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Protein

Flavohemoprotein

Gene

hmp

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O2 and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
In the presence of oxygen and NADH, FHP has NADH oxidase activity, which leads to the generation of superoxide and H2O2, both in vitro and in vivo, and it has been suggested that FHP might act as an amplifier of superoxide stress. Under anaerobic conditions, FHP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.

Miscellaneous

No protein-heme interactions have been detected at the distal side of the heme molecule.
FHP is able to bind phospholipids with high affinity.

Catalytic activityi

2 nitric oxide + 2 O2 + NAD(P)H = 2 nitrate + NAD(P)+ + H+.1 Publication

Cofactori

Protein has several cofactor binding sites:

Kineticsi

  1. KM=0.10 µM for NO
  2. KM=80 µM for O2
  3. KM=70 µM for NADH

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei29Involved in heme-bound ligand stabilization and O-O bond activation1
    Sitei84Influences the redox potential of the prosthetic heme and FAD groups1
    Metal bindingi85Iron (heme proximal ligand)1
    Active sitei95Charge relay system1
    Active sitei137Charge relay system1
    Binding sitei190FAD1
    Sitei394Influences the redox potential of the prosthetic heme and FAD groups1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi206 – 209FAD4
    Nucleotide bindingi275 – 280NADPBy similarity6
    Nucleotide bindingi395 – 398FAD4

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    Biological processDetoxification, Oxygen transport, Transport
    LigandFAD, Flavoprotein, Heme, Iron, Metal-binding, NAD, NADP

    Enzyme and pathway databases

    BRENDAi1.14.12.17 231
    SABIO-RKiP39662

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Flavohemoprotein
    Alternative name(s):
    FHP
    Flavohemoglobin
    Hemoglobin-like protein
    Nitric oxide dioxygenase (EC:1.14.12.17)
    Short name:
    NO oxygenase
    Short name:
    NOD
    Gene namesi
    Name:hmp
    Synonyms:fhp
    Ordered Locus Names:PHG200
    Encoded oniPlasmid megaplasmid pHG10 Publication
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    Proteomesi
    • UP000008210 Componenti: Plasmid megaplasmid pHG1

    Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi60A → Y: Does not affect phospholipid-binding. 1 Publication1
    Mutagenesisi98V → F: Blocks phospholipid-binding. 1 Publication1

    Chemistry databases

    DrugBankiDB03979 1-[Glycerolylphosphonyl]-2-[8-(2-Hexyl-Cyclopropyl)-Octanal-1-Yl]-3-[Hexadecanal-1-Yl]-Glycerol
    DB03147 Flavin adenine dinucleotide

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000524411 – 403FlavohemoproteinAdd BLAST403

    Expressioni

    Inductioni

    Under oxygen-limited conditions.1 Publication

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1403
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi4 – 19Combined sources16
    Helixi21 – 35Combined sources15
    Helixi37 – 41Combined sources5
    Helixi47 – 49Combined sources3
    Helixi50 – 67Combined sources18
    Helixi71 – 88Combined sources18
    Helixi92 – 94Combined sources3
    Helixi95 – 110Combined sources16
    Helixi111 – 113Combined sources3
    Helixi116 – 145Combined sources30
    Beta strandi155 – 164Combined sources10
    Beta strandi166 – 176Combined sources11
    Beta strandi190 – 196Combined sources7
    Turni198 – 200Combined sources3
    Beta strandi201 – 209Combined sources9
    Beta strandi219 – 224Combined sources6
    Beta strandi229 – 231Combined sources3
    Helixi235 – 243Combined sources9
    Beta strandi249 – 252Combined sources4
    Beta strandi269 – 275Combined sources7
    Helixi278 – 288Combined sources11
    Beta strandi290 – 292Combined sources3
    Beta strandi296 – 303Combined sources8
    Beta strandi305 – 307Combined sources3
    Helixi309 – 320Combined sources12
    Beta strandi324 – 332Combined sources9
    Turni339 – 341Combined sources3
    Beta strandi344 – 348Combined sources5
    Helixi351 – 353Combined sources3
    Helixi355 – 358Combined sources4
    Beta strandi364 – 370Combined sources7
    Helixi371 – 383Combined sources13
    Helixi388 – 390Combined sources3
    Beta strandi391 – 393Combined sources3
    Beta strandi396 – 398Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CQXX-ray1.75A/B1-403[»]
    3OZUX-ray2.00A1-403[»]
    3OZVX-ray2.40A/B1-403[»]
    3OZWX-ray2.30A/B1-403[»]
    ProteinModelPortaliP39662
    SMRiP39662
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39662

