Reviewed, UniProtKB/Swiss-Prot Q1LU04 (PDXH_BAUCH)

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:	BCI_0082

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	216 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 – 216	216	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000255853
Regions
	Nucleotide binding	80 – 81	2	FMN By similarity
	Nucleotide binding	144 – 145	2	FMN By similarity
	Region	12 – 15	4	Substrate binding By similarity
	Region	195 – 197	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)
	Q1LU04-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 225724267EE7639C	FASTA	216	25,278
	10 20 30 40 50 60 MNKQSINIAQ IRREYTHKRL RRADLTLEPM ELFERWFRQA STAQLLDLTV VSVATVDQTG 70 80 90 100 110 120 QPYQRLVLLK HFDAKGMVFY TNLGSRKAQH LAHNARISLH FPWHALERQV MVLGTAKQLA 130 140 150 160 170 180 LKEVMHYFSS RPRNSQISAW ASSQSSLIDT RDTLVSTFLK FNNYFHQGKV PLPSFWGGYR 190 200 210 VHIDSMEFWQ GGAYRLHDRF IYQRIASGWR IDRLAP

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000238 Genomic DNA. Translation: ABF14338.1.
RefSeq	YP_588560.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4056190.
GenomeReviews	Gene locus BCI_0082 in contig CP000238_GR.
KEGG	bci:BCI_0082.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LU04.
OMA	Q1LU04. FTFFTNY.
Family and domain databases
HAMAP	MF_01629. [Tree]
InterPro	IPR011576. PNPOx_rel_FMN_bd_core. IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. 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_BAUCH

Accession

Primary (citable) accession number: Q1LU04

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	May 30, 2006
Last modified:	June 16, 2009
This is version 23 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)