Q3IDP4 (PDXH_PSEHT) Reviewed, UniProtKB/Swiss-Prot

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:	PSHAa0658

Organism

Pseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]

Taxonomic identifier

326442 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas › Pseudoalteromonas haloplanktis

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_01629
Catalytic activity	Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP-Rule MF_01629 Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP-Rule 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-Rule 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	pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: GOC 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 – 212	212	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629		PRO_0000167735
Regions
	Nucleotide binding	75 – 76	2	FMN By similarity
	Nucleotide binding	139 – 140	2	FMN By similarity
	Region	7 – 10	4	Substrate binding By similarity
	Region	190 – 192	3	Substrate binding By similarity
Sites
	Binding site	60	1	FMN By similarity
	Binding site	63	1	FMN; via amide nitrogen By similarity
	Binding site	65	1	Substrate By similarity
	Binding site	82	1	FMN By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	130	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3IDP4 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 7E19CC4F2ADE156C	FASTA	212	24,362
	10 20 30 40 50 60 MKLEDIRREY LQNALSEDNL LDDPFKQFET WLEHAVASNL PDPTAMVVAT VDDTGQPSQR 70 80 90 100 110 120 IVLLKHLDND GFVFFTNTGS RKAQELKGNN KISLHFPWHP MERQVIVYGE AKPLPTSAVA 130 140 150 160 170 180 KYFLSRPKES QLAAWASAQS RPVSSRKVLM ETFANMKNKF AKGEIPLPDF WGGYCVVPQK 190 200 210 IEFWQGGAHR LHDRFMYQRQ ADNSWQITRL NP

References

[1]

"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125." Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A. Genome Res. 15:1325-1335(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TAC 125.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR954246 Genomic DNA. Translation: CAI85742.1.
RefSeq	YP_339185.1. NC_007481.1.
3D structure databases
ProteinModelPortal	Q3IDP4.
SMR	Q3IDP4. Positions 14-212.
ModBase	Search...
Protein-protein interaction databases
STRING	326442.PSHAa0658.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAI85742; CAI85742; PSHAa0658.
GeneID	3709964.
KEGG	pha:PSHAa0658.
PATRIC	32294843. VBIPseHal105694_0621.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HOG000242755.
KO	K00275.
OMA	ERIEFWQ.
ProtClustDB	CLSK749894.
Enzyme and pathway databases
BioCyc	PHAL326442:GJIU-668-MONOMER.
UniPathway	UPA00190; UER00304. UPA00190; UER00305.
Family and domain databases
Gene3D	2.30.110.10. 1 hit.
HAMAP	MF_01629. PdxH.
InterPro	IPR000659. Pyridox_Oxase. IPR019740. Pyridox_Oxase_CS. IPR011576. Pyridox_Oxase_FMN-bd. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR012349. Split_barrel_FMN-bd. [Graphical view]
PANTHER	PTHR10851. PTHR10851. 1 hit.
Pfam	PF10590. PNPOx_C. 1 hit. PF01243. Pyridox_oxidase. 1 hit. [Graphical view]
PIRSF	PIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAM	SSF50475. FMN_binding. 1 hit.
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_PSEHT

Accession

Primary (citable) accession number: Q3IDP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program