HMP_ECOLI
ID HMP_ECOLI Reviewed; 396 AA.
AC P24232;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Flavohemoprotein;
DE AltName: Full=Flavohemoglobin;
DE AltName: Full=HMP;
DE AltName: Full=Hemoglobin-like protein;
DE AltName: Full=Nitric oxide dioxygenase;
DE Short=NO oxygenase;
DE Short=NOD;
DE EC=1.14.12.17;
GN Name=hmp; Synonyms=fsrB, hmpA; OrderedLocusNames=b2552, JW2536;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX PubMed=2034230; DOI=10.1007/bf00273586;
RA Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E.,
RA Poole R.K.;
RT "Isolation and nucleotide sequence of the hmp gene that encodes a
RT haemoglobin-like protein in Escherichia coli K-12.";
RL Mol. Gen. Genet. 226:49-58(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX PubMed=6190704; DOI=10.1016/0378-1119(83)90059-8;
RA Plamann M.D., Stauffer G.V.;
RT "Characterization of the Escherichia coli gene for serine
RT hydroxymethyltransferase.";
RL Gene 22:9-18(1983).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION AS A FERRISIDEROPHORE REDUCTASE.
RC STRAIN=K12;
RX PubMed=1601132; DOI=10.1016/0014-5793(92)80452-m;
RA Andrews S.C., Shipley D., Keen J.N., Findlay J.B.C., Harrison P.M.,
RA Guest J.R.;
RT "The haemoglobin-like protein (HMP) of Escherichia coli has
RT ferrisiderophore reductase activity and its C-terminal domain shares
RT homology with ferredoxin NADP+ reductases.";
RL FEBS Lett. 302:247-252(1992).
RN [7]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP PROTEIN SEQUENCE OF 1-20, AND CHARACTERIZATION.
RX PubMed=9724711; DOI=10.1073/pnas.95.18.10378;
RA Gardner P.R., Gardner A.M., Martin L.A., Salzman A.L.;
RT "Nitric oxide dioxygenase: an enzymic function for flavohemoglobin.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10378-10383(1998).
RN [9]
RP RAPID-SCAN AND FLASH PHOTOLYSIS SPECTROSCOPY.
RX PubMed=1325799; DOI=10.1016/s0006-291x(05)81463-9;
RA Orii Y., Ioannidis N., Poole R.K.;
RT "The oxygenated flavohaemoglobin from Escherichia coli: evidence from
RT photodissociation and rapid-scan studies for two kinetic and spectral
RT forms.";
RL Biochem. Biophys. Res. Commun. 187:94-100(1992).
RN [10]
RP FUNCTION AS A FERRIC CITRATE REDUCTASE.
RX PubMed=8292013; DOI=10.1006/bbrc.1994.1018;
RA Eschenbrenner M., Coves J., Fontecave M.;
RT "Ferric reductases in Escherichia coli: the contribution of the
RT haemoglobin-like protein.";
RL Biochem. Biophys. Res. Commun. 198:127-131(1994).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=7875569; DOI=10.1111/j.1574-6968.1995.tb07361.x;
RA Vasudevan S.G., Tang P., Dixon N.E., Poole R.K.;
RT "Distribution of the flavohaemoglobin, HMP, between periplasm and cytoplasm
RT in Escherichia coli.";
RL FEMS Microbiol. Lett. 125:219-224(1995).
RN [12]
RP FUNCTION AS A NADH OXIDASE, AND ROLE IN OXIDATIVE STRESS.
RX PubMed=8612736; DOI=10.1016/0014-5793(96)00154-8;
RA Membrillo-Hernandez J., Ioannidis N., Poole R.K.;
RT "The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in
RT vitro and causes oxidative stress in vivo.";
RL FEBS Lett. 382:141-144(1996).
RN [13]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12;
RX PubMed=8808940; DOI=10.1128/jb.178.18.5487-5492.1996;
RA Poole R.K., Anjum M.F., Membrillo-Hernandez J., Kim S.O., Hughes M.N.,
RA Stewart V.;
RT "Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene
RT expression in Escherichia coli K-12.";
RL J. Bacteriol. 178:5487-5492(1996).
RN [14]
RP FUNCTION AS A AEROBIC NADH OXIDASE AND ANAEROBIC FAD REDUCTASE.
RX PubMed=8704956; DOI=10.1099/13500872-142-5-1141;
RA Poole R.K., Ioannidis N., Orii Y.;
RT "Reactions of the Escherichia coli flavohaemoglobin (Hmp) with NADH and
RT near-micromolar oxygen: oxygen affinity of NADH oxidase activity.";
RL Microbiology 142:1141-1148(1996).
