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P24232

- HMP_ECOLI

UniProt

P24232 - HMP_ECOLI

Protein

Flavohemoprotein

Gene

hmp

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    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, HMP 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 HMP might act as an amplifier of superoxide stress. Under anaerobic conditions, HMP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.
    Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if these reactions are of any biological significance in vivo.

    Catalytic activityi

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

    Cofactori

    Binds 1 FAD per subunit.
    Binds 1 heme B group per subunit.

    Kineticsi

    1. KM=0.28 µM for NO1 Publication
    2. KM=90 µM for O21 Publication
    3. KM=1.8 µM for NADH1 Publication
    4. KM=19.6 µM for NADPH1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei29 – 291Involved in heme-bound ligand stabilization and O-O bond activation
    Sitei84 – 841Influences the redox potential of the prosthetic heme and FAD groups
    Metal bindingi85 – 851Iron (heme proximal ligand)
    Active sitei95 – 951Charge relay system1 Publication
    Active sitei135 – 1351Charge relay system1 Publication
    Binding sitei188 – 1881FAD
    Sitei388 – 3881Influences the redox potential of the prosthetic heme and FAD groups

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi204 – 2074FAD
    Nucleotide bindingi268 – 2736NADPBy similarity
    Nucleotide bindingi389 – 3924FAD

    GO - Molecular functioni

    1. FAD binding Source: EcoCyc
    2. fatty acid binding Source: EcoCyc
    3. heme binding Source: EcoCyc
    4. hydroperoxide reductase activity Source: EcoCyc
    5. iron ion binding Source: InterPro
    6. nitric oxide dioxygenase activity Source: EcoCyc
    7. oxygen binding Source: InterPro
    8. oxygen transporter activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. response to nitrosative stress Source: EcoCyc
    2. response to toxic substance Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Detoxification, Oxygen transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein, Heme, Iron, Metal-binding, NAD, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10456-MONOMER.
    ECOL316407:JW2536-MONOMER.
    MetaCyc:EG10456-MONOMER.
    SABIO-RKP24232.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Flavohemoprotein
    Alternative name(s):
    Flavohemoglobin
    HMP
    Hemoglobin-like protein
    Nitric oxide dioxygenase (EC:1.14.12.17)
    Short name:
    NO oxygenase
    Short name:
    NOD
    Gene namesi
    Name:hmp
    Synonyms:fsrB, hmpA
    Ordered Locus Names:b2552, JW2536
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10456. hmp.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Has also been found to localize into the periplasm, but spectral analysis revealed that biochemically active HMP is exclusively found in the cytoplasmic fraction.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291Y → E or H: 15 to 35-fold reduction in NO dioxygenase activity. 1 Publication
    Mutagenesisi29 – 291Y → F: 30-fold reduction in NO dioxygenase activity, and 80-fold increase in the O(2) dissociation rate constant. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 396396FlavohemoproteinPRO_0000052431Add
    BLAST

    Proteomic databases

    PaxDbiP24232.
    PRIDEiP24232.

    Expressioni

    Inductioni

    By nitric oxyde NO (under aerobic conditions), nitrite, nitrate (under anaerobic conditions), nitroso compounds, and paraquat.3 Publications

    Gene expression databases

    GenevestigatoriP24232.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    IntActiP24232. 4 interactions.
    STRINGi511145.b2552.

    Structurei

    Secondary structure

    1
    396
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1815
    Helixi21 – 3515
    Helixi37 – 415
    Helixi52 – 6514
    Helixi66 – 749
    Helixi75 – 8713
    Helixi92 – 11019
    Helixi114 – 14431
    Beta strandi150 – 16213
    Beta strandi164 – 17411
    Beta strandi188 – 1936
    Beta strandi202 – 2076
    Beta strandi217 – 2226
    Helixi228 – 2358
    Beta strandi242 – 2498
    Beta strandi262 – 2676
    Helixi268 – 2714
    Helixi272 – 28312
    Beta strandi290 – 2978
    Turni299 – 3013
    Helixi305 – 3139
    Beta strandi315 – 32612
    Helixi329 – 3346
    Beta strandi338 – 3425
    Helixi345 – 3473
    Beta strandi348 – 3503
    Beta strandi358 – 3636
    Helixi365 – 37713
    Helixi382 – 3843
    Beta strandi385 – 3884
    Beta strandi390 – 3923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GVHX-ray2.19A1-396[»]
    ProteinModelPortaliP24232.
    SMRiP24232. Positions 1-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24232.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini150 – 255106FAD-binding FR-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 138138GlobinAdd
    BLAST
    Regioni147 – 396250ReductaseAdd
    BLAST
    Regioni259 – 396138NAD or NADP-bindingAdd
    BLAST

    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
    Contains 1 FAD-binding FR-type domain.Curated

    Phylogenomic databases

    eggNOGiCOG1018.
    HOGENOMiHOG000238921.
    KOiK05916.
    OMAiDQYQIVG.
    OrthoDBiEOG64V2BB.
    PhylomeDBiP24232.

