[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20. STRAIN=K12; DOI=10.1007/BF00273586; PubMed=2034230 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1093/dnares/4.2.91; PubMed=9205837 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0378-1119(83)90059-8; PubMed=6190704 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1016/0014-5793(92)80452-M; PubMed=1601132 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.95.18.10378; PubMed=9724711 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/S0006-291X(05)81463-9; PubMed=1325799 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1006/bbrc.1994.1018; PubMed=8292013 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0378-1097(94)00501-H; PubMed=7875569 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0014-5793(96)00154-8; PubMed=8612736 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1111/j.1574-6968.1998.tb13893.x; PubMed=9770277 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.273.41.26528; PubMed=9756889 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.95.24.14100; PubMed=9826660 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/S0014-5793(99)00157-X; PubMed=10094495 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.274.2.748; PubMed=9873011 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.275.17.12581; PubMed=10777548 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.M004141200; PubMed=10922365 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.M002471200; PubMed=10915782 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1042/0264-6021:3530207; PubMed=11139382 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/S0167-4838(01)00256-4; PubMed=11690654 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.M009280200; PubMed=11092893 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.181199698; PubMed=11517313 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.M110470200; PubMed=11751864 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1021/bi0206311; PubMed=12741837 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.M301285200; PubMed=12663656 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.M303282200; PubMed=12783887 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.M303629200; PubMed=12826671 [NCBI, ExPASy, EBI, Israel, Japan] 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). DOI=10.1074/jbc.M202228200; PubMed=11964402 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/S0168-6445(03)00056-1; PubMed=14550944 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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 NO + 2 O₂ + NAD(P)H = 2 NO₃^- + NAD(P)⁺.
COFACTOR: Binds 1 FAD per subunit.
COFACTOR: Binds 1 heme B group per subunit.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=0.28 µM for NO;
K_M=90 µM for O₂;
K_M=1.8 µM for NADH;
K_M=19.6 µM for NADPH;
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cytoplasm. 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.
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.
SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X58872; CAA41682.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75605.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16460.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J01620; AAA23911.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15992; S15992.

RefSeq

AP_003138.1; -.
NP_417047.1; -.

3D structure databases

PDB

1GVH; X-ray; 2.19 A; A=1-396.

[ExPASy / RCSB / EBI]

PDBsum

1GVH; -.

ModBase

P24232.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10456-MON; -.
MetaCyc:EG10456-MON; -.

Organism-specific databases

EchoBASE

EB0451; -.

EcoGene

EG10456; hmp.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0008941;	Molecular function: nitric oxide dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0019825;	Molecular function: oxygen binding (inferred from electronic annotation from InterPro).
GO:0005344;	Molecular function: oxygen transporter activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0015671;	Biological process: oxygen transport (inferred from electronic annotation from HAMAP).
GO:0009636;	Biological process: response to toxin (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01252; -; 1.
PBIL [Tree]

InterPro

IPR001709; FPN_cyt_redctse.
IPR012292; Globin.
IPR000971; Globin_subset.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR001221; Phe_hydroxylase.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.490.10; Globin_related; 1.

Pfam

PF00970; FAD_binding_6; 1.
PF00042; Globin; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00371; FPNCR.
PR00410; PHEHYDRXLASE.

PROSITE

PS51384; FAD_FR; 1.
PS01033; GLOBIN; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P24232.

Genome annotation databases

GeneID

947018; -.

GenomeReviews

U00096_GR; b2552.
AP009048_GR; JW2536.

KEGG

ecj:JW2536; -.
eco:b2552; -.

Phylogenomic databases

HOGENOM

P24232; -.

Genome annotation databases

CMR

P24232; b2552.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Cytoplasm; Detoxification; Direct protein sequencing; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 396`	`396`	`Flavohemoprotein.`	`PRO_0000052431`
`DOMAIN`	`150 255`	`106`	`FAD-binding FR-type.`
`NP_BIND`	`204 207`	`4`	`FAD.`
`NP_BIND`	`268 273`	`6`	`NADP (By similarity).`
`NP_BIND`	`389 392`	`4`	`FAD.`
`REGION`	`1 138`	`138`	`Globin.`
`REGION`	`147 396`	`250`	`Reductase.`
`REGION`	`259 396`	`138`	`NAD or NADP-binding.`
`ACT_SITE`	`95 95`		`Charge relay system.`
`ACT_SITE`	`135 135`		`Charge relay system.`
`METAL`	`85 85`		`Iron (heme proximal ligand).`
`BINDING`	`188 188`		`FAD.`
`SITE`	`29 29`	`1`	`Involved in heme-bound ligand stabilization and O-O bond activation.`
`SITE`	`84 84`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups.`
`SITE`	`388 388`	`1`	`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.`
`MUTAGEN`	`29 29`		`Y->F: 30-fold reduction in NO dioxygenase activity, and 80-fold increase in the O(2) dissociation rate constant.`
`HELIX`	`4 18`	`15`
`HELIX`	`21 35`	`15`
`HELIX`	`37 41`	`5`
`HELIX`	`52 65`	`14`
`HELIX`	`66 74`	`9`
`HELIX`	`75 87`	`13`
`HELIX`	`92 110`	`19`
`HELIX`	`114 144`	`31`
`STRAND`	`150 162`	`13`
`STRAND`	`164 174`	`11`
`STRAND`	`188 193`	`6`
`STRAND`	`202 207`	`6`
`STRAND`	`217 222`	`6`
`HELIX`	`228 235`	`8`
`STRAND`	`242 249`	`8`
`STRAND`	`262 267`	`6`
`HELIX`	`268 271`	`4`
`HELIX`	`272 283`	`12`
`STRAND`	`290 297`	`8`
`TURN`	`299 301`	`3`
`HELIX`	`305 313`	`9`
`STRAND`	`315 326`	`12`
`HELIX`	`329 334`	`6`
`STRAND`	`338 342`	`5`
`HELIX`	`345 347`	`3`
`STRAND`	`348 350`	`3`
`STRAND`	`358 363`	`6`
`HELIX`	`365 377`	`13`
`HELIX`	`382 384`	`3`
`STRAND`	`385 388`	`4`
`STRAND`	`390 392`	`3`

Sequence information

Length: 396 AA [This is the length of the unprocessed precursor]

Molecular weight: 43868 Da [This is the MW of the unprocessed precursor]

CRC64: 49961BDE1444BD6B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA 

        70         80         90        100        110        120 
IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGE HLLATLDEMF SPGQEVLDAW 

       130        140        150        160        170        180 
GKAYGVLANV FINREAEIYN ENASKAGGWE GTRDFRIVAK TPRSALITSF ELEPVDGGAV 

       190        200        210        220        230        240 
AEYRPGQYLG VWLKPEGFPH QEIRQYSLTR KPDGKGYRIA VKREEGGQVS NWLHNHANVG 

       250        260        270        280        290        300 
DVVKLVAPAG DFFMAVADDT PVTLISAGVG QTPMLAMLDT LAKAGHTAQV NWFHAAENGD 

       310        320        330        340        350        360 
VHAFADEVKE LGQSLPRFTA HTWYRQPSEA DRAKGQFDSE GLMDLSKLEG AFSDPTMQFY 

       370        380        390 
LCGPVGFMQF TAKQLVDLGV KQENIHYECF GPHKVL

P24232 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools