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Protein

Flavin reductase (NADPH)

Gene

BLVRB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe3+ iron to Fe2+ in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin.1 Publication

Catalytic activityi

Reduced riboflavin + NADP+ = riboflavin + NADPH.2 Publications
Bilirubin + NAD(P)+ = biliverdin + NAD(P)H.3 Publications

Enzyme regulationi

Mesobiliverdin acts as competitve inhibitor for flavin reduction, indicating that flavin and tetrapyrrole substrates compete for the same site.1 Publication

Kineticsi

  1. KM=36 µM for NADP2 Publications
  2. KM=5.6 mM for NADH2 Publications
  3. KM=0.3 µM for biliverdin IX-beta2 Publications
  4. KM=52 µM for FMN2 Publications
  5. KM=125 µM for FAD2 Publications
  6. KM=53 µM for riboflavin2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei35NADP1
    Binding sitei132NADP1
    Binding sitei153Substrate1
    Binding sitei154NADP; via amide nitrogen1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi10 – 15NADP6
    Nucleotide bindingi54 – 55NADP2
    Nucleotide bindingi75 – 78NADP4

    GO - Molecular functioni

    • biliverdin reductase activity Source: UniProtKB
    • riboflavin reductase (NADPH) activity Source: UniProtKB

    GO - Biological processi

    • heme catabolic process Source: UniProtKB

    Keywordsi

    Molecular functionOxidoreductase
    LigandNADP

    Enzyme and pathway databases

    BRENDAi1.3.1.24 2681
    1.5.1.30 2681
    ReactomeiR-HSA-189483 Heme degradation
    SABIO-RKiP30043

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Flavin reductase (NADPH) (EC:1.5.1.302 Publications)
    Short name:
    FR
    Alternative name(s):
    Biliverdin reductase B (EC:1.3.1.243 Publications)
    Short name:
    BVR-B
    Biliverdin-IX beta-reductase
    Green heme-binding protein
    Short name:
    GHBP
    NADPH-dependent diaphorase
    NADPH-flavin reductase
    Short name:
    FLR
    Gene namesi
    Name:BLVRB
    Synonyms:FLR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 19

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000090013.9
    HGNCiHGNC:1063 BLVRB
    MIMi600941 gene
    neXtProtiNX_P30043

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi153H → A: Reduced affinity for biliverdin. 1 Publication1

    Organism-specific databases

    DisGeNETi645
    OpenTargetsiENSG00000090013
    PharmGKBiPA25374

    Chemistry databases

    DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB02073 Biliverdine Ix Alpha
    DB04363 Mesobiliverdin Iv Alpha
    DB00157 NADH
    DB00140 Riboflavin
    DB03247 Riboflavin Monophosphate

    Polymorphism and mutation databases

    BioMutaiBLVRB
    DMDMi1706870

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved5 Publications
    ChainiPRO_00000649482 – 206Flavin reductase (NADPH)Add BLAST205

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei42PhosphoserineCombined sources1
    Modified residuei82PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiP30043
    PaxDbiP30043
    PeptideAtlasiP30043
    PRIDEiP30043
    ProteomicsDBi54623
    TopDownProteomicsiP30043

    2D gel databases

    DOSAC-COBS-2DPAGEiP30043
    REPRODUCTION-2DPAGEiIPI00783862
    SWISS-2DPAGEiP30043
    UCD-2DPAGEiP30043

    PTM databases

    iPTMnetiP30043
    PhosphoSitePlusiP30043

    Expressioni

    Tissue specificityi

    Predominantly expressed in liver and erythrocytes. At lower levels in heart, lung, adrenal gland and cerebrum.1 Publication

    Gene expression databases

    BgeeiENSG00000090013
    CleanExiHS_BLVRB
    ExpressionAtlasiP30043 baseline and differential
    GenevisibleiP30043 HS

    Organism-specific databases

    HPAiHPA041698
    HPA041937

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi107114, 14 interactors
    IntActiP30043, 6 interactors
    STRINGi9606.ENSP00000263368