RN [15]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12;
RX PubMed=9150210; DOI=10.1128/jb.179.10.3164-3170.1997;
RA Membrillo-Hernandez J., Kim S.O., Cook G.M., Poole R.K.;
RT "Paraquat regulation of hmp (flavohemoglobin) gene expression in
RT Escherichia coli K-12 is SoxRS independent but modulated by sigma S.";
RL J. Bacteriol. 179:3164-3170(1997).
RN [16]
RP FUNCTION AS A CYTOCHROME C REDUCTASE AND FERRISIDEROPHORE REDUCTASE.
RX PubMed=9168606; DOI=10.1099/00221287-143-5-1557;
RA Poole R.K., Rogers N.J., D'mello R.A.M., Hughes M.N., Orii Y.;
RT "Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-
RT hydroxamate K by electron transfer from NADH via FAD: sensitivity of
RT oxidoreductase activity to haem-bound dioxygen.";
RL Microbiology 143:1557-1565(1997).
RN [17]
RP FUNCTION AS A NADH AND NADPH OXIDASE.
RX PubMed=9770277; DOI=10.1111/j.1574-6968.1998.tb13893.x;
RA Anjum M.F., Ioannidis N., Poole R.K.;
RT "Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged
RT oxidative stress and implications for its physiological role in Escherichia
RT coli.";
RL FEMS Microbiol. Lett. 166:219-223(1998).
RN [18]
RP ROLE IN NITRIC OXIDE DETOXIFICATION.
RX PubMed=9756889; DOI=10.1074/jbc.273.41.26528;
RA Gardner P.R., Costantino G., Salzman A.L.;
RT "Constitutive and adaptive detoxification of nitric oxide in Escherichia
RT coli. Role of nitric-oxide dioxygenase in the protection of aconitase.";
RL J. Biol. Chem. 273:26528-26533(1998).
RN [19]
RP TRANSCRIPTIONAL REGULATION BY NITRIC OXIDE DONORS.
RC STRAIN=K12;
RX PubMed=9767577; DOI=10.1046/j.1365-2958.1998.01000.x;
RA Membrillo-Hernandez J., Coopamah M.D., Channa A., Hughes M.N., Poole R.K.;
RT "A novel mechanism for upregulation of the Escherichia coli K-12 hmp
RT (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione:
RT nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp
RT intergenic region.";
RL Mol. Microbiol. 29:1101-1112(1998).
RN [20]
RP FUNCTION AS A NITRIC OXIDE DIOXYGENASE.
RX PubMed=9826660; DOI=10.1073/pnas.95.24.14100;
RA Hausladen A., Gow A., Stamler J.S.;
RT "Nitrosative stress: metabolic pathway involving the flavohemoglobin.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14100-14105(1998).
RN [21]
RP FUNCTION AS AN ANAEROBIC NITRIC OXIDE REDUCTASE.
RX PubMed=10094495; DOI=10.1016/s0014-5793(99)00157-x;
RA Kim S.O., Orii Y., Lloyd D., Hughes M.N., Poole R.K.;
RT "Anoxic function for the Escherichia coli flavohaemoglobin (Hmp):
RT reversible binding of nitric oxide and reduction to nitrous oxide.";
RL FEBS Lett. 445:389-394(1999).
RN [22]
RP ROLE IN RESISTANCE TO NITRIC OXIDE AND PARAQUAT.
RX PubMed=9873011; DOI=10.1074/jbc.274.2.748;
RA Membrillo-Hernandez J., Coopamah M.D., Anjum M.F., Stevanin T.M., Kelly A.,
RA Hughes M.N., Poole R.K.;
RT "The flavohemoglobin of Escherichia coli confers resistance to a
RT nitrosating agent, a 'nitric oxide releaser', and paraquat and is essential
RT for transcriptional responses to oxidative stress.";
RL J. Biol. Chem. 274:748-754(1999).
RN [23]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-29.
RX PubMed=10777548; DOI=10.1074/jbc.275.17.12581;
RA Gardner A.M., Martin L.A., Gardner P.R., Dou Y., Olson J.S.;
RT "Steady-state and transient kinetics of Escherichia coli nitric-oxide
RT dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for
RT dioxygen binding and catalysis.";
RL J. Biol. Chem. 275:12581-12589(2000).
RN [24]
RP CHARACTERIZATION.
RX PubMed=10922365; DOI=10.1074/jbc.m004141200;
RA Gardner P.R., Gardner A.M., Martin L.A., Dou Y., Li T., Olson J.S., Zhu H.,
RA Riggs A.F.;
RT "Nitric-oxide dioxygenase activity and function of flavohemoglobins.
