Q9A9Q6 (PDXH_CAUCR) 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:	CC_0918

Organism

Caulobacter crescentus (strain ATCC 19089 / CB15) [Reference proteome] [HAMAP]

Taxonomic identifier

190650 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter › Caulobacter crescentus

Protein attributes

Sequence length	222 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 Reference 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 – 222	222	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629		PRO_0000167697
Regions
	Nucleotide binding	86 – 87	2	FMN By similarity
	Nucleotide binding	150 – 151	2	FMN By similarity
	Region	201 – 203	3	Substrate binding By similarity
Sites
	Binding site	71	1	FMN By similarity
	Binding site	74	1	FMN; via amide nitrogen By similarity
	Binding site	76	1	Substrate By similarity
	Binding site	93	1	FMN By similarity
	Binding site	133	1	Substrate By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	141	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9A9Q6 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 8733734B492753FB	FASTA	222	25,197
	10 20 30 40 50 60 MSADPTLIPA SPSEDDYVRQ VREATPPPLL SEEDPFALFA EWLEEAGKKE PNDPNAMTVS 70 80 90 100 110 120 TVDADGMPDS RMVLLKDFDA RGFVFYTNTQ SAKGQELNAH PKAALLFHWK SLRRQVRIRG 130 140 150 160 170 180 TVEPVTEAEA DAYFASRARH SQIGAWASDQ SQPLPDRHAL EKRVAEMGLK FGLGKVPRPP 190 200 210 220 HWSGYRITPV TIEFWRDRPF RLHERLVFDR ADGGWTTKRL FP

References

[1]

"Complete genome sequence of Caulobacter crescentus." Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T., Dodson R.J. , Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19089 / CB15.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005673 Genomic DNA. Translation: AAK22902.1.
PIR	B87363.
RefSeq	NP_419734.1. NC_002696.2.
3D structure databases
ProteinModelPortal	Q9A9Q6.
SMR	Q9A9Q6. Positions 30-211.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK22902; AAK22902; CC_0918.
GeneID	942713.
KEGG	ccr:CC_0918.
PATRIC	21298794. VBICauCre124313_0931.
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HOG000242755.
KO	K00275.
OMA	HWSGFRI.
ProtClustDB	PRK05679.
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_CAUCR

Accession

Primary (citable) accession number: Q9A9Q6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program