Reviewed, UniProtKB/Swiss-Prot B0C079 (PDXH_ACAM1)

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:	AM1_4597

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Acaryochloris

Protein attributes

Sequence length	219 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 – 219	219	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000335775
Regions
	Nucleotide binding	83 – 84	2	FMN By similarity
	Nucleotide binding	147 – 148	2	FMN By similarity
	Region	15 – 18	4	Substrate binding By similarity
	Region	198 – 200	3	Substrate binding By similarity
Sites
	Binding site	68	1	FMN By similarity
	Binding site	71	1	FMN; via amide nitrogen By similarity
	Binding site	73	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)
	B0C079-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: 20CC2DECB88A2623	FASTA	219	25,529
	10 20 30 40 50 60 MSLIDPTQTS ISDLRRDYRQ QALLETEVNA NPILQFQSWF EQAVQAELPE PNAMTLATVS 70 80 90 100 110 120 ADSQPSARMV LLKGFDQQGF IFYTNYLSRK GQDLAQRPWA ALVFWWAELE RQVRIEGKVV 130 140 150 160 170 180 KVSDSETKAY FESRPRGSQL GAWASDQSQV IGDRDILDQR LQALEQKYQN QPIPRPPHWG 190 200 210 GYRVTPHLIE FWQGRTSRLH DRLCYRYSDQ EWILERLSP

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000828 Genomic DNA. Translation: ABW29571.1.
RefSeq	YP_001518889.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5683399.
GenomeReviews	Gene locus AM1_4597 in contig CP000828_GR.
KEGG	amr:AM1_4597.
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_ACAM1

Accession

Primary (citable) accession number: B0C079

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	November 3, 2009
This is version 15 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)