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Protein

F420H(2)-dependent reductase Rv1155

Gene

Rv1155

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

Functioni

F420H2-dependent reductase able to catalyze the reduction of biliverdin-IXalpha to bilirubin-IXalpha in vitro. However, kinetic parameters show that it is less efficient than the biliverdin reductase Rv2074 and suggest biliverdin-IXalpha is unlikely to be the native substrate of Rv1155, which probably catalyzes the reduction of an alternative molecule in vivo (PubMed:27364382). Binds coenzyme F420, but does not bind FMN or other flavins (PubMed:25644473). Cannot use pyridoxine 5'-phosphate, pyridoxamine 5'-phosphate, pyridoxal 5'-phosphate (PLP), the anti-tuberculosis drug PA-824 or aflatoxin analogs as substrates (PubMed:25644473).2 Publications

Kineticsi

kcat is 0.024 sec(-1) for the reduction of biliverdin.1 Publication
  1. KM=82.8 µM for biliverdin1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei32Coenzyme F4201 Publication1
    Binding sitei37Coenzyme F420; via amide nitrogen1 Publication1
    Binding sitei50Coenzyme F420; via carbonyl oxygen1 Publication1
    Binding sitei138Coenzyme F420; shared with dimeric partner1 Publication1

    GO - Molecular functioni

    • coenzyme F420 binding Source: UniProtKB
    • FMN binding Source: MTBBASE
    • protein homodimerization activity Source: UniProtKB
    • pyridoxal phosphate binding Source: MTBBASE
    • pyridoxamine-phosphate oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    • vitamin B6 metabolic process Source: MTBBASE

    Keywordsi

    Molecular functionOxidoreductase

    Enzyme and pathway databases

    BRENDAi1.4.3.5. 3445.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F420H(2)-dependent reductase Rv11551 Publication (EC:1.-.-.-1 Publication)
    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 – 147F420H(2)-dependent reductase Rv1155Add BLAST147

    Proteomic databases

    PaxDbiO06553.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    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
    Regioni56 – 60Coenzyme F420-binding1 Publication5
    Regioni77 – 79Coenzyme F420-binding; shared with dimeric partner1 Publication3

    Sequence similaritiesi

    Phylogenomic databases

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

    Family and domain databases

    Gene3Di2.30.110.10. 1 hit.
    InterProiView protein in InterPro
    IPR019920. F420-binding_dom_put.
    IPR011576. Pyridox_Oxase_put.
    IPR012349. Split_barrel_FMN-bd.
    PfamiView protein in Pfam
    PF01243. Putative_PNPOx. 1 hit.
    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.

    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.

    Organism-specific databases

    TubercuListiRv1155.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BRENDAi1.4.3.5. 3445.

    Miscellaneous databases

    EvolutionaryTraceiO06553.

    Family and domain databases

    Gene3Di2.30.110.10. 1 hit.
    InterProiView protein in InterPro
    IPR019920. F420-binding_dom_put.
    IPR011576. Pyridox_Oxase_put.
    IPR012349. Split_barrel_FMN-bd.
    PfamiView protein in Pfam
    PF01243. Putative_PNPOx. 1 hit.
    SUPFAMiSSF50475. SSF50475. 1 hit.
    TIGRFAMsiTIGR03618. Rv1155_F420. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiF420R_MYCTU
    AccessioniPrimary (citable) accession number: O06553
    Secondary accession number(s): L0T7G6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2010
    Last sequence update: July 1, 1997
    Last modified: June 7, 2017
    This is version 112 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to be an FMN-dependent pyridoxine 5'-phosphate oxidase.1 Publication
    FMN and PLP are seen in the crystal structures published in PubMed:16239726, however, the enzyme does not bind these compounds in vitro, and the complexes obtained in the crystal structures may be the result of weak FMN/PLP binding that is stabilized by the crystal lattice.1 Publication

    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
    3. SIMILARITY comments
      Index of protein domains and families

    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.