Reviewed, UniProtKB/Swiss-Prot A1TQY3 (PDXH_ACIAC)

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:	Aave_2803

Organism

Acidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]

Taxonomic identifier

397945 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length	225 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 – 225	225	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000292282
Regions
	Nucleotide binding	89 – 90	2	FMN By similarity
	Nucleotide binding	153 – 154	2	FMN By similarity
	Region	21 – 24	4	Substrate binding By similarity
	Region	203 – 205	3	Substrate binding By similarity
Sites
	Binding site	74	1	FMN By similarity
	Binding site	77	1	FMN; via amide nitrogen By similarity
	Binding site	79	1	Substrate By similarity
	Binding site	96	1	FMN By similarity
	Binding site	136	1	Substrate By similarity
	Binding site	140	1	Substrate By similarity
	Binding site	144	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1TQY3-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: B79CE0E6547A210B	FASTA	225	25,428
	10 20 30 40 50 60 MHNRGMSSPS SPLSSSIADL RKSYERAELG EEASHADPLR QFDQWLQEAV AAQVPEPNAM 70 80 90 100 110 120 TLATVGADLR PSTRVVLIKG YDERGIVWYT NYGSRKGRQL AGNPFAALQF HWVELERVVR 130 140 150 160 170 180 IEGRVEKVSD AESDAYFASR PLDSRIGAWA SPQSEVISGR GVLVANAAKY GAQFLLQPLR 190 200 210 220 PPHWGGFRLK PDRWEFWQGR KSRLHDRLCY REETPGAWVR ERLAP

References

[1]

"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000512 Genomic DNA. Translation: ABM33371.1.
RefSeq	YP_971145.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A1TQY3.
Genome annotation databases
GeneID	4666365.
GenomeReviews	Gene locus Aave_2803 in contig CP000512_GR.
KEGG	aav:Aave_2803.
NMPDR	fig|397945.5.peg.2381.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	FTFFTNY.
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_ACIAC

Accession

Primary (citable) accession number: A1TQY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	February 6, 2007
Last modified:	November 3, 2009
This is version 22 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)