Reviewed, UniProtKB/Swiss-Prot A0LR32 (PDXH_ACIC1)

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:	Acel_0116

Organism

Acidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]

Taxonomic identifier

351607 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Acidothermaceae › Acidothermus

Protein attributes

Sequence length	224 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 – 224	224	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000292281
Regions
	Nucleotide binding	83 – 84	2	FMN By similarity
	Nucleotide binding	148 – 149	2	FMN By similarity
	Region	200 – 202	3	Substrate binding By similarity
Sites
	Binding site	69	1	FMN By similarity
	Binding site	72	1	FMN; via amide nitrogen By similarity
	Binding site	74	1	Substrate By similarity
	Binding site	90	1	FMN By similarity
	Binding site	130	1	Substrate By similarity
	Binding site	134	1	Substrate By similarity
	Binding site	138	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0LR32-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: D50A98E36BA4A6B9	FASTA	224	25,428
	10 20 30 40 50 60 MRHGTHTGSN PYAEAYVEVT AGGLAETDLA ADPIEQFRRW LADAIRYNLP EPTAMVVATA 70 80 90 100 110 120 DADGRPSSRH VLLKSVDDGF VFFTNYRSRK GRDLSENPSA SLCFPWFAIG RQVVVLGTVT 130 140 150 160 170 180 KVTREETEEY FASRPRDSQC GAWSSENQSS VVPSRAWLDE RYAEVAQRFA GVEHIPPPPF 190 200 210 220 WGGFRVIPET VEFWQARPAR MHDRLRYRRT ADGERPWIIE RLSP

References

[1]

"Complete sequence of Acidothermus cellulolyticus 11B." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000481 Genomic DNA. Translation: ABK51892.1.
RefSeq	YP_871878.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4484559.
GenomeReviews	Gene locus Acel_0116 in contig CP000481_GR.
KEGG	ace:Acel_0116.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A0LR32. 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. [Graphical view]
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_ACIC1

Accession

Primary (citable) accession number: A0LR32

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	December 12, 2006
Last modified:	June 16, 2009
This is version 17 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)