding site	66	1	FMN By similarity
	Binding site	69	1	FMN; via amide nitrogen By similarity
	Binding site	71	1	Substrate By similarity
	Binding site	82	1	FMN By similarity
	Binding site	88	1	FMN By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	136	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PBF2-1 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: 7EAF2175CEDBD818	FASTA	218	24,885
	10 20 30 40 50 60 MIDFFEGVSW LIMPFSGVCV READSSPMDV FGLWYSEMLR ATGAHMREPS AMVLATCDVQ 70 80 90 100 110 120 NRPSARVVLL KKYGEAGFEF VTNFNSRKGR EIADNPQVAL VFDWRHIGRQ VRVEGLATLM 130 140 150 160 170 180 DASESDAYHA SRSRESKISA WCSQQSAVLE SRKLLLEQFE RERQRFDGQE IPRPGHWGGV 190 200 210 RVVPHVVEFW EDGAHRLHSR KQYSRGDSGS WSCVDLYP

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000030 Genomic DNA. Translation: AAV86377.1. Different initiation.
RefSeq	YP_153632.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PBF2.
Genome annotation databases
GeneID	3171784.
GenomeReviews	Gene locus AM281 in contig CP000030_GR.
KEGG	ama:AM281.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5PBF2.
OMA	FTFFTNY.
Enzyme and pathway databases
BioCyc	AMAR234826:AM281-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_ANAMM

Accession

Primary (citable) accession number: Q5PBF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	January 24, 2006
Last modified:	November 3, 2009
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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