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Protein

Putative pyridoxamine 5'-phosphate oxidase

Gene

F57B9.1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).By similarity

Catalytic activityi

Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2.
Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2.

Cofactori

FMNBy similarityNote: Binds 1 FMN per subunit.By similarity

Pathwayi: pyridoxal 5'-phosphate salvage

This protein is involved in step 1 of the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Putative pyridoxamine 5'-phosphate oxidase (F57B9.1)
This subpathway is part of the pathway pyridoxal 5'-phosphate salvage, which is itself part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate, the pathway pyridoxal 5'-phosphate salvage and in Cofactor metabolism.

Pathwayi: pyridoxal 5'-phosphate salvage

This protein is involved in step 1 of the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxine 5'-phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Putative pyridoxamine 5'-phosphate oxidase (F57B9.1)
This subpathway is part of the pathway pyridoxal 5'-phosphate salvage, which is itself part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxine 5'-phosphate, the pathway pyridoxal 5'-phosphate salvage and in Cofactor metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771Pyridoxal 5'-phosphateBy similarity
Binding sitei116 – 1161FMNBy similarity
Binding sitei134 – 1341Pyridoxal 5'-phosphateBy similarity
Binding sitei138 – 1381Pyridoxal 5'-phosphateBy similarity
Binding sitei142 – 1421Pyridoxal 5'-phosphateBy similarity
Binding sitei199 – 1991FMNBy similarity
Binding sitei209 – 2091FMNBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi72 – 754FMNBy similarity
Nucleotide bindingi87 – 882FMNBy similarity
Nucleotide bindingi93 – 942FMNBy similarity
Nucleotide bindingi151 – 1522FMNBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

ReactomeiR-CEL-964975. Vitamins B6 activation to pyridoxal phosphate.
UniPathwayiUPA01068; UER00304.
UPA01068; UER00305.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative pyridoxamine 5'-phosphate oxidase (EC:1.4.3.5)
Alternative name(s):
PNP/PMP oxidase
Short name:
PNPOx
Gene namesi
ORF Names:F57B9.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiF57B9.1; CE44186; WBGene00018996.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226Putative pyridoxamine 5'-phosphate oxidasePRO_0000167788Add
BLAST

Proteomic databases

EPDiQ20939.
PaxDbiQ20939.
PRIDEiQ20939.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi41187. 1 interaction.
IntActiQ20939. 1 interaction.
STRINGi6239.F57B9.1.

Structurei

3D structure databases

ProteinModelPortaliQ20939.
SMRiQ20939. Positions 25-226.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 194Pyridoxal 5'-phosphate bindingBy similarity
Regioni205 – 2073Pyridoxal 5'-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2586. Eukaryota.
COG0259. LUCA.
GeneTreeiENSGT00390000011219.
HOGENOMiHOG000242755.
InParanoidiQ20939.
KOiK00275.
OMAiPEHWGGY.
OrthoDBiEOG7B8S4P.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
HAMAPiMF_01629. PdxH.
InterProiIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERiPTHR10851:SF0. PTHR10851:SF0. 1 hit.
PfamiPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR00558. pdxH. 1 hit.
PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q20939-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METPSIDIQN IRAKYLNSHD PYLLESKLPT TSPFELFDIW FRNVASQSDL
60 70 80 90 100
TFEEINAVSL STVGKDLRPS SRMVLLKAYT PTGFSFYTNY TSRKGNQLEE
110 120 130 140 150
NPNAAMLFYW PKVNRQIRVE GVVEKLPDEM AVAYWNSRPV ASRIGSKSSD
160 170 180 190 200
QSKVVPDREF LESKKVALTE LSVREGAQAI TKPESWGGYH LIPRYFEFWQ
210 220
GQSDRLHDRI VFERDVDVWL LKRLSP
Length:226
Mass (Da):26,101
Last modified:October 19, 2011 - v2
Checksum:i99E80C34C740AE2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081266 Genomic DNA. Translation: CCD70322.1.
PIRiA88494.
RefSeqiNP_498518.2. NM_066117.3.
UniGeneiCel.10391.

Genome annotation databases

EnsemblMetazoaiF57B9.1; F57B9.1; WBGene00018996.
GeneIDi175973.
KEGGicel:CELE_F57B9.1.
UCSCiF57B9.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081266 Genomic DNA. Translation: CCD70322.1.
PIRiA88494.
RefSeqiNP_498518.2. NM_066117.3.
UniGeneiCel.10391.

3D structure databases

ProteinModelPortaliQ20939.
SMRiQ20939. Positions 25-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi41187. 1 interaction.
IntActiQ20939. 1 interaction.
STRINGi6239.F57B9.1.

Proteomic databases

EPDiQ20939.
PaxDbiQ20939.
PRIDEiQ20939.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF57B9.1; F57B9.1; WBGene00018996.
GeneIDi175973.
KEGGicel:CELE_F57B9.1.
UCSCiF57B9.1. c. elegans.

Organism-specific databases

CTDi175973.
WormBaseiF57B9.1; CE44186; WBGene00018996.

Phylogenomic databases

eggNOGiKOG2586. Eukaryota.
COG0259. LUCA.
GeneTreeiENSGT00390000011219.
HOGENOMiHOG000242755.
InParanoidiQ20939.
KOiK00275.
OMAiPEHWGGY.
OrthoDBiEOG7B8S4P.

Enzyme and pathway databases

UniPathwayiUPA01068; UER00304.
UPA01068; UER00305.
ReactomeiR-CEL-964975. Vitamins B6 activation to pyridoxal phosphate.

Miscellaneous databases

NextBioi890562.
PROiQ20939.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
HAMAPiMF_01629. PdxH.
InterProiIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERiPTHR10851:SF0. PTHR10851:SF0. 1 hit.
PfamiPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR00558. pdxH. 1 hit.
PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiPDXH_CAEEL
AccessioniPrimary (citable) accession number: Q20939
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 19, 2011
Last modified: May 11, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.