Q1DCS1 (PDXH_MYXXD) 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:	MXAN_1295

Organism

Myxococcus xanthus (strain DK 1622) [Complete proteome] [HAMAP]

Taxonomic identifier

246197 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Myxococcus › Myxococcus xanthus

Protein attributes

Sequence length	206 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.
Sequence caution	The sequence ABF87165.1 differs from that shown. Reason: Erroneous initiation.

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 – 206	206	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629		PRO_0000255872
Regions
	Nucleotide binding	70 – 71	2	FMN By similarity
	Nucleotide binding	134 – 135	2	FMN By similarity
	Region	185 – 187	3	Substrate binding By similarity
Sites
	Binding site	55	1	FMN By similarity
	Binding site	58	1	FMN; via amide nitrogen By similarity
	Binding site	60	1	Substrate By similarity
	Binding site	77	1	FMN By similarity
	Binding site	117	1	Substrate By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	125	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1DCS1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: A1D845CDAC8A5196	FASTA	206	23,783
	10 20 30 40 50 60 MHTCRAPFML HRVMIPPDPI QRFAELFERA KQAIAVDPNA MVVATVGDDG RPSARVVLLK 70 80 90 100 110 120 DFDARGFVFY TNHESRKGRE ARAHPYAALC FYWQPLNEQV RVEGRVERVT DAEADAYFQS 130 140 150 160 170 180 RARGSQVGAW ASLQSQPLAT REELEARVAE VEQKYAGQPV PRPPHWSGFR VVPDRIEFWH 190 200 AQESRLHDRH VYLREDGGWR TQMLYP

References

[1]

"Evolution of sensory complexity recorded in a myxobacterial genome." Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A. , Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B. Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DK 1622.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000113 Genomic DNA. Translation: ABF87165.1. Different initiation.
RefSeq	YP_629552.1. NC_008095.1.
3D structure databases
ProteinModelPortal	Q1DCS1.
ModBase	Search...
Protein-protein interaction databases
STRING	246197.MXAN_1295.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABF87165; ABF87165; MXAN_1295.
GeneID	4101861.
KEGG	mxa:MXAN_1295.
PATRIC	22645173. VBIMyxXan43560_1289.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HOG000242755.
KO	K00275.
Enzyme and pathway databases
BioCyc	MXAN246197:GIWU-1282-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_MYXXD

Accession

Primary (citable) accession number: Q1DCS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	May 1, 2013
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program