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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)DescriptionActionsGraphical viewLength
Binding sitei37FMN1 Publication1
Binding sitei50FMN; via carbonyl oxygen1 Publication1
Binding sitei79Pyridoxal phosphate1 Publication1

GO - Molecular functioni

  • FMN binding Source: MTBBASE
  • protein homodimerization activity Source: MTBBASE
  • pyridoxal phosphate binding Source: MTBBASE
  • pyridoxamine-phosphate oxidase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-5322-MONOMER.
BRENDAi1.4.3.5. 3445.

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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1155.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003999011 – 147Putative pyridoxine/pyridoxamine 5'-phosphate oxidaseAdd BLAST147

Proteomic databases

PaxDbiO06553.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: MTBBASE

Protein-protein interaction databases

STRINGi83332.Rv1155.

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 15Combined sources10
Beta strandi18 – 25Combined sources8
Beta strandi31 – 37Combined sources7
Beta strandi39 – 41Combined sources3
Turni42 – 45Combined sources4
Beta strandi46 – 52Combined sources7
Helixi56 – 63Combined sources8
Beta strandi66 – 72Combined sources7
Beta strandi74 – 77Combined sources4
Beta strandi79 – 85Combined sources7
Helixi98 – 110Combined sources13
Helixi117 – 126Combined sources10
Beta strandi129 – 135Combined sources7
Beta strandi138 – 142Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W9AX-ray1.80A/B1-147[»]
1XXOX-ray1.80A/B1-147[»]
1Y30X-ray2.20A/B1-147[»]
2AQ6X-ray1.70A/B1-147[»]
4QVBX-ray2.30A/B2-147[»]
ProteinModelPortaliO06553.
SMRiO06553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO06553.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 35FMN binding4
Regioni34 – 35Pyridoxal phosphate binding2
Regioni55 – 57FMN binding3
Regioni55 – 57Pyridoxal phosphate binding3

Phylogenomic databases

eggNOGiENOG410905P. Bacteria.
ENOG4111NHN. LUCA.
HOGENOMiHOG000022434.
InParanoidiO06553.
KOiK07005.
OMAiDPRASYH.
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.
WP_003898745.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP43910; CCP43910; Rv1155.
GeneIDi885604.
KEGGimtu:Rv1155.
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.
WP_003898745.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W9AX-ray1.80A/B1-147[»]
1XXOX-ray1.80A/B1-147[»]
1Y30X-ray2.20A/B1-147[»]
2AQ6X-ray1.70A/B1-147[»]
4QVBX-ray2.30A/B2-147[»]
ProteinModelPortaliO06553.
SMRiO06553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1155.

Proteomic databases

PaxDbiO06553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43910; CCP43910; Rv1155.
GeneIDi885604.
KEGGimtu:Rv1155.
PATRICi18151117. VBIMycTub87468_1296.

Organism-specific databases

TubercuListiRv1155.

Phylogenomic databases

eggNOGiENOG410905P. Bacteria.
ENOG4111NHN. LUCA.
HOGENOMiHOG000022434.
InParanoidiO06553.
KOiK07005.
OMAiDPRASYH.
PhylomeDBiO06553.

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-5322-MONOMER.
BRENDAi1.4.3.5. 3445.

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...

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: November 2, 2016
This is version 110 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

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 one 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.