    Family and domain databases

    Gene3Di1.10.490.10. 1 hit.
    HAMAPiMF_01252. Hmp.
    InterProiIPR017927. Fd_Rdtase_FAD-bd.
    IPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR023950. Hmp.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR001221. Phe_hydroxylase.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00970. FAD_binding_6. 1 hit.
    PF00042. Globin. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PRINTSiPR00410. PHEHYDRXLASE.
    SUPFAMiSSF46458. SSF46458. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS01033. GLOBIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P24232-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN    50
    GDQREALFNA IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGE 100
    HLLATLDEMF SPGQEVLDAW GKAYGVLANV FINREAEIYN ENASKAGGWE 150
    GTRDFRIVAK TPRSALITSF ELEPVDGGAV AEYRPGQYLG VWLKPEGFPH 200
    QEIRQYSLTR KPDGKGYRIA VKREEGGQVS NWLHNHANVG DVVKLVAPAG 250
    DFFMAVADDT PVTLISAGVG QTPMLAMLDT LAKAGHTAQV NWFHAAENGD 300
    VHAFADEVKE LGQSLPRFTA HTWYRQPSEA DRAKGQFDSE GLMDLSKLEG 350
    AFSDPTMQFY LCGPVGFMQF TAKQLVDLGV KQENIHYECF GPHKVL 396
    Length:396
    Mass (Da):43,868
    Last modified:March 1, 1992 - v1
    Checksum:i49961BDE1444BD6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58872 Genomic DNA. Translation: CAA41682.1.
    U00096 Genomic DNA. Translation: AAC75605.1.
    AP009048 Genomic DNA. Translation: BAA16460.1.
    J01620 Genomic DNA. Translation: AAA23911.1.
    PIRiS15992.
    RefSeqiNP_417047.1. NC_000913.3.
    YP_490780.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75605; AAC75605; b2552.
    BAA16460; BAA16460; BAA16460.
    GeneIDi12930206.
    947018.
    KEGGiecj:Y75_p2505.
    eco:b2552.
    PATRICi32120503. VBIEscCol129921_2654.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58872 Genomic DNA. Translation: CAA41682.1 .
    U00096 Genomic DNA. Translation: AAC75605.1 .
    AP009048 Genomic DNA. Translation: BAA16460.1 .
    J01620 Genomic DNA. Translation: AAA23911.1 .
    PIRi S15992.
    RefSeqi NP_417047.1. NC_000913.3.
    YP_490780.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GVH X-ray 2.19 A 1-396 [» ]
    ProteinModelPortali P24232.
    SMRi P24232. Positions 1-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P24232. 4 interactions.
    STRINGi 511145.b2552.

    Proteomic databases

    PaxDbi P24232.
    PRIDEi P24232.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75605 ; AAC75605 ; b2552 .
    BAA16460 ; BAA16460 ; BAA16460 .
    GeneIDi 12930206.
    947018.
    KEGGi ecj:Y75_p2505.
    eco:b2552.
    PATRICi 32120503. VBIEscCol129921_2654.

    Organism-specific databases

    EchoBASEi EB0451.
    EcoGenei EG10456. hmp.

    Phylogenomic databases

    eggNOGi COG1018.
    HOGENOMi HOG000238921.
    KOi K05916.
    OMAi DQYQIVG.
    OrthoDBi EOG64V2BB.
    PhylomeDBi P24232.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10456-MONOMER.
    ECOL316407:JW2536-MONOMER.
    MetaCyc:EG10456-MONOMER.
    SABIO-RK P24232.

    Miscellaneous databases

    EvolutionaryTracei P24232.
    PROi P24232.

    Gene expression databases

    Genevestigatori P24232.

