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Q0A757 (PDXH_ALHEH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:Mlg_1988
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola ›

Protein attributes

Sequence length196 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.

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.

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000292287

Regions

Nucleotide binding59 – 602FMN By similarity
Nucleotide binding123 – 1242FMN By similarity
Region175 – 1773Substrate binding By similarity

Sites

Binding site441FMN By similarity
Binding site471FMN; via amide nitrogen By similarity
Binding site491Substrate By similarity
Binding site661FMN By similarity
Binding site1061Substrate By similarity
Binding site1101Substrate By similarity
Binding site1141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0A757 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 75E447CD3577A59D

FASTA19622,046
        10         20         30         40         50         60 
MQLLEQALAR FAEVYGRAAE AADVVDHTAC TLATCSASGW PQVRTVLLKG YDERGFAFYT 

        70         80         90        100        110        120 
NRHSRKGQAL AENPRAAVCF HWAPLAEQVV IEGVVTPVAE AEADAYWAGR PRESQIGGWA 

       130        140        150        160        170        180 
SHQSRGLESR EVLEQRVAEY AARFPDGEAV PRPPHWSGYR LAPVRIEFWR ARPGRLHERD 

       190 
VYEHTAEGWC HRLLNP

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MLHE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000453 Genomic DNA. Translation: ABI57330.1.
RefSeqYP_742820.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0A757.
ModBaseSearch...

Protein-protein interaction databases

STRING187272.Mlg_1988.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI57330; ABI57330; Mlg_1988.
GeneID4268531.
KEGGaeh:Mlg_1988.
PATRIC20863229. VBIAlkEhr114327_1983.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAWGGYLIA.
ProtClustDBCLSK727536.

Enzyme and pathway databases

BioCycAEHR187272:GHAX-2044-MONOMER.
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. FMN_binding. 1 hit.
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_ALHEH
AccessionPrimary (citable) accession number: Q0A757
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: October 17, 2006
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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