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Protein

Putative pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

Rv1155

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371FMN1 Publication
Binding sitei50 – 501FMN; via carbonyl oxygen1 Publication
Binding sitei79 – 791Pyridoxal phosphate1 Publication

GO - Molecular functioni

  1. FMN binding Source: MTBBASE
  2. protein homodimerization activity Source: MTBBASE
  3. pyridoxal phosphate binding Source: MTBBASE
  4. pyridoxamine-phosphate oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. vitamin B6 metabolic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciMTBRV:RV1155-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Ordered Locus Names:Rv1155
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001584: Chromosome

Organism-specific databases

TubercuListiRv1155.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Putative pyridoxine/pyridoxamine 5'-phosphate oxidasePRO_0000399901Add
BLAST

Proteomic databases

PRIDEiO06553.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi83332.Rv1155.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1510Combined sources
Beta strandi18 – 258Combined sources
Beta strandi31 – 377Combined sources
Beta strandi39 – 413Combined sources
Turni42 – 454Combined sources
Beta strandi46 – 527Combined sources
Helixi56 – 638Combined sources
Beta strandi66 – 727Combined sources
Beta strandi74 – 774Combined sources
Beta strandi79 – 857Combined sources
Helixi98 – 11013Combined sources
Helixi117 – 12610Combined sources
Beta strandi129 – 1357Combined sources
Beta strandi138 – 1425Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W9AX-ray1.80A/B1-147[»]
1XXOX-ray1.80A/B1-147[»]
1Y30X-ray2.20A/B1-147[»]
2AQ6X-ray1.70A/B1-147[»]
ProteinModelPortaliO06553.
SMRiO06553. Positions 5-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO06553.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 354FMN binding
Regioni34 – 352Pyridoxal phosphate binding
Regioni55 – 573FMN binding
Regioni55 – 573Pyridoxal phosphate binding

Phylogenomic databases

eggNOGiNOG07001.
HOGENOMiHOG000022434.
InParanoidiO06553.
KOiK07005.
OMAiDRAKTRN.
OrthoDBiEOG6VB6XZ.
PhylomeDBiO06553.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR019920. F420-binding_dom_put.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR03618. Rv1155_F420. 1 hit.

Sequencei

Sequence statusi: Complete.

O06553-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARQVFDDKL LAVISGNSIG VLATIKHDGR PQLSNVQYHF DPRKLLIQVS
60 70 80 90 100
IAEPRAKTRN LRRDPRASIL VDADDGWSYA VAEGTAQLTP PAAAPDDDTV
110 120 130 140
EALIALYRNI AGEHSDWDDY RQAMVTDRRV LLTLPISHVY GLPPGMR
Length:147
Mass (Da):16,301
Last modified:July 1, 1997 - v1
Checksum:iDAF63639A04D6A0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43910.1.
PIRiD70555.
RefSeqiNP_215671.1. NC_000962.3.
YP_006514527.1. NC_018143.2.

Genome annotation databases

EnsemblBacteriaiCCP43910; CCP43910; Rv1155.
GeneIDi13319731.
885604.
KEGGimtu:Rv1155.
mtv:RVBD_1155.
PATRICi18151117. VBIMycTub87468_1296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43910.1.
PIRiD70555.
RefSeqiNP_215671.1. NC_000962.3.
YP_006514527.1. NC_018143.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W9AX-ray1.80A/B1-147[»]
1XXOX-ray1.80A/B1-147[»]
1Y30X-ray2.20A/B1-147[»]
2AQ6X-ray1.70A/B1-147[»]
ProteinModelPortaliO06553.
SMRiO06553. Positions 5-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1155.

Proteomic databases

PRIDEiO06553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43910; CCP43910; Rv1155.
GeneIDi13319731.
885604.
KEGGimtu:Rv1155.
mtv:RVBD_1155.
PATRICi18151117. VBIMycTub87468_1296.

Organism-specific databases

TubercuListiRv1155.

Phylogenomic databases

eggNOGiNOG07001.
HOGENOMiHOG000022434.
InParanoidiO06553.
KOiK07005.
OMAiDRAKTRN.
OrthoDBiEOG6VB6XZ.
PhylomeDBiO06553.

Enzyme and pathway databases

BioCyciMTBRV:RV1155-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO06553.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR019920. F420-binding_dom_put.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR03618. Rv1155_F420. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  3. "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.
  4. "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.

Entry informationi

Entry nameiY1155_MYCTU
AccessioniPrimary (citable) accession number: O06553
Secondary accession number(s): L0T7G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: July 1, 1997
Last modified: January 7, 2015
This is version 101 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.