SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8X647

- PDXH_ECO57

UniProt

Q8X647 - PDXH_ECO57

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene
pdxH, Z2652, ECs2347
Organism
Escherichia coli O157:H7
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) By similarity.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 By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671FMN By similarity
Binding sitei70 – 701FMN; via amide nitrogen By similarity
Binding sitei72 – 721Substrate By similarity
Binding sitei89 – 891FMN By similarity
Binding sitei129 – 1291Substrate By similarity
Binding sitei133 – 1331Substrate By similarity
Binding sitei137 – 1371Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 832FMN By similarity
Nucleotide bindingi146 – 1472FMN By similarity

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

BioCyciECOL386585:GJFA-2318-MONOMER.
ECOO157:PDXH-MONOMER.
UniPathwayiUPA00190; UER00304.
UPA00190; UER00305.

Names & Taxonomyi

Protein namesi
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 namesi
Name:pdxH
Ordered Locus Names:Z2652, ECs2347
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Pyridoxine/pyridoxamine 5'-phosphate oxidaseUniRule annotationPRO_0000167707Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z2652.

Structurei

3D structure databases

ProteinModelPortaliQ8X647.
SMRiQ8X647. Positions 5-218.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 174Substrate binding By similarity
Regioni197 – 1993Substrate binding By similarity

Sequence similaritiesi

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.

Q8X647-1 [UniParc]FASTAAdd to Basket

« Hide

MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP    50
TAMVVATVDE HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS 100
LLFPWHTLER QVMVIGKAER LSTLEVMKYF HSRPRDSQIG SWVSKQSSRI 150
SARGILESKF LELKQKFQQG EVPLPSFWGG FRVSLEQIEF WQGGEHRLHD 200
RFLYQRENDA WKIDRLAP 218
Length:218
Mass (Da):25,561
Last modified:March 1, 2002 - v1
Checksum:i95582F0EA6D83923
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG56627.1.
BA000007 Genomic DNA. Translation: BAB35770.1.
PIRiC90922.
G85770.
RefSeqiNP_288074.1. NC_002655.2.
NP_310374.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG56627; AAG56627; Z2652.
BAB35770; BAB35770; BAB35770.
GeneIDi912730.
961593.
KEGGiece:Z2652.
ecs:ECs2347.
PATRICi18354022. VBIEscCol44059_2224.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG56627.1 .
BA000007 Genomic DNA. Translation: BAB35770.1 .
PIRi C90922.
G85770.
RefSeqi NP_288074.1. NC_002655.2.
NP_310374.1. NC_002695.1.

3D structure databases

ProteinModelPortali Q8X647.
SMRi Q8X647. Positions 5-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z2652.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG56627 ; AAG56627 ; Z2652 .
BAB35770 ; BAB35770 ; BAB35770 .
GeneIDi 912730.
961593.
KEGGi ece:Z2652.
ecs:ECs2347.
PATRICi 18354022. VBIEscCol44059_2224.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00190 ; UER00304 .
UPA00190 ; UER00305 .
BioCyci ECOL386585:GJFA-2318-MONOMER.
ECOO157:PDXH-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiPDXH_ECO57
AccessioniPrimary (citable) accession number: Q8X647
Secondary accession number(s): Q7ADK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 86 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

Similar proteinsi