Q83D18 (PDXH_COXBU) 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:	CBU_0928

Organism

Coxiella burnetii

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	196 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 MF_01629
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. HAMAP MF_01629
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. HAMAP MF_01629
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 Reference proteome
Gene Ontology (GO)
Biological process	pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro pyridoxamine-phosphate oxidase activity Inferred from electronic annotation. Source: EC
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_0000167700
Regions
	Nucleotide binding	61 – 62	2	FMN By similarity
	Nucleotide binding	125 – 126	2	FMN By similarity
	Region	175 – 177	3	Substrate binding By similarity
Sites
	Binding site	46	1	FMN By similarity
	Binding site	49	1	FMN; via amide nitrogen By similarity
	Binding site	51	1	Substrate By similarity
	Binding site	68	1	FMN By similarity
	Binding site	108	1	Substrate By similarity
	Binding site	112	1	Substrate By similarity
	Binding site	116	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q83D18 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 75DDC0F2C706C1DA	FASTA	196	23,636
	10 20 30 40 50 60 MFRLDLLSDP LEQFKLWYDE AIRHETLHPD AMVLATADSK GKPSARNVLY KGISKGGFLI 70 80 90 100 110 120 FTNYHSRKAH ELDENPQAAW VFYWPKTYKQ VRGEGRVERL TQEESEAYFE TRSYESQIAA 130 140 150 160 170 180 WVSEQSQEIP DREYLITRYK KYREKFQDDV RCPEFWGGFR LIPDRMEFWV GQEHRLHDRF 190 CYLKENQEWK IIRLAP

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO90455.1.
RefSeq	NP_819941.1. NC_002971.3.
3D structure databases
ProteinModelPortal	Q83D18.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1208821.
GenomeReviews	Gene locus CBU_0928 in contig AE016828_GR.
KEGG	cbu:CBU_0928.
NMPDR	fig|227377.1.peg.885.
PATRIC	17930563. VBICoxBur82552_0918.
TIGR	CBU_0928.
Phylogenomic databases
HOGENOM	HBG327559.
OMA	FTFFTNY.
PhylomeDB	Q83D18.
ProtClustDB	CLSK914420.
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_0928-MONOMER.
Family and domain databases
HAMAP	MF_01629. PdxH. [Tree]
InterPro	IPR000659. Pyridox_Oxase. IPR019740. Pyridox_Oxase_CS. IPR011576. Pyridox_Oxase_FMN-bd. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR012349. Split_barrel_FMN-bd. IPR009002. Split_barrel_FMN-bd-related. [Graphical view]
Gene3D	G3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
KO	K00275.
PANTHER	PTHR10851. Pyridox_oxidase. 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_COXBU

Accession

Primary (citable) accession number: Q83D18

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program