Q9RNP3 (PDXH_ZYMMO) 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:	ZMO0851

Organism

Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]

Taxonomic identifier

264203 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas › Zymomonas mobilis › Zymomonas mobilis subsp. mobilis

Protein attributes

Sequence length	192 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. HAMAP-Rule MF_01629
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. HAMAP-Rule 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	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 – 192	192	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629		PRO_0000167781
Regions
	Nucleotide binding	56 – 57	2	FMN By similarity
	Nucleotide binding	120 – 121	2	FMN By similarity
	Region	171 – 173	3	Substrate binding By similarity
Sites
	Binding site	41	1	FMN By similarity
	Binding site	44	1	FMN; via amide nitrogen By similarity
	Binding site	46	1	Substrate By similarity
	Binding site	63	1	FMN By similarity
	Binding site	103	1	Substrate By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	111	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RNP3 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 58C8A41EBF7A8FF6	FASTA	192	22,486
	10 20 30 40 50 60 MTQDPHKMFD EWMDEAKKAE TDDPTAMALA TASKQAFPCV RMMLLKGHTK DGFVFFTNLG 70 80 90 100 110 120 SRKGHELLEN PVATLLFHWK KLRRQVRIEG AATLISDEEA DAYFATRARK SQLGAWASEQ 130 140 150 160 170 180 SRPLPARDVF EKRIADIEAR YEGKDVPRPP YWTGFRVSPI RMEFWNDREF RLHERELFTL 190 NDGRWQSEFL YP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of 41E10 fosmid clone of Zymomonas mobilis." Um H.W., Kang H.S. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.
[2]	"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4." Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. , Kang H.L., Lee S.Y., Lee K.J., Kang H.S. Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF179611 Genomic DNA. Translation: AAD53919.1. AE008692 Genomic DNA. Translation: AAV89475.1.
RefSeq	YP_162586.1. NC_006526.2.
3D structure databases
ProteinModelPortal	Q9RNP3.
ModBase	Search...
Protein-protein interaction databases
STRING	264203.ZMO0851.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAV89475; AAV89475; ZMO0851.
GeneID	3187529.
KEGG	zmo:ZMO0851.
PATRIC	32566996. VBIZymMob102260_0802.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HOG000242755.
KO	K00275.
OMA	ERIEFWQ.
ProtClustDB	CLSK2524688.
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_ZYMMO

Accession

Primary (citable) accession number: Q9RNP3
Secondary accession number(s): Q5NP85

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program