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Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
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).UniRule annotation

Catalytic activityi

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

Cofactori

FMNUniRule annotationNote: Binds 1 FMN per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601FMNUniRule annotation
Binding sitei63 – 631FMN; via amide nitrogenUniRule annotation
Binding sitei65 – 651SubstrateUniRule annotation
Binding sitei82 – 821FMNUniRule annotation
Binding sitei122 – 1221SubstrateUniRule annotation
Binding sitei126 – 1261SubstrateUniRule annotation
Binding sitei130 – 1301SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi75 – 762FMNUniRule annotation
Nucleotide bindingi139 – 1402FMNUniRule annotation

GO - Molecular functioni

  1. FMN binding Source: UniProtKB-HAMAP
  2. pyridoxamine-phosphate oxidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pyridoxine biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciNGON242231:GI2G-625-MONOMER.
UniPathwayiUPA00190; UER00304.
UPA00190; UER00305.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxine/pyridoxamine 5'-phosphate oxidaseUniRule annotation (EC:1.4.3.5UniRule annotation)
Alternative name(s):
PNP/PMP oxidaseUniRule annotation
Short name:
PNPOxUniRule annotation
Pyridoxal 5'-phosphate synthaseUniRule annotation
Gene namesi
Name:pdxHUniRule annotation
Ordered Locus Names:NGO0658
OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Taxonomic identifieri242231 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000535: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Pyridoxine/pyridoxamine 5'-phosphate oxidasePRO_0000167725Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi242231.NGO0658.

Structurei

3D structure databases

ProteinModelPortaliQ5F8V2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 104Substrate bindingUniRule annotation
Regioni189 – 1913Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the pyridoxamine 5'-phosphate oxidase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0259.
HOGENOMiHOG000242755.
KOiK00275.
OMAiPHWGGFR.
OrthoDBiEOG60KN2Z.

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. PTHR10851. 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.

Q5F8V2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDLHNIREDY SKRELSEADC ADNPIEQFER WLDEAVRAEV NEPTAVNVAA
60 70 80 90 100
VDGRGRPNSR MVLLKEVNSE GFVFFTNYHS RKGRSLELNP FAAMTFFWPE
110 120 130 140 150
LERQVRVEGR VGRLAEKLSD EYFESRPYQS RLGAWASAQS EVIPNKAVLV
160 170 180 190 200
AKAAAVGLKH PLHVPRPPHW GGYIVIPDLI EFWQGRPSRL HDRIQYRLLD
210
GGWIRERLSP
Length:210
Mass (Da):24,177
Last modified:March 15, 2005 - v1
Checksum:iFF9C40DA2A1B5BB9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004969 Genomic DNA. Translation: AAW89385.1.
RefSeqiYP_207797.1. NC_002946.2.

Genome annotation databases

EnsemblBacteriaiAAW89385; AAW89385; NGO0658.
GeneIDi3282467.
KEGGingo:NGO0658.
PATRICi20334410. VBINeiGon24812_0777.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004969 Genomic DNA. Translation: AAW89385.1.
RefSeqiYP_207797.1. NC_002946.2.

3D structure databases

ProteinModelPortaliQ5F8V2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi242231.NGO0658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW89385; AAW89385; NGO0658.
GeneIDi3282467.
KEGGingo:NGO0658.
PATRICi20334410. VBINeiGon24812_0777.

Phylogenomic databases

eggNOGiCOG0259.
HOGENOMiHOG000242755.
KOiK00275.
OMAiPHWGGFR.
OrthoDBiEOG60KN2Z.

Enzyme and pathway databases

UniPathwayiUPA00190; UER00304.
UPA00190; UER00305.
BioCyciNGON242231:GI2G-625-MONOMER.

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. PTHR10851. 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. "The complete genome sequence of Neisseria gonorrhoeae."
    Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
    , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700825 / FA 1090.

Entry informationi

Entry nameiPDXH_NEIG1
AccessioniPrimary (citable) accession number: Q5F8V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 15, 2005
Last modified: January 7, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.