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

 HMP_ECOLI               Reviewed;         396 AA.
P24232;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
30-AUG-2017, entry version 167.
RecName: Full=Flavohemoprotein;
AltName: Full=Flavohemoglobin;
AltName: Full=HMP;
AltName: Full=Hemoglobin-like protein;
AltName: Full=Nitric oxide dioxygenase;
Short=NO oxygenase;
Short=NOD;
EC=1.14.12.17;
Name=hmp; Synonyms=fsrB, hmpA; OrderedLocusNames=b2552, JW2536;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
STRAIN=K12;
PubMed=2034230; DOI=10.1007/BF00273586;
Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E.,
Poole R.K.;
"Isolation and nucleotide sequence of the hmp gene that encodes a
haemoglobin-like protein in Escherichia coli K-12.";
Mol. Gen. Genet. 226:49-58(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
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.;
"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.";
DNA Res. 4:91-113(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
PubMed=6190704; DOI=10.1016/0378-1119(83)90059-8;
Plamann M.D., Stauffer G.V.;
"Characterization of the Escherichia coli gene for serine
hydroxymethyltransferase.";
Gene 22:9-18(1983).
[6]
PARTIAL PROTEIN SEQUENCE, AND FUNCTION AS A FERRISIDEROPHORE
REDUCTASE.
STRAIN=K12;
PubMed=1601132; DOI=10.1016/0014-5793(92)80452-M;
Andrews S.C., Shipley D., Keen J.N., Findlay J.B.C., Harrison P.M.,
Guest J.R.;
"The haemoglobin-like protein (HMP) of Escherichia coli has
ferrisiderophore reductase activity and its C-terminal domain shares
homology with ferredoxin NADP+ reductases.";
FEBS Lett. 302:247-252(1992).
[7]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
PROTEIN SEQUENCE OF 1-20, AND CHARACTERIZATION.
PubMed=9724711; DOI=10.1073/pnas.95.18.10378;
Gardner P.R., Gardner A.M., Martin L.A., Salzman A.L.;
"Nitric oxide dioxygenase: an enzymic function for flavohemoglobin.";
Proc. Natl. Acad. Sci. U.S.A. 95:10378-10383(1998).
[9]
RAPID-SCAN AND FLASH PHOTOLYSIS SPECTROSCOPY.
PubMed=1325799; DOI=10.1016/S0006-291X(05)81463-9;
Orii Y., Ioannidis N., Poole R.K.;
"The oxygenated flavohaemoglobin from Escherichia coli: evidence from
photodissociation and rapid-scan studies for two kinetic and spectral
forms.";
Biochem. Biophys. Res. Commun. 187:94-100(1992).
[10]
FUNCTION AS A FERRIC CITRATE REDUCTASE.
PubMed=8292013; DOI=10.1006/bbrc.1994.1018;
Eschenbrenner M., Coves J., Fontecave M.;
"Ferric reductases in Escherichia coli: the contribution of the
haemoglobin-like protein.";
Biochem. Biophys. Res. Commun. 198:127-131(1994).
[11]
SUBCELLULAR LOCATION.
PubMed=7875569; DOI=10.1111/j.1574-6968.1995.tb07361.x;
Vasudevan S.G., Tang P., Dixon N.E., Poole R.K.;
"Distribution of the flavohaemoglobin, HMP, between periplasm and
cytoplasm in Escherichia coli.";
FEMS Microbiol. Lett. 125:219-224(1995).
[12]
FUNCTION AS A NADH OXIDASE, AND ROLE IN OXIDATIVE STRESS.
PubMed=8612736; DOI=10.1016/0014-5793(96)00154-8;
Membrillo-Hernandez J., Ioannidis N., Poole R.K.;
"The flavohaemoglobin (HMP) of Escherichia coli generates superoxide
in vitro and causes oxidative stress in vivo.";
FEBS Lett. 382:141-144(1996).
[13]
TRANSCRIPTIONAL REGULATION.
STRAIN=K12;
PubMed=8808940; DOI=10.1128/jb.178.18.5487-5492.1996;
Poole R.K., Anjum M.F., Membrillo-Hernandez J., Kim S.O., Hughes M.N.,
Stewart V.;
"Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin)
gene expression in Escherichia coli K-12.";
J. Bacteriol. 178:5487-5492(1996).
[14]
FUNCTION AS A AEROBIC NADH OXIDASE AND ANAEROBIC FAD REDUCTASE.
PubMed=8704956; DOI=10.1099/13500872-142-5-1141;
Poole R.K., Ioannidis N., Orii Y.;
"Reactions of the Escherichia coli flavohaemoglobin (Hmp) with NADH
and near-micromolar oxygen: oxygen affinity of NADH oxidase
activity.";
Microbiology 142:1141-1148(1996).
[15]
TRANSCRIPTIONAL REGULATION.
STRAIN=K12;
PubMed=9150210; DOI=10.1128/jb.179.10.3164-3170.1997;
Membrillo-Hernandez J., Kim S.O., Cook G.M., Poole R.K.;
"Paraquat regulation of hmp (flavohemoglobin) gene expression in
Escherichia coli K-12 is SoxRS independent but modulated by sigma S.";
J. Bacteriol. 179:3164-3170(1997).
[16]
FUNCTION AS A CYTOCHROME C REDUCTASE AND FERRISIDEROPHORE REDUCTASE.
PubMed=9168606; DOI=10.1099/00221287-143-5-1557;
Poole R.K., Rogers N.J., D'mello R.A.M., Hughes M.N., Orii Y.;
"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.";
Microbiology 143:1557-1565(1997).
[17]
FUNCTION AS A NADH AND NADPH OXIDASE.
PubMed=9770277; DOI=10.1111/j.1574-6968.1998.tb13893.x;
Anjum M.F., Ioannidis N., Poole R.K.;
"Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged
oxidative stress and implications for its physiological role in
Escherichia coli.";
FEMS Microbiol. Lett. 166:219-223(1998).
[18]
ROLE IN NITRIC OXIDE DETOXIFICATION.
PubMed=9756889; DOI=10.1074/jbc.273.41.26528;
Gardner P.R., Costantino G., Salzman A.L.;
"Constitutive and adaptive detoxification of nitric oxide in
Escherichia coli. Role of nitric-oxide dioxygenase in the protection
of aconitase.";
J. Biol. Chem. 273:26528-26533(1998).
[19]
TRANSCRIPTIONAL REGULATION BY NITRIC OXIDE DONORS.
STRAIN=K12;
PubMed=9767577; DOI=10.1046/j.1365-2958.1998.01000.x;
Membrillo-Hernandez J., Coopamah M.D., Channa A., Hughes M.N.,
Poole R.K.;
"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.";
Mol. Microbiol. 29:1101-1112(1998).
[20]
FUNCTION AS A NITRIC OXIDE DIOXYGENASE.
PubMed=9826660; DOI=10.1073/pnas.95.24.14100;
Hausladen A., Gow A., Stamler J.S.;
"Nitrosative stress: metabolic pathway involving the
flavohemoglobin.";
Proc. Natl. Acad. Sci. U.S.A. 95:14100-14105(1998).
[21]
FUNCTION AS AN ANAEROBIC NITRIC OXIDE REDUCTASE.
PubMed=10094495; DOI=10.1016/S0014-5793(99)00157-X;
Kim S.O., Orii Y., Lloyd D., Hughes M.N., Poole R.K.;
"Anoxic function for the Escherichia coli flavohaemoglobin (Hmp):
reversible binding of nitric oxide and reduction to nitrous oxide.";
FEBS Lett. 445:389-394(1999).
[22]
ROLE IN RESISTANCE TO NITRIC OXIDE AND PARAQUAT.
PubMed=9873011; DOI=10.1074/jbc.274.2.748;
Membrillo-Hernandez J., Coopamah M.D., Anjum M.F., Stevanin T.M.,
Kelly A., Hughes M.N., Poole R.K.;
"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.";
J. Biol. Chem. 274:748-754(1999).
[23]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-29.
PubMed=10777548; DOI=10.1074/jbc.275.17.12581;
Gardner A.M., Martin L.A., Gardner P.R., Dou Y., Olson J.S.;
"Steady-state and transient kinetics of Escherichia coli nitric-oxide
dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential
for dioxygen binding and catalysis.";
J. Biol. Chem. 275:12581-12589(2000).
[24]
CHARACTERIZATION.
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).
[25]
ROLE IN NITRIC OXIDE DETOXIFICATION.
PubMed=10915782; DOI=10.1074/jbc.M002471200;
Stevanin T.M., Ioannidis N., Mills C.E., Kim S.O., Hughes M.N.,
Poole R.K.;
"Flavohemoglobin Hmp affords inducible protection for Escherichia coli
respiration, catalyzed by cytochromes bo' or bd, from nitric oxide.";
J. Biol. Chem. 275:35868-35875(2000).
[26]
CHARACTERIZATION.
PubMed=11139382; DOI=10.1042/0264-6021:3530207;
Mills C.E., Sedelnikova S., Soeballe B., Hughes M.N., Poole R.K.;
"Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD
and haem contents has a low affinity for dioxygen in the absence or
presence of nitric oxide.";
Biochem. J. 353:207-213(2001).
[27]
INFRARED SPECTROSCOPY.
PubMed=11690654; DOI=10.1016/S0167-4838(01)00256-4;
Bonamore A., Chiancone E., Boffi A.;
"The distal heme pocket of Escherichia coli flavohemoglobin probed by
infrared spectroscopy.";
Biochim. Biophys. Acta 1549:174-178(2001).
[28]
ACTIVE SITE, AND RESONANCE RAMAN SPECTROSCOPY.
PubMed=11092893; DOI=10.1074/jbc.M009280200;
Mukai M., Mills C.E., Poole R.K., Yeh S.-R.;
"Flavohemoglobin, a globin with a peroxidase-like catalytic site.";
J. Biol. Chem. 276:7272-7277(2001).
[29]
DENITROSYLASE ACTIVITY.
PubMed=11517313; DOI=10.1073/pnas.181199698;
Hausladen A., Gow A., Stamler J.S.;
"Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl
equivalent with molecular oxygen.";
Proc. Natl. Acad. Sci. U.S.A. 98:10108-10112(2001).
[30]
ENZYME ACTIVITY, AND ROLE IN AEROBIC NITRIC OXIDE DETOXIFICATION.
PubMed=11751864; DOI=10.1074/jbc.M110470200;
Gardner A.M., Gardner P.R.;
"Flavohemoglobin detoxifies nitric oxide in aerobic, but not
anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic
nitric oxide-scavenging activity.";
J. Biol. Chem. 277:8166-8171(2002).
[31]
INTERACTION WITH LIPIDS.
PubMed=12741837; DOI=10.1021/bi0206311;
Bonamore A., Farina A., Gattoni M., Schinina M.E., Bellelli A.,
Boffi A.;
"Interaction with membrane lipids and heme ligand binding properties
of Escherichia coli flavohemoglobin.";
Biochemistry 42:5792-5801(2003).
[32]
ALKYLHYDROPEROXIDE REDUCTASE ACTIVITY.
PubMed=12663656; DOI=10.1074/jbc.M301285200;
Bonamore A., Gentili P., Ilari A., Schinina M.E., Boffi A.;
"Escherichia coli flavohemoglobin is an efficient alkylhydroperoxide
reductase.";
J. Biol. Chem. 278:22272-22277(2003).
[33]
ROLE IN NITRIC OXIDE FORMATION.
PubMed=12783887; DOI=10.1074/jbc.M303282200;
Corker H., Poole R.K.;
"Nitric oxide formation by Escherichia coli. Dependence on nitrite
reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp.";
J. Biol. Chem. 278:31584-31592(2003).
[34]
CHARACTERIZATION OF SEPARATE FUNCTIONAL DOMAINS.
PubMed=12826671; DOI=10.1074/jbc.M303629200;
Hernandez-Urzua E., Mills C.E., White G.P., Contreras-Zentella M.L.,
Escamilla E., Vasudevan S.G., Membrillo-Hernandez J., Poole R.K.;
"Flavohemoglobin Hmp, but not its individual domains, confers
protection from respiratory inhibition by nitric oxide in Escherichia
coli.";
J. Biol. Chem. 278:34975-34982(2003).
[35]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS).
PubMed=11964402; DOI=10.1074/jbc.M202228200;
Ilari A., Bonamore A., Farina A., Johnson K.A., Boffi A.;
"The X-ray structure of ferric Escherichia coli flavohemoglobin
reveals an unexpected geometry of the distal heme pocket.";
J. Biol. Chem. 277:23725-23732(2002).
[36]
REVIEW.
PubMed=10844666; DOI=10.1046/j.1365-2958.2000.01889.x;
Poole R.K., Hughes M.N.;
"New functions for the ancient globin family: bacterial responses to
nitric oxide and nitrosative stress.";
Mol. Microbiol. 36:775-783(2000).
[37]
REVIEW.
PubMed=14550944; DOI=10.1016/S0168-6445(03)00056-1;
Frey A.D., Kallio P.T.;
"Bacterial hemoglobins and flavohemoglobins: versatile proteins and
their impact on microbiology and biotechnology.";
FEMS Microbiol. Rev. 27:525-545(2003).
-!- 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, HMP 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 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.
-!- FUNCTION: 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 ACTIVITY: 2 nitric oxide + 2 O(2) + NAD(P)H = 2 nitrate
+ NAD(P)(+) + H(+). {ECO:0000269|PubMed:11751864}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b group per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.28 uM for NO {ECO:0000269|PubMed:10777548};
KM=90 uM for O(2) {ECO:0000269|PubMed:10777548};
KM=1.8 uM for NADH {ECO:0000269|PubMed:10777548};
KM=19.6 uM for NADPH {ECO:0000269|PubMed:10777548};
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7875569}.
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.
-!- INDUCTION: By nitric oxyde NO (under aerobic conditions), nitrite,
nitrate (under anaerobic conditions), nitroso compounds, and
paraquat. {ECO:0000269|PubMed:8808940, ECO:0000269|PubMed:9150210,
ECO:0000269|PubMed:9767577}.
-!- 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: HMP is able to bind specifically unsaturated and/or
cyclopropanated fatty acids 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; X58872; CAA41682.1; -; Genomic_DNA.
EMBL; U00096; AAC75605.1; -; Genomic_DNA.
EMBL; AP009048; BAA16460.1; -; Genomic_DNA.
EMBL; J01620; AAA23911.1; -; Genomic_DNA.
PIR; S15992; S15992.
RefSeq; NP_417047.1; NC_000913.3.
RefSeq; WP_000883122.1; NZ_LN832404.1.
PDB; 1GVH; X-ray; 2.19 A; A=1-396.
PDBsum; 1GVH; -.
ProteinModelPortal; P24232; -.
SMR; P24232; -.
BioGrid; 4259200; 11.
IntAct; P24232; 4.
STRING; 316385.ECDH10B_2719; -.
DrugBank; DB03147; Flavin adenine dinucleotide.
PaxDb; P24232; -.
PRIDE; P24232; -.
EnsemblBacteria; AAC75605; AAC75605; b2552.
EnsemblBacteria; BAA16460; BAA16460; BAA16460.
GeneID; 947018; -.
KEGG; ecj:JW2536; -.
KEGG; eco:b2552; -.
PATRIC; fig|1411691.4.peg.4182; -.
EchoBASE; EB0451; -.
EcoGene; EG10456; hmp.
eggNOG; ENOG4105CJJ; Bacteria.
eggNOG; COG1017; LUCA.
eggNOG; COG1018; LUCA.
HOGENOM; HOG000238921; -.
InParanoid; P24232; -.
KO; K05916; -.
PhylomeDB; P24232; -.
BioCyc; EcoCyc:EG10456-MONOMER; -.
BioCyc; MetaCyc:EG10456-MONOMER; -.
BRENDA; 1.14.12.17; 2026.
SABIO-RK; P24232; -.
EvolutionaryTrace; P24232; -.
PRO; PR:P24232; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
GO; GO:0005504; F:fatty acid binding; IDA:EcoCyc.
GO; GO:0020037; F:heme binding; IDA:EcoCyc.
GO; GO:0032843; F:hydroperoxide reductase activity; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008941; F:nitric oxide dioxygenase activity; IDA:EcoCyc.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
GO; GO:0071500; P:cellular response to nitrosative stress; IBA:GO_Central.
GO; GO:0046210; P:nitric oxide catabolic process; IBA:GO_Central.
GO; GO:0051409; P:response to nitrosative stress; IMP:EcoCyc.
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.
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;
Reference proteome; Transport.
CHAIN 1 396 Flavohemoprotein.
/FTId=PRO_0000052431.
DOMAIN 150 255 FAD-binding FR-type.
NP_BIND 204 207 FAD.
NP_BIND 268 273 NADP. {ECO:0000250}.
NP_BIND 389 392 FAD.
REGION 1 138 Globin.
REGION 147 396 Reductase.
REGION 259 396 NAD or NADP-binding.
ACT_SITE 95 95 Charge relay system.
{ECO:0000269|PubMed:11092893}.
ACT_SITE 135 135 Charge relay system.
{ECO:0000269|PubMed:11092893}.
METAL 85 85 Iron (heme proximal ligand).
BINDING 188 188 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 388 388 Influences the redox potential of the
prosthetic heme and FAD groups.
MUTAGEN 29 29 Y->E,H: 15 to 35-fold reduction in NO
dioxygenase activity.
{ECO:0000269|PubMed:10777548}.
MUTAGEN 29 29 Y->F: 30-fold reduction in NO dioxygenase
activity, and 80-fold increase in the
O(2) dissociation rate constant.
{ECO:0000269|PubMed:10777548}.
HELIX 4 18 {ECO:0000244|PDB:1GVH}.
HELIX 21 35 {ECO:0000244|PDB:1GVH}.
HELIX 37 41 {ECO:0000244|PDB:1GVH}.
HELIX 52 65 {ECO:0000244|PDB:1GVH}.
HELIX 66 74 {ECO:0000244|PDB:1GVH}.
HELIX 75 87 {ECO:0000244|PDB:1GVH}.
HELIX 92 110 {ECO:0000244|PDB:1GVH}.
HELIX 114 144 {ECO:0000244|PDB:1GVH}.
STRAND 150 162 {ECO:0000244|PDB:1GVH}.
STRAND 164 174 {ECO:0000244|PDB:1GVH}.
STRAND 188 193 {ECO:0000244|PDB:1GVH}.
STRAND 202 207 {ECO:0000244|PDB:1GVH}.
STRAND 217 222 {ECO:0000244|PDB:1GVH}.
HELIX 228 235 {ECO:0000244|PDB:1GVH}.
STRAND 242 249 {ECO:0000244|PDB:1GVH}.
STRAND 262 267 {ECO:0000244|PDB:1GVH}.
HELIX 268 271 {ECO:0000244|PDB:1GVH}.
HELIX 272 283 {ECO:0000244|PDB:1GVH}.
STRAND 290 297 {ECO:0000244|PDB:1GVH}.
TURN 299 301 {ECO:0000244|PDB:1GVH}.
HELIX 305 313 {ECO:0000244|PDB:1GVH}.
STRAND 315 326 {ECO:0000244|PDB:1GVH}.
HELIX 329 334 {ECO:0000244|PDB:1GVH}.
STRAND 338 342 {ECO:0000244|PDB:1GVH}.
HELIX 345 347 {ECO:0000244|PDB:1GVH}.
STRAND 348 350 {ECO:0000244|PDB:1GVH}.
STRAND 358 363 {ECO:0000244|PDB:1GVH}.
HELIX 365 377 {ECO:0000244|PDB:1GVH}.
HELIX 382 384 {ECO:0000244|PDB:1GVH}.
STRAND 385 388 {ECO:0000244|PDB:1GVH}.
STRAND 390 392 {ECO:0000244|PDB:1GVH}.
SEQUENCE 396 AA; 43868 MW; 49961BDE1444BD6B CRC64;
MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA
IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGE HLLATLDEMF SPGQEVLDAW
GKAYGVLANV FINREAEIYN ENASKAGGWE GTRDFRIVAK TPRSALITSF ELEPVDGGAV
AEYRPGQYLG VWLKPEGFPH QEIRQYSLTR KPDGKGYRIA VKREEGGQVS NWLHNHANVG
DVVKLVAPAG DFFMAVADDT PVTLISAGVG QTPMLAMLDT LAKAGHTAQV NWFHAAENGD
VHAFADEVKE LGQSLPRFTA HTWYRQPSEA DRAKGQFDSE GLMDLSKLEG AFSDPTMQFY
LCGPVGFMQF TAKQLVDLGV KQENIHYECF GPHKVL


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