RT Sensitivity to nitric oxide and carbon monoxide inhibition.";
RL J. Biol. Chem. 275:31581-31587(2000).
RN [25]
RP ROLE IN NITRIC OXIDE DETOXIFICATION.
RX PubMed=10915782; DOI=10.1074/jbc.m002471200;
RA Stevanin T.M., Ioannidis N., Mills C.E., Kim S.O., Hughes M.N., Poole R.K.;
RT "Flavohemoglobin Hmp affords inducible protection for Escherichia coli
RT respiration, catalyzed by cytochromes bo' or bd, from nitric oxide.";
RL J. Biol. Chem. 275:35868-35875(2000).
RN [26]
RP CHARACTERIZATION.
RX PubMed=11139382; DOI=10.1042/0264-6021:3530207;
RA Mills C.E., Sedelnikova S., Soeballe B., Hughes M.N., Poole R.K.;
RT "Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and
RT haem contents has a low affinity for dioxygen in the absence or presence of
RT nitric oxide.";
RL Biochem. J. 353:207-213(2001).
RN [27]
RP INFRARED SPECTROSCOPY.
RX PubMed=11690654; DOI=10.1016/s0167-4838(01)00256-4;
RA Bonamore A., Chiancone E., Boffi A.;
RT "The distal heme pocket of Escherichia coli flavohemoglobin probed by
RT infrared spectroscopy.";
RL Biochim. Biophys. Acta 1549:174-178(2001).
RN [28]
RP ACTIVE SITE, AND RESONANCE RAMAN SPECTROSCOPY.
RX PubMed=11092893; DOI=10.1074/jbc.m009280200;
RA Mukai M., Mills C.E., Poole R.K., Yeh S.-R.;
RT "Flavohemoglobin, a globin with a peroxidase-like catalytic site.";
RL J. Biol. Chem. 276:7272-7277(2001).
RN [29]
RP DENITROSYLASE ACTIVITY.
RX PubMed=11517313; DOI=10.1073/pnas.181199698;
RA Hausladen A., Gow A., Stamler J.S.;
RT "Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl
RT equivalent with molecular oxygen.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10108-10112(2001).
RN [30]
RP ENZYME ACTIVITY, AND ROLE IN AEROBIC NITRIC OXIDE DETOXIFICATION.
RX PubMed=11751864; DOI=10.1074/jbc.m110470200;
RA Gardner A.M., Gardner P.R.;
RT "Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic,
RT Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-
RT scavenging activity.";
RL J. Biol. Chem. 277:8166-8171(2002).
RN [31]
RP INTERACTION WITH LIPIDS.
RX PubMed=12741837; DOI=10.1021/bi0206311;
RA Bonamore A., Farina A., Gattoni M., Schinina M.E., Bellelli A., Boffi A.;
RT "Interaction with membrane lipids and heme ligand binding properties of
RT Escherichia coli flavohemoglobin.";
RL Biochemistry 42:5792-5801(2003).
RN [32]
RP ALKYLHYDROPEROXIDE REDUCTASE ACTIVITY.
RX PubMed=12663656; DOI=10.1074/jbc.m301285200;
RA Bonamore A., Gentili P., Ilari A., Schinina M.E., Boffi A.;
RT "Escherichia coli flavohemoglobin is an efficient alkylhydroperoxide
RT reductase.";
RL J. Biol. Chem. 278:22272-22277(2003).
RN [33]
RP ROLE IN NITRIC OXIDE FORMATION.
RX PubMed=12783887; DOI=10.1074/jbc.m303282200;
RA Corker H., Poole R.K.;
RT "Nitric oxide formation by Escherichia coli. Dependence on nitrite
RT reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp.";
RL J. Biol. Chem. 278:31584-31592(2003).
RN [34]
RP CHARACTERIZATION OF SEPARATE FUNCTIONAL DOMAINS.
RX PubMed=12826671; DOI=10.1074/jbc.m303629200;
RA Hernandez-Urzua E., Mills C.E., White G.P., Contreras-Zentella M.L.,
RA Escamilla E., Vasudevan S.G., Membrillo-Hernandez J., Poole R.K.;
RT "Flavohemoglobin Hmp, but not its individual domains, confers protection
RT from respiratory inhibition by nitric oxide in Escherichia coli.";
RL J. Biol. Chem. 278:34975-34982(2003).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS).
RX PubMed=11964402; DOI=10.1074/jbc.m202228200;
RA Ilari A., Bonamore A., Farina A., Johnson K.A., Boffi A.;
RT "The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an
RT unexpected geometry of the distal heme pocket.";
RL J. Biol. Chem. 277:23725-23732(2002).
RN [36]
RP REVIEW.
