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A7ZMA0

- PDXH_ECO24

UniProt

A7ZMA0 - PDXH_ECO24

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Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Status
Reviewed - 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

Binds 1 FMN per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671FMNUniRule annotation
Binding sitei70 – 701FMN; via amide nitrogenUniRule annotation
Binding sitei72 – 721SubstrateUniRule annotation
Binding sitei89 – 891FMNUniRule annotation
Binding sitei129 – 1291SubstrateUniRule annotation
Binding sitei133 – 1331SubstrateUniRule annotation
Binding sitei137 – 1371SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 832FMNUniRule annotation
Nucleotide bindingi146 – 1472FMNUniRule 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

BioCyciECOL331111:GH7P-1833-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:EcE24377A_1848
OrganismiEscherichia coli O139:H28 (strain E24377A / ETEC)
Taxonomic identifieri331111 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001122: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Pyridoxine/pyridoxamine 5'-phosphate oxidasePRO_1000069691Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi331111.EcE24377A_1848.

Structurei

3D structure databases

ProteinModelPortaliA7ZMA0.
SMRiA7ZMA0. Positions 5-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 174Substrate bindingUniRule annotation
Regioni197 – 1993Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0259.
HOGENOMiHOG000242755.
KOiK00275.
OMAiNMGSRKA.
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.

A7ZMA0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP
60 70 80 90 100
TAMVVATVDE HAQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS
110 120 130 140 150
LLFPWHTLER QVMVIGKAER LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI
160 170 180 190 200
SARGILESKF LELKQKFQQG EVPLPSFWGG FRISLEQIEF WQGGEHRLHD
210
RFLYQRENDA WKIDRLAP
Length:218
Mass (Da):25,573
Last modified:October 23, 2007 - v1
Checksum:iD4E7CB0742CF5A39
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000800 Genomic DNA. Translation: ABV21134.1.
RefSeqiYP_001462929.1. NC_009801.1.

Genome annotation databases

EnsemblBacteriaiABV21134; ABV21134; EcE24377A_1848.
GeneIDi5587953.
KEGGiecw:EcE24377A_1848.
PATRICi18292955. VBIEscCol31211_2133.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000800 Genomic DNA. Translation: ABV21134.1 .
RefSeqi YP_001462929.1. NC_009801.1.

3D structure databases

ProteinModelPortali A7ZMA0.
SMRi A7ZMA0. Positions 5-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331111.EcE24377A_1848.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV21134 ; ABV21134 ; EcE24377A_1848 .
GeneIDi 5587953.
KEGGi ecw:EcE24377A_1848.
PATRICi 18292955. VBIEscCol31211_2133.

Phylogenomic databases

eggNOGi COG0259.
HOGENOMi HOG000242755.
KOi K00275.
OMAi NMGSRKA.
OrthoDBi EOG60KN2Z.

Enzyme and pathway databases

UniPathwayi UPA00190 ; UER00304 .
UPA00190 ; UER00305 .
BioCyci ECOL331111:GH7P-1833-MONOMER.

Family and domain databases

Gene3Di 2.30.110.10. 1 hit.
HAMAPi MF_01629. PdxH.
InterProi IPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view ]
PANTHERi PTHR10851. PTHR10851. 1 hit.
Pfami PF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMi SSF50475. SSF50475. 1 hit.
TIGRFAMsi TIGR00558. pdxH. 1 hit.
PROSITEi PS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E24377A / ETEC.

Entry informationi

Entry nameiPDXH_ECO24
AccessioniPrimary (citable) accession number: A7ZMA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: October 1, 2014
This is version 51 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

Documents

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

External Data

Dasty 3