C5BN92 (PDXH_TERTT) 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:	TERTU_2874

Organism

Teredinibacter turnerae (strain ATCC 39867 / T7901) [Complete proteome] [HAMAP]

Taxonomic identifier

377629 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadales genera incertae sedis › Teredinibacter › Teredinibacter turnerae

Protein attributes

Sequence length	211 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 – 211	211	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629		PRO_1000215765
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)
	C5BN92 [UniParc]. Last modified July 28, 2009. Version 1. Checksum: 26F42A0452E29C5F	FASTA	211	24,109
	10 20 30 40 50 60 MNLEDIRREY LLGGLNREDL LPNPIDQFNV WLEQAIASGV PDPTAMTLAT VSKSGQPSQR 70 80 90 100 110 120 IVLLKHLDQR GFVFFTNYRS HKAEDIAGNP CVSLHFPWHF MERQVKVQGE AVKISTAETL 130 140 150 160 170 180 KYFLTRPRES QLAAWASEQS QRIDSRKALL SQFEAMKAKF TKGEIPLPDF WGGYVVKPQA 190 200 210 IEFWQGGASR LHDRFLYCNE NGSWQISRLA P

References

[1]

"The complete genome of Teredinibacter turnerae T7901: an intracellular endosymbiont of marine wood-boring bivalves (shipworms)." Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S., Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M., Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S., Hanora A., Schmidt E.W., Haygood M.G. , Posfai J., Benner J., Madinger C., Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L. PLoS ONE 4:E6085-E6085(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39867 / T7901.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001614 Genomic DNA. Translation: ACR10723.1.
RefSeq	YP_003074265.1. NC_012997.1.
3D structure databases
ProteinModelPortal	C5BN92.
ModBase	Search...
Protein-protein interaction databases
STRING	377629.TERTU_2874.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACR10723; ACR10723; TERTU_2874.
GeneID	8213322.
KEGG	ttu:TERTU_2874.
PATRIC	23872677. VBITerTur118718_2666.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HOG000242755.
KO	K00275.
OMA	ERIEFWQ.
ProtClustDB	CLSK2528716.
Enzyme and pathway databases
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_TERTT

Accession

Primary (citable) accession number: C5BN92

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	July 28, 2009
Last modified:	May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program