Reviewed, UniProtKB/Swiss-Prot Q11U72 (PDXH_CYTH3)

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:	CHU_1775

Organism

Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469) [Complete proteome] [HAMAP]

Taxonomic identifier

269798 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Flexibacteraceae › Cytophaga

Protein attributes

Sequence length	215 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
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 – 215	215	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000255863
Regions
	Nucleotide binding	77 – 78	2	FMN By similarity
	Nucleotide binding	141 – 142	2	FMN By similarity
	Region	9 – 12	4	Substrate binding By similarity
	Region	193 – 195	3	Substrate binding By similarity
Sites
	Binding site	62	1	FMN By similarity
	Binding site	65	1	FMN; via amide nitrogen By similarity
	Binding site	67	1	Substrate By similarity
	Binding site	84	1	FMN By similarity
	Binding site	124	1	Substrate By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q11U72-1 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 46492608793B9759	FASTA	215	24,745
	10 20 30 40 50 60 MKTNLADIRK EYSSRSLDTK DILPSPVEQF RLWLNQALEA GALEATAMNL ATVNEAGKPA 70 80 90 100 110 120 SRIVLLKGIE HGSFVFYTNY KSHKGSDITH NSFGALNFFW PELERQVRIE GKITKVSPED 130 140 150 160 170 180 SDTYFNSRPY QSKIGAWVSD QSKEVASREE LESKITYYEN KYPEGSVVPR PAHWGGYTLK 190 200 210 PAYFEFWQGR PSRLHDRIVY DLEGDIRWNV FRICP

References

[1]

"Genome sequence of the cellulolytic gliding bacterium Cytophaga hutchinsonii." Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B., McBride M.J. Appl. Environ. Microbiol. 73:3536-3546(2007) [PubMed: 17400776] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000383 Genomic DNA. Translation: ABG59042.1.
RefSeq	YP_678384.1.
3D structure databases
SMR	Q11U72. Positions 16-215.
ModBase	Search...
Protein-protein interaction databases
STRING	Q11U72.
Genome annotation databases
GeneID	4186847.
GenomeReviews	Gene locus CHU_1775 in contig CP000383_GR.
KEGG	chu:CHU_1775.
NMPDR	fig|269798.12.peg.1691.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HBG327559.
OMA	EVEPNAM.
Enzyme and pathway databases
BioCyc	CHUT269798:CHU_1775-MONOMER.
Family and domain databases
HAMAP	MF_01629. PdxH. [Tree]
InterPro	IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR011576. PyridoxamineP_oxidase_FMN-bd. IPR009002. Split_barrel_FMN-bd_related. 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]
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_CYTH3

Accession

Primary (citable) accession number: Q11U72

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	August 22, 2006
Last modified:	February 9, 2010
This is version 30 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)