Reviewed, UniProtKB/Swiss-Prot Q1QWA6 (PDXH_CHRSD)

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:	Csal_1900

Organism

Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]

Taxonomic identifier

290398 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Halomonadaceae › Chromohalobacter

Protein attributes

Sequence length	215 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 – 215	215	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000255862
Regions
	Nucleotide binding	77 – 78	2	FMN By similarity
	Nucleotide binding	141 – 142	2	FMN By similarity
	Region	9 – 12	4	Substrate binding By similarity
	Region	192 – 194	3	Substrate binding By similarity
Sites
	Binding site	62	1	FMN By similarity
	Binding site	65	1	FMN; via amide nitrogen By similarity
	Binding site	67	1	Substrate By similarity
	Binding site	84	1	FMN By similarity
	Binding site	124	1	Substrate By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1QWA6-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: F0130BD1535A6311	FASTA	215	25,050
	10 20 30 40 50 60 MNYDIADLRR DYAGETLSVE SAPASPLDLF QTWFAAAREH ETQDANAMTL ATVDSQGLPH 70 80 90 100 110 120 ARVVLLKQLD DKGLVFFTNY QSHKGSELTN VPYAALVFWW PTLQRQIRIE GRVEKASAEV 130 140 150 160 170 180 SDAYFANRPR DSQLGAWISQ QSVEIPDRDW LEERKQRFEQ VYGEQTVERP PHWGGYRVLP 190 200 210 FLLEFWQGQP NRLHDRIRYR YHEQDAAWSK TRLAP

References

[1]

"Complete sequence of Chromohalobacter salexigens DSM 3043." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., Canovas D., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000285 Genomic DNA. Translation: ABE59252.1.
RefSeq	YP_573951.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4026813.
GenomeReviews	Gene locus Csal_1900 in contig CP000285_GR.
KEGG	csa:Csal_1900.
NMPDR	fig|290398.4.peg.2243.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1QWA6.
OMA	Q1QWA6. FTFFTNY.
Enzyme and pathway databases
BioCyc	CSAL290398:CSAL_1900-MON.
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_CHRSD

Accession

Primary (citable) accession number: Q1QWA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	May 16, 2006
Last modified:	June 16, 2009
This is version 25 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)