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P24232

- HMP_ECOLI

UniProt

P24232 - HMP_ECOLI

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Protein

Flavohemoprotein

Gene

hmp

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- 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, 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

Protein has several cofactor binding sites:
  • FADNote: Binds 1 FAD per subunit.
  • heme bNote: 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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 1815Combined sources
Helixi21 – 3515Combined sources
Helixi37 – 415Combined sources
Helixi52 – 6514Combined sources
Helixi66 – 749Combined sources
Helixi75 – 8713Combined sources
Helixi92 – 11019Combined sources
Helixi114 – 14431Combined sources
Beta strandi150 – 16213Combined sources
Beta strandi164 – 17411Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi202 – 2076Combined sources
Beta strandi217 – 2226Combined sources
Helixi228 – 2358Combined sources
Beta strandi242 – 2498Combined sources
Beta strandi262 – 2676Combined sources
Helixi268 – 2714Combined sources
Helixi272 – 28312Combined sources
Beta strandi290 – 2978Combined sources
Turni299 – 3013Combined sources
Helixi305 – 3139Combined sources
Beta strandi315 – 32612Combined sources
Helixi329 – 3346Combined sources
Beta strandi338 – 3425Combined sources
Helixi345 – 3473Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi358 – 3636Combined sources
Helixi365 – 37713Combined sources
Helixi382 – 3843Combined sources
Beta strandi385 – 3884Combined sources
Beta strandi390 – 3923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP24232.
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

        10         20         30         40         50
MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN
60 70 80 90 100
GDQREALFNA IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGE
110 120 130 140 150
HLLATLDEMF SPGQEVLDAW GKAYGVLANV FINREAEIYN ENASKAGGWE
160 170 180 190 200
GTRDFRIVAK TPRSALITSF ELEPVDGGAV AEYRPGQYLG VWLKPEGFPH
210 220 230 240 250
QEIRQYSLTR KPDGKGYRIA VKREEGGQVS NWLHNHANVG DVVKLVAPAG
260 270 280 290 300
DFFMAVADDT PVTLISAGVG QTPMLAMLDT LAKAGHTAQV NWFHAAENGD
310 320 330 340 350
VHAFADEVKE LGQSLPRFTA HTWYRQPSEA DRAKGQFDSE GLMDLSKLEG
360 370 380 390
AFSDPTMQFY LCGPVGFMQF TAKQLVDLGV KQENIHYECF GPHKVL
Length:396
Mass (Da):43,868
Last modified:March 1, 1992 - v1
Checksum:i49961BDE1444BD6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

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.
InParanoidi P24232.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 149 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