    Family and domain databases

    Gene3Di 1.10.490.10. 1 hit.
    HAMAPi MF_01252. Hmp.
    InterProi IPR017927. Fd_Rdtase_FAD-bd.
    IPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    IPR023950. Hmp.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR001221. Phe_hydroxylase.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF00970. FAD_binding_6. 1 hit.
    PF00042. Globin. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00410. PHEHYDRXLASE.
    SUPFAMi SSF46458. SSF46458. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    PS01033. GLOBIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12."
      Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E., Poole R.K.
      Mol. Gen. Genet. 226:49-58(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20.
      Strain: K12.
    2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Characterization of the Escherichia coli gene for serine hydroxymethyltransferase."
      Plamann M.D., Stauffer G.V.
      Gene 22:9-18(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
    6. "The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases."
      Andrews S.C., Shipley D., Keen J.N., Findlay J.B.C., Harrison P.M., Guest J.R.
      FEBS Lett. 302:247-252(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS A FERRISIDEROPHORE REDUCTASE.
      Strain: K12.
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    8. "Nitric oxide dioxygenase: an enzymic function for flavohemoglobin."
      Gardner P.R., Gardner A.M., Martin L.A., Salzman A.L.
      Proc. Natl. Acad. Sci. U.S.A. 95:10378-10383(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-20, CHARACTERIZATION.
    9. "The oxygenated flavohaemoglobin from Escherichia coli: evidence from photodissociation and rapid-scan studies for two kinetic and spectral forms."
      Orii Y., Ioannidis N., Poole R.K.
      Biochem. Biophys. Res. Commun. 187:94-100(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: RAPID-SCAN AND FLASH PHOTOLYSIS SPECTROSCOPY.
    10. "Ferric reductases in Escherichia coli: the contribution of the haemoglobin-like protein."
      Eschenbrenner M., Coves J., Fontecave M.
      Biochem. Biophys. Res. Commun. 198:127-131(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A FERRIC CITRATE REDUCTASE.
    11. "Distribution of the flavohaemoglobin, HMP, between periplasm and cytoplasm in Escherichia coli."
      Vasudevan S.G., Tang P., Dixon N.E., Poole R.K.
      FEMS Microbiol. Lett. 125:219-224(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo."
      Membrillo-Hernandez J., Ioannidis N., Poole R.K.
      FEBS Lett. 382:141-144(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A NADH OXIDASE, ROLE IN OXIDATIVE STRESS.
    13. "Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12."
      Poole R.K., Anjum M.F., Membrillo-Hernandez J., Kim S.O., Hughes M.N., Stewart V.
      J. Bacteriol. 178:5487-5492(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSCRIPTIONAL REGULATION.
      Strain: K12.
    14. "Reactions of the Escherichia coli flavohaemoglobin (Hmp) with NADH and near-micromolar oxygen: oxygen affinity of NADH oxidase activity."
      Poole R.K., Ioannidis N., Orii Y.
      Microbiology 142:1141-1148(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A AEROBIC NADH OXIDASE AND ANAEROBIC FAD REDUCTASE.
    15. "Paraquat regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12 is SoxRS independent but modulated by sigma S."
      Membrillo-Hernandez J., Kim S.O., Cook G.M., Poole R.K.
      J. Bacteriol. 179:3164-3170(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSCRIPTIONAL REGULATION.
      Strain: K12.
    16. "Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase activity to haem-bound dioxygen."
      Poole R.K., Rogers N.J., D'mello R.A.M., Hughes M.N., Orii Y.
      Microbiology 143:1557-1565(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A CYTOCHROME C REDUCTASE AND FERRISIDEROPHORE REDUCTASE.
    17. "Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged oxidative stress and implications for its physiological role in Escherichia coli."
      Anjum M.F., Ioannidis N., Poole R.K.
      FEMS Microbiol. Lett. 166:219-223(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A NADH AND NADPH OXIDASE.
    18. "Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase."
      Gardner P.R., Costantino G., Salzman A.L.
      J. Biol. Chem. 273:26528-26533(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN NITRIC OXIDE DETOXIFICATION.
    19. "A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region."
      Membrillo-Hernandez J., Coopamah M.D., Channa A., Hughes M.N., Poole R.K.
      Mol. Microbiol. 29:1101-1112(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSCRIPTIONAL REGULATION BY NITRIC OXIDE DONORS.
      Strain: K12.
    20. "Nitrosative stress: metabolic pathway involving the flavohemoglobin."
      Hausladen A., Gow A., Stamler J.S.
      Proc. Natl. Acad. Sci. U.S.A. 95:14100-14105(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A NITRIC OXIDE DIOXYGENASE.
