Pyridoxine/pyridoxamine 5'-phosphate oxidase - Synechocystis sp. (strain PCC 6803 / Kazusa)

Contribute

Send feedback

Read comments (?) or add your own

P74211 (PDXH_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Synonyms:	fprA
Ordered Locus Names:	sll1440

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis ›

Protein attributes

Sequence length	214 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.
Sequence caution	The sequence BAA18303.1 differs from that shown. Reason: Erroneous initiation.

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 – 214

214

Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629

PRO_0000167763

Regions

Nucleotide binding

78 – 79

FMN By similarity

Nucleotide binding

142 – 143

FMN By similarity

Region

10 – 13

Substrate binding By similarity

Region

193 – 195

Substrate binding By similarity

Sites

Binding site

FMN By similarity

Binding site

FMN; via amide nitrogen By similarity

Binding site

Substrate By similarity

Binding site

FMN By similarity

Binding site

125

Substrate By similarity

Binding site

129

Substrate By similarity

Binding site

133

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P74211 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 7516345395EE481C
Show »

FASTA

214

24,587

        10         20         30         40         50         60 
MDGVSLADLR LNYTQGGLIE AEVADHPFAQ FHIWLQQAIA AELPEPNAMT LSTLSEEGHP 

        70         80         90        100        110        120 
VGRMVLLKGL DERGFVFYTN YDSAKGQQLT AHPWAGLVFW WAALERQVRV DGQVEKIDPA 

       130        140        150        160        170        180 
ESDAYFQSRP RGSQLGAWAS PQSRIVGDRQ ELEDNLARWE KQYENQSIPR PPHWGGFRVI 

       190        200        210 
PHRIEFWQGR PSRLHDRLQF NLLDGQWHRQ RLAP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.
[2]	"Cloning of omega 3 desaturase from cyanobacteria and its use in altering the degree of membrane-lipid unsaturation." Sakamoto T., Los D.A., Higashi S., Wada H., Nishida I., Ohmori M., Murata N. Plant Mol. Biol. 26:249-263(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-214.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA18303.1. Different initiation. D13780 Genomic DNA. Translation: BAA02923.1.
PIR	S75844.
RefSeq	NP_441623.1. NC_000911.1. YP_007451505.1. NC_020286.1.
3D structure databases
ProteinModelPortal	P74211.
ModBase	Search...
Protein-protein interaction databases
IntAct	P74211. 3 interactions.
STRING	1148.sll1440.
Proteomic databases
PaxDb	P74211.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA18303; BAA18303; BAA18303.
GeneID	14617168. 953055.
KEGG	syn:sll1440.
PATRIC	23840689. VBISynSp132158_1899.
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HOG000242755.
KO	K00275.
OMA	ERIEFWQ.
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_SYNY3

Accession

Primary (citable) accession number: P74211
Secondary accession number(s): Q55239

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents