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Flavohemoprotein (FHP) (Flavohemoglobin) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (EC 1.14.12.17)

 HMP_CUPNH               Reviewed;         403 AA.
P39662; Q7WXD4;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 145.
RecName: Full=Flavohemoprotein;
AltName: Full=FHP;
AltName: Full=Flavohemoglobin;
AltName: Full=Hemoglobin-like protein;
AltName: Full=Nitric oxide dioxygenase;
Short=NO oxygenase;
Short=NOD;
EC=1.14.12.17;
Name=hmp; Synonyms=fhp; OrderedLocusNames=PHG200;
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
(Ralstonia eutropha).
Plasmid megaplasmid pHG1.
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Burkholderiaceae; Cupriavidus.
NCBI_TaxID=381666;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8125952;
Cramm R., Siddiqui R.A., Friedrich B.;
"Primary sequence and evidence for a physiological function of the
flavohemoprotein of Alcaligenes eutrophus.";
J. Biol. Chem. 269:7349-7354(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=12948488; DOI=10.1016/S0022-2836(03)00894-5;
Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B.,
Gottschalk G.;
"Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16
megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and
anaerobiosis.";
J. Mol. Biol. 332:369-383(2003).
[3]
PARTIAL PROTEIN SEQUENCE.
PubMed=1594608; DOI=10.1073/pnas.89.11.5015;
Zhu H., Riggs A.F.;
"Yeast flavohemoglobin is an ancient protein related to globins and a
reductase family.";
Proc. Natl. Acad. Sci. U.S.A. 89:5015-5019(1992).
[4]
COFACTOR, INDUCTION, AND SPECTRAL PROPERTIES.
PubMed=218634; DOI=10.1016/0005-2795(79)90422-7;
Probst I., Wolf G., Schlegel H.G.;
"An oxygen-binding flavohemoprotein from Alcaligenes eutrophus.";
Biochim. Biophys. Acta 576:471-478(1979).
[5]
ENZYME ACTIVITY.
PubMed=10922365; DOI=10.1074/jbc.M004141200;
Gardner P.R., Gardner A.M., Martin L.A., Dou Y., Li T., Olson J.S.,
Zhu H., Riggs A.F.;
"Nitric-oxide dioxygenase activity and function of flavohemoglobins.
Sensitivity to nitric oxide and carbon monoxide inhibition.";
J. Biol. Chem. 275:31581-31587(2000).
[6]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
PubMed=8557026;
Ermler U., Siddiqui R.A., Cramm R., Friedrich B.;
"Crystal structure of the flavohemoglobin from Alcaligenes eutrophus
at 1.75-A resolution.";
EMBO J. 14:6067-6077(1995).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF NATIVE PROTEIN AND MUTANT
V98F, PHOSPHOLIPID BINDING, AND MUTAGENESIS OF ALA-60 AND VAL-98.
PubMed=10336624; DOI=10.1046/j.1432-1327.1999.00381.x;
Ollesch G., Kaunzinger A., Juchelka D., Schubert-Zsilavecz M.,
Ermler U.;
"Phospholipid bound to the flavohemoprotein from Alcaligenes
eutrophus.";
Eur. J. Biochem. 262:396-405(1999).
-!- FUNCTION: Is involved in NO detoxification in an aerobic process,
termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2)
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.
-!- FUNCTION: In the presence of oxygen and NADH, FHP has NADH oxidase
activity, which leads to the generation of superoxide and
H(2)O(2), 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.
-!- CATALYTIC ACTIVITY: 2 nitric oxide + 2 O(2) + NAD(P)H = 2 nitrate
+ NAD(P)(+) + H(+). {ECO:0000269|PubMed:10922365}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:218634};
Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:218634};
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:218634};
Note=Binds 1 heme b group per subunit.
{ECO:0000269|PubMed:218634};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.10 uM for NO;
KM=80 uM for O(2);
KM=70 uM for NADH;
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: Under oxygen-limited conditions.
{ECO:0000269|PubMed:218634}.
-!- DOMAIN: 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.
-!- MISCELLANEOUS: No protein-heme interactions have been detected at
the distal side of the heme molecule.
-!- MISCELLANEOUS: FHP is able to bind phospholipids with high
affinity.
-!- SIMILARITY: Belongs to the globin family. Two-domain
flavohemoproteins subfamily. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
pyridine nucleotide cytochrome reductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X74334; CAA52381.1; -; Genomic_DNA.
EMBL; AY305378; AAP85952.1; -; Genomic_DNA.
PIR; A53396; A53396.
RefSeq; WP_011154115.1; NC_005241.1.
PDB; 1CQX; X-ray; 1.75 A; A/B=1-403.
PDB; 3OZU; X-ray; 2.00 A; A=1-403.
PDB; 3OZV; X-ray; 2.40 A; A/B=1-403.
PDB; 3OZW; X-ray; 2.30 A; A/B=1-403.
PDBsum; 1CQX; -.
PDBsum; 3OZU; -.
PDBsum; 3OZV; -.
PDBsum; 3OZW; -.
ProteinModelPortal; P39662; -.
SMR; P39662; -.
DrugBank; DB03979; 1-[Glycerolylphosphonyl]-2-[8-(2-Hexyl-Cyclopropyl)-Octanal-1-Yl]-3-[Hexadecanal-1-Yl]-Glycerol.
DrugBank; DB03147; Flavin adenine dinucleotide.
EnsemblBacteria; AAP85952; AAP85952; PHG200.
KEGG; reh:PHG200; -.
PATRIC; fig|381666.6.peg.150; -.
HOGENOM; HOG000238921; -.
KO; K05916; -.
OMA; FNTAHQA; -.
BRENDA; 1.14.12.17; 231.
SABIO-RK; P39662; -.
EvolutionaryTrace; P39662; -.
Proteomes; UP000008210; Plasmid megaplasmid pHG1.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008941; F:nitric oxide dioxygenase activity; IDA:CACAO.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
GO; GO:0051409; P:response to nitrosative stress; IEA:InterPro.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
HAMAP; MF_01252; Hmp; 1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like_sf.
InterPro; IPR023950; Hmp.
InterPro; IPR008333; OxRdtase_FAD-bd_dom.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR001221; Phe_hydroxylase.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00970; FAD_binding_6; 1.
Pfam; PF00042; Globin; 1.
Pfam; PF00175; NAD_binding_1; 1.
PRINTS; PR00410; PHEHYDRXLASE.
SUPFAM; SSF46458; SSF46458; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS01033; GLOBIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Detoxification;
Direct protein sequencing; FAD; Flavoprotein; Heme; Iron;
Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Plasmid;
Reference proteome; Transport.
CHAIN 1 403 Flavohemoprotein.
/FTId=PRO_0000052441.
DOMAIN 152 262 FAD-binding FR-type.
NP_BIND 206 209 FAD.
NP_BIND 275 280 NADP. {ECO:0000250}.
NP_BIND 395 398 FAD.
REGION 1 140 Globin.
REGION 149 403 Reductase.
REGION 266 403 NAD or NADP-binding.
ACT_SITE 95 95 Charge relay system.
ACT_SITE 137 137 Charge relay system.
METAL 85 85 Iron (heme proximal ligand).
BINDING 190 190 FAD.
SITE 29 29 Involved in heme-bound ligand
stabilization and O-O bond activation.
SITE 84 84 Influences the redox potential of the
prosthetic heme and FAD groups.
SITE 394 394 Influences the redox potential of the
prosthetic heme and FAD groups.
MUTAGEN 60 60 A->Y: Does not affect phospholipid-
binding. {ECO:0000269|PubMed:10336624}.
MUTAGEN 98 98 V->F: Blocks phospholipid-binding.
{ECO:0000269|PubMed:10336624}.
CONFLICT 218 218 S -> T (in Ref. 1; CAA52381).
{ECO:0000305}.
HELIX 4 19 {ECO:0000244|PDB:1CQX}.
HELIX 21 35 {ECO:0000244|PDB:1CQX}.
HELIX 37 41 {ECO:0000244|PDB:1CQX}.
HELIX 47 49 {ECO:0000244|PDB:3OZW}.
HELIX 50 67 {ECO:0000244|PDB:1CQX}.
HELIX 71 88 {ECO:0000244|PDB:1CQX}.
HELIX 92 94 {ECO:0000244|PDB:1CQX}.
HELIX 95 110 {ECO:0000244|PDB:1CQX}.
HELIX 111 113 {ECO:0000244|PDB:1CQX}.
HELIX 116 145 {ECO:0000244|PDB:1CQX}.
STRAND 155 164 {ECO:0000244|PDB:1CQX}.
STRAND 166 176 {ECO:0000244|PDB:1CQX}.
STRAND 190 196 {ECO:0000244|PDB:1CQX}.
TURN 198 200 {ECO:0000244|PDB:1CQX}.
STRAND 201 209 {ECO:0000244|PDB:1CQX}.
STRAND 219 224 {ECO:0000244|PDB:1CQX}.
STRAND 229 231 {ECO:0000244|PDB:3OZW}.
HELIX 235 243 {ECO:0000244|PDB:1CQX}.
STRAND 249 252 {ECO:0000244|PDB:1CQX}.
STRAND 269 275 {ECO:0000244|PDB:1CQX}.
HELIX 278 288 {ECO:0000244|PDB:1CQX}.
STRAND 290 292 {ECO:0000244|PDB:3OZW}.
STRAND 296 303 {ECO:0000244|PDB:1CQX}.
STRAND 305 307 {ECO:0000244|PDB:1CQX}.
HELIX 309 320 {ECO:0000244|PDB:1CQX}.
STRAND 324 332 {ECO:0000244|PDB:1CQX}.
TURN 339 341 {ECO:0000244|PDB:1CQX}.
STRAND 344 348 {ECO:0000244|PDB:1CQX}.
HELIX 351 353 {ECO:0000244|PDB:1CQX}.
HELIX 355 358 {ECO:0000244|PDB:1CQX}.
STRAND 364 370 {ECO:0000244|PDB:1CQX}.
HELIX 371 383 {ECO:0000244|PDB:1CQX}.
HELIX 388 390 {ECO:0000244|PDB:1CQX}.
STRAND 391 393 {ECO:0000244|PDB:1CQX}.
STRAND 396 398 {ECO:0000244|PDB:3OZV}.
SEQUENCE 403 AA; 44782 MW; 2E3ED365087F5EA0 CRC64;
MLTQKTKDIV KATAPVLAEH GYDIIKCFYQ RMFEAHPELK NVFNMAHQEQ GQQQQALARA
VYAYAENIED PNSLMAVLKN IANKHASLGV KPEQYPIVGE HLLAAIKEVL GNAATDDIIS
AWAQAYGNLA DVLMGMESEL YERSAEQPGG WKGWRTFVIR EKRPESDVIT SFILEPADGG
PVVNFEPGQY TSVAIDVPAL GLQQIRQYSL SDMPNGRSYR ISVKREGGGP QPPGYVSNLL
HDHVNVGDQV KLAAPYGSFH IDVDAKTPIV LISGGVGLTP MVSMLKVALQ APPRQVVFVH
GARNSAVHAM RDRLREAAKT YENLDLFVFY DQPLPEDVQG RDYDYPGLVD VKQIEKSILL
PDADYYICGP IPFMRMQHDA LKNLGIHEAR IHYEVFGPDL FAE


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