    Structurei

    Secondary structure

    1206
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 10Combined sources6
    Helixi14 – 25Combined sources12
    Beta strandi29 – 35Combined sources7
    Helixi37 – 39Combined sources3
    Beta strandi42 – 44Combined sources3
    Beta strandi48 – 53Combined sources6
    Helixi58 – 65Combined sources8
    Beta strandi69 – 73Combined sources5
    Helixi86 – 101Combined sources16
    Beta strandi105 – 109Combined sources5
    Helixi112 – 114Combined sources3
    Helixi118 – 120Combined sources3
    Helixi123 – 125Combined sources3
    Helixi126 – 141Combined sources16
    Beta strandi144 – 149Combined sources6
    Beta strandi152 – 155Combined sources4
    Beta strandi164 – 169Combined sources6
    Beta strandi174 – 177Combined sources4
    Helixi178 – 187Combined sources10
    Helixi188 – 190Combined sources3
    Turni193 – 196Combined sources4
    Beta strandi198 – 202Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1HDOX-ray1.15A2-205[»]
    1HE2X-ray1.20A2-205[»]
    1HE3X-ray1.40A2-205[»]
    1HE4X-ray1.40A2-205[»]
    1HE5X-ray1.50A2-205[»]
    5OOGX-ray1.33A1-206[»]
    5OOHX-ray1.20A1-206[»]
    ProteinModelPortaliP30043
    SMRiP30043
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30043

    Family & Domainsi

    Phylogenomic databases

    eggNOGiENOG410IXV9 Eukaryota
    ENOG4111JAS LUCA
    GeneTreeiENSGT00390000014810
    HOGENOMiHOG000262432
    HOVERGENiHBG050695
    InParanoidiP30043
    KOiK05901
    OMAiTEIRPAW
    OrthoDBiEOG091G0PLW
    PhylomeDBiP30043
    TreeFamiTF324063

    Family and domain databases

    InterProiView protein in InterPro
    IPR016040 NAD(P)-bd_dom
    IPR036291 NAD(P)-bd_dom_sf
    PfamiView protein in Pfam
    PF13460 NAD_binding_10, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P30043-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAVKKIAIFG ATGQTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPRPAHV
    60 70 80 90 100
    VVGDVLQAAD VDKTVAGQDA VIVLLGTRND LSPTTVMSEG ARNIVAAMKA
    110 120 130 140 150
    HGVDKVVACT SAFLLWDPTK VPPRLQAVTD DHIRMHKVLR ESGLKYVAVM
    160 170 180 190 200
    PPHIGDQPLT GAYTVTLDGR GPSRVISKHD LGHFMLRCLT TDEYDGHSTY

    PSHQYQ
    Length:206
    Mass (Da):22,119
    Last modified:January 23, 2007 - v3
    Checksum:i3057E6D69A9F9F9F
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti16G → C AA sequence (PubMed:7929092).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_01916846R → Q1 PublicationCorresponds to variant dbSNP:rs11547746Ensembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D26308 mRNA Translation: BAA05370.1
    D32143 mRNA Translation: BAA06874.1
    AK312137 mRNA Translation: BAG35073.1
    AY340485 Genomic DNA Translation: AAP88933.1
    AC010271 Genomic DNA No translation available.
    CH471126 Genomic DNA Translation: EAW56969.1
    BC109371 mRNA Translation: AAI09372.1
    CCDSiCCDS33029.1
    PIRiJC2070
    RefSeqiNP_000704.1, NM_000713.2
    UniGeneiHs.515785

    Genome annotation databases

    EnsembliENST00000263368; ENSP00000263368; ENSG00000090013
    GeneIDi645
    KEGGihsa:645

    Keywords - Coding sequence diversityi

    Polymorphism

    Similar proteinsi

    Entry informationi

    Entry nameiBLVRB_HUMAN
    AccessioniPrimary (citable) accession number: P30043
    Secondary accession number(s): A6NKD8
    , B2R5C6, P32078, P53005, Q32LZ2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: June 20, 2018
    This is version 179 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

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