    21. "Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): reversible binding of nitric oxide and reduction to nitrous oxide."
      Kim S.O., Orii Y., Lloyd D., Hughes M.N., Poole R.K.
      FEBS Lett. 445:389-394(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ANAEROBIC NITRIC OXIDE REDUCTASE.
    22. "The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a 'nitric oxide releaser', and paraquat and is essential for transcriptional responses to oxidative stress."
      Membrillo-Hernandez J., Coopamah M.D., Anjum M.F., Stevanin T.M., Kelly A., Hughes M.N., Poole R.K.
      J. Biol. Chem. 274:748-754(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN RESISTANCE TO NITRIC OXIDE AND PARAQUAT.
    23. "Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis."
      Gardner A.M., Martin L.A., Gardner P.R., Dou Y., Olson J.S.
      J. Biol. Chem. 275:12581-12589(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-29.
    24. "Nitric-oxide dioxygenase activity and function of flavohemoglobins. Sensitivity to nitric oxide and carbon monoxide inhibition."
      Gardner P.R., Gardner A.M., Martin L.A., Dou Y., Li T., Olson J.S., Zhu H., Riggs A.F.
      J. Biol. Chem. 275:31581-31587(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    25. "Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo' or bd, from nitric oxide."
      Stevanin T.M., Ioannidis N., Mills C.E., Kim S.O., Hughes M.N., Poole R.K.
      J. Biol. Chem. 275:35868-35875(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN NITRIC OXIDE DETOXIFICATION.
    26. "Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide."
      Mills C.E., Sedelnikova S., Soeballe B., Hughes M.N., Poole R.K.
      Biochem. J. 353:207-213(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    27. "The distal heme pocket of Escherichia coli flavohemoglobin probed by infrared spectroscopy."
      Bonamore A., Chiancone E., Boffi A.
      Biochim. Biophys. Acta 1549:174-178(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INFRARED SPECTROSCOPY.
    28. "Flavohemoglobin, a globin with a peroxidase-like catalytic site."
      Mukai M., Mills C.E., Poole R.K., Yeh S.-R.
      J. Biol. Chem. 276:7272-7277(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, RESONANCE RAMAN SPECTROSCOPY.
    29. "Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen."
      Hausladen A., Gow A., Stamler J.S.
      Proc. Natl. Acad. Sci. U.S.A. 98:10108-10112(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DENITROSYLASE ACTIVITY.
    30. "Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity."
      Gardner A.M., Gardner P.R.
      J. Biol. Chem. 277:8166-8171(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, ROLE IN AEROBIC NITRIC OXIDE DETOXIFICATION.
    31. "Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin."
      Bonamore A., Farina A., Gattoni M., Schinina M.E., Bellelli A., Boffi A.
      Biochemistry 42:5792-5801(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIPIDS.
    32. "Escherichia coli flavohemoglobin is an efficient alkylhydroperoxide reductase."
      Bonamore A., Gentili P., Ilari A., Schinina M.E., Boffi A.
      J. Biol. Chem. 278:22272-22277(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALKYLHYDROPEROXIDE REDUCTASE ACTIVITY.
    33. "Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp."
      Corker H., Poole R.K.
      J. Biol. Chem. 278:31584-31592(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN NITRIC OXIDE FORMATION.
    34. "Flavohemoglobin Hmp, but not its individual domains, confers protection from respiratory inhibition by nitric oxide in Escherichia coli."
      Hernandez-Urzua E., Mills C.E., White G.P., Contreras-Zentella M.L., Escamilla E., Vasudevan S.G., Membrillo-Hernandez J., Poole R.K.
      J. Biol. Chem. 278:34975-34982(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF SEPARATE FUNCTIONAL DOMAINS.
    35. "The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket."
      Ilari A., Bonamore A., Farina A., Johnson K.A., Boffi A.
      J. Biol. Chem. 277:23725-23732(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS).
    36. "New functions for the ancient globin family: bacterial responses to nitric oxide and nitrosative stress."
      Poole R.K., Hughes M.N.
      Mol. Microbiol. 36:775-783(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    37. "Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology."
      Frey A.D., Kallio P.T.
      FEMS Microbiol. Rev. 27:525-545(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiHMP_ECOLI
    AccessioniPrimary (citable) accession number: P24232
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    No protein-heme interactions have been detected at the distal side of the heme molecule.
    HMP is able to bind specifically unsaturated and/or cyclopropanated fatty acids with high affinity.

    Keywords - Technical termi

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

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3