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P74211 (PDXH_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Protein existenceInferred 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 BAA18303.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 214214Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167763

Regions

Nucleotide binding78 – 792FMN By similarity
Nucleotide binding142 – 1432FMN By similarity
Region10 – 134Substrate binding By similarity
Region193 – 1953Substrate binding By similarity

Sites

Binding site631FMN By similarity
Binding site661FMN; via amide nitrogen By similarity
Binding site681Substrate By similarity
Binding site851FMN By similarity
Binding site1251Substrate By similarity
Binding site1291Substrate By similarity
Binding site1331Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P74211 [UniParc].

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

FASTA21424,587
        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' 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. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., 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.
PIRS75844.
RefSeqNP_441623.1. NC_000911.1.
YP_007451505.1. NC_020286.1.

3D structure databases

ProteinModelPortalP74211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP74211. 3 interactions.
STRING1148.sll1440.

Proteomic databases

PaxDbP74211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA18303; BAA18303; BAA18303.
GeneID953055.
KEGGsyn:sll1440.
syz:MYO_117460.
PATRIC23840689. VBISynSp132158_1899.

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.
PhylomeDBP74211.

Enzyme and pathway databases

UniPathwayUPA00190; UER00304.
UPA00190; UER00305.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
HAMAPMF_01629. PdxH.
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERPTHR10851. PTHR10851. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. SSF50475. 1 hit.
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_SYNY3
AccessionPrimary (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: July 9, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways