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O06553 (Y1155_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative 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
Ordered Locus Names:Rv1155
OrganismMycobacterium tuberculosis (strain ATCC 25618 / H37Rv) [Reference proteome] [HAMAP]
Taxonomic identifier83332 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2.

Subunit structure

Homodimer. Ref.2 Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 147147Putative pyridoxine/pyridoxamine 5'-phosphate oxidase
PRO_0000399901

Regions

Region32 – 354FMN binding
Region34 – 352Pyridoxal phosphate binding
Region55 – 573FMN binding
Region55 – 573Pyridoxal phosphate binding

Sites

Binding site371FMN
Binding site501FMN; via carbonyl oxygen
Binding site791Pyridoxal phosphate

Secondary structure

........................... 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O06553 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: DAF63639A04D6A0D

FASTA14716,301
        10         20         30         40         50         60 
MARQVFDDKL LAVISGNSIG VLATIKHDGR PQLSNVQYHF DPRKLLIQVS IAEPRAKTRN 

        70         80         90        100        110        120 
LRRDPRASIL VDADDGWSYA VAEGTAQLTP PAAAPDDDTV EALIALYRNI AGEHSDWDDY 

       130        140 
RQAMVTDRRV LLTLPISHVY GLPPGMR 

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Structures of Mycobacterium tuberculosispyridoxine 5'-phosphate oxidase and its complexes with flavin mononucleotide and pyridoxal 5'-phosphate."
Biswal B.K., Cherney M.M., Wang M., Garen C., James M.N.
Acta Crystallogr. D 61:1492-1499(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH FMN AND PYRIDOXAL PHOSPHATE, SUBUNIT.
[3]"Crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis."
Canaan S., Sulzenbacher G., Roig-Zamboni V., Scappuccini-Calvo L., Frassinetti F., Maurin D., Cambillau C., Bourne Y.
FEBS Lett. 579:215-221(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL123456 Genomic DNA. Translation: CCP43910.1.
PIRD70555.
RefSeqNP_215671.1. NC_000962.3.
YP_006514527.1. NC_018143.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W9AX-ray1.80A/B1-147[»]
1XXOX-ray1.80A/B1-147[»]
1Y30X-ray2.20A/B1-147[»]
2AQ6X-ray1.70A/B1-147[»]
ProteinModelPortalO06553.
SMRO06553. Positions 5-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING83332.Rv1155.

Proteomic databases

PRIDEO06553.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCP43910; CCP43910; Rv1155.
GeneID13319731.
885604.
KEGGmtu:Rv1155.
mtv:RVBD_1155.
PATRIC18151117. VBIMycTub87468_1296.

Organism-specific databases

TubercuListRv1155.

Phylogenomic databases

eggNOGNOG07001.
HOGENOMHOG000022434.
KOK07005.
OMADRAKTRN.
OrthoDBEOG6VB6XZ.
ProtClustDBCLSK790983.

Enzyme and pathway databases

BioCycMTBRV:RV1155-MONOMER.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
InterProIPR019920. F420-binding_dom_put.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamPF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
SUPFAMSSF50475. SSF50475. 1 hit.
TIGRFAMsTIGR03618. Rv1155_F420. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO06553.

Entry information

Entry nameY1155_MYCTU
AccessionPrimary (citable) accession number: O06553
Secondary accession number(s): L0T7G6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references