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini152 – 262FAD-binding FR-typeAdd BLAST111

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 140GlobinAdd BLAST140
    Regioni149 – 403ReductaseAdd BLAST255
    Regioni266 – 403NAD or NADP-bindingAdd BLAST138

    Domaini

    Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.

    Sequence similaritiesi

    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000238921
    KOiK05916
    OMAiFNTAHQA

    Family and domain databases

    Gene3Di1.10.490.10, 1 hit
    HAMAPiMF_01252 Hmp, 1 hit
    InterProiView protein in InterPro
    IPR017927 Fd_Rdtase_FAD-bd
    IPR000971 Globin
    IPR009050 Globin-like_sf
    IPR012292 Globin/Proto
    IPR023950 Hmp
    IPR008333 OxRdtase_FAD-bd_dom
    IPR001433 OxRdtase_FAD/NAD-bd
    IPR001221 Phe_hydroxylase
    IPR017938 Riboflavin_synthase-like_b-brl
    PfamiView protein in Pfam
    PF00970 FAD_binding_6, 1 hit
    PF00042 Globin, 1 hit
    PF00175 NAD_binding_1, 1 hit
    PRINTSiPR00410 PHEHYDRXLASE
    SUPFAMiSSF46458 SSF46458, 1 hit
    SSF63380 SSF63380, 1 hit
    PROSITEiView protein in PROSITE
    PS51384 FAD_FR, 1 hit
    PS01033 GLOBIN, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P39662-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLTQKTKDIV KATAPVLAEH GYDIIKCFYQ RMFEAHPELK NVFNMAHQEQ
    60 70 80 90 100
    GQQQQALARA VYAYAENIED PNSLMAVLKN IANKHASLGV KPEQYPIVGE
    110 120 130 140 150
    HLLAAIKEVL GNAATDDIIS AWAQAYGNLA DVLMGMESEL YERSAEQPGG
    160 170 180 190 200
    WKGWRTFVIR EKRPESDVIT SFILEPADGG PVVNFEPGQY TSVAIDVPAL
    210 220 230 240 250
    GLQQIRQYSL SDMPNGRSYR ISVKREGGGP QPPGYVSNLL HDHVNVGDQV
    260 270 280 290 300
    KLAAPYGSFH IDVDAKTPIV LISGGVGLTP MVSMLKVALQ APPRQVVFVH
    310 320 330 340 350
    GARNSAVHAM RDRLREAAKT YENLDLFVFY DQPLPEDVQG RDYDYPGLVD
    360 370 380 390 400
    VKQIEKSILL PDADYYICGP IPFMRMQHDA LKNLGIHEAR IHYEVFGPDL

    FAE
    Length:403
    Mass (Da):44,782
    Last modified:January 23, 2007 - v2
    Checksum:i2E3ED365087F5EA0
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti218S → T in CAA52381 (PubMed:8125952).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X74334 Genomic DNA Translation: CAA52381.1
    AY305378 Genomic DNA Translation: AAP85952.1
    PIRiA53396
    RefSeqiWP_011154115.1, NC_005241.1

    Genome annotation databases

    EnsemblBacteriaiAAP85952; AAP85952; PHG200
    KEGGireh:PHG200
    PATRICifig|381666.6.peg.150

    Similar proteinsi

    Entry informationi

    Entry nameiHMP_CUPNH
    AccessioniPrimary (citable) accession number: P39662
    Secondary accession number(s): Q7WXD4
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: April 25, 2018
    This is version 146 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health