Reviewed, UniProtKB/Swiss-Prot Q0A757 (PDXH_ALHEH)

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:	Mlg_1988

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

Protein attributes

Sequence length	196 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 – 196	196	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000292287
Regions
	Nucleotide binding	59 – 60	2	FMN By similarity
	Nucleotide binding	123 – 124	2	FMN By similarity
	Region	175 – 177	3	Substrate binding By similarity
Sites
	Binding site	44	1	FMN By similarity
	Binding site	47	1	FMN; via amide nitrogen By similarity
	Binding site	49	1	Substrate By similarity
	Binding site	66	1	FMN By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	114	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0A757-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 75E447CD3577A59D	FASTA	196	22,046
	10 20 30 40 50 60 MQLLEQALAR FAEVYGRAAE AADVVDHTAC TLATCSASGW PQVRTVLLKG YDERGFAFYT 70 80 90 100 110 120 NRHSRKGQAL AENPRAAVCF HWAPLAEQVV IEGVVTPVAE AEADAYWAGR PRESQIGGWA 130 140 150 160 170 180 SHQSRGLESR EVLEQRVAEY AARFPDGEAV PRPPHWSGYR LAPVRIEFWR ARPGRLHERD 190 VYEHTAEGWC HRLLNP

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." 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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000453 Genomic DNA. Translation: ABI57330.1.
RefSeq	YP_742820.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4268531.
GenomeReviews	Gene locus Mlg_1988 in contig CP000453_GR.
KEGG	aeh:Mlg_1988.
NMPDR	fig|187272.6.peg.1895.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0A757.
OMA	Q0A757. RKGSELE.
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]
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_ALHEH

Accession

Primary (citable) accession number: Q0A757

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	October 17, 2006
Last modified:	June 16, 2009
This is version 21 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)