RX PubMed=10844666; DOI=10.1046/j.1365-2958.2000.01889.x;
RA Poole R.K., Hughes M.N.;
RT "New functions for the ancient globin family: bacterial responses to nitric
RT oxide and nitrosative stress.";
RL Mol. Microbiol. 36:775-783(2000).
RN [37]
RP REVIEW.
RX PubMed=14550944; DOI=10.1016/s0168-6445(03)00056-1;
RA Frey A.D., Kallio P.T.;
RT "Bacterial hemoglobins and flavohemoglobins: versatile proteins and their
RT impact on microbiology and biotechnology.";
RL FEMS Microbiol. Rev. 27:525-545(2003).
CC -!- FUNCTION: Is involved in NO detoxification in an aerobic process,
CC termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and
CC NAD(P)H to convert NO to nitrate, which protects the bacterium from
CC various noxious nitrogen compounds. Therefore, plays a central role in
CC the inducible response to nitrosative stress.
CC -!- FUNCTION: In the presence of oxygen and NADH, HMP has NADH oxidase
CC activity, which leads to the generation of superoxide and H(2)O(2),
CC both in vitro and in vivo, and it has been suggested that HMP might act
CC as an amplifier of superoxide stress. Under anaerobic conditions, HMP
CC also exhibits nitric oxide reductase and FAD reductase activities.
CC However, all these reactions are much lower than NOD activity.
CC -!- FUNCTION: Various electron acceptors are also reduced by HMP in vitro,
CC including dihydropterine, ferrisiderophores, ferric citrate, cytochrome
CC c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it
CC is unknown if these reactions are of any biological significance in
CC vivo.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate;
CC Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.12.17;
CC Evidence={ECO:0000269|PubMed:11751864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate;
CC Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.12.17;
CC Evidence={ECO:0000269|PubMed:11751864};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b group per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 uM for NO {ECO:0000269|PubMed:10777548};
CC KM=90 uM for O(2) {ECO:0000269|PubMed:10777548};
CC KM=1.8 uM for NADH {ECO:0000269|PubMed:10777548};
CC KM=19.6 uM for NADPH {ECO:0000269|PubMed:10777548};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7875569}. Note=Has
CC also been found to localize into the periplasm, but spectral analysis
CC revealed that biochemically active HMP is exclusively found in the
CC cytoplasmic fraction.
CC -!- INDUCTION: By nitric oxyde NO (under aerobic conditions), nitrite,
CC nitrate (under anaerobic conditions), nitroso compounds, and paraquat.
CC {ECO:0000269|PubMed:8808940, ECO:0000269|PubMed:9150210,
CC ECO:0000269|PubMed:9767577}.
CC -!- DOMAIN: Consists of two distinct domains; an N-terminal heme-containing
CC oxygen-binding domain and a C-terminal reductase domain with binding
CC sites for FAD and NAD(P)H.
CC -!- MISCELLANEOUS: No protein-heme interactions have been detected at the
CC distal side of the heme molecule.
CC -!- MISCELLANEOUS: HMP is able to bind specifically unsaturated and/or
CC cyclopropanated fatty acids with high affinity.
CC -!- SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins
CC subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000305}.
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DR EMBL; X58872; CAA41682.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75605.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16460.1; -; Genomic_DNA.
DR EMBL; J01620; AAA23911.1; -; Genomic_DNA.
DR PIR; S15992; S15992.
DR RefSeq; NP_417047.1; NC_000913.3.
DR RefSeq; WP_000883122.1; NZ_STEB01000011.1.
DR PDB; 1GVH; X-ray; 2.19 A; A=1-396.
DR PDBsum; 1GVH; -.
DR AlphaFoldDB; P24232; -.
DR SMR; P24232; -.
DR BioGRID; 4259200; 11.
DR IntAct; P24232; 4.
DR STRING; 511145.b2552; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR jPOST; P24232; -.
DR PaxDb; P24232; -.
DR PRIDE; P24232; -.
DR EnsemblBacteria; AAC75605; AAC75605; b2552.
DR EnsemblBacteria; BAA16460; BAA16460; BAA16460.
DR GeneID; 66673560; -.
DR GeneID; 947018; -.
DR KEGG; ecj:JW2536; -.
DR KEGG; eco:b2552; -.
DR PATRIC; fig|1411691.4.peg.4182; -.
DR EchoBASE; EB0451; -.
DR eggNOG; COG1017; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_12_0_6; -.
DR InParanoid; P24232; -.
DR OMA; ADIHYEV; -.
DR PhylomeDB; P24232; -.
DR BioCyc; EcoCyc:EG10456-MON; -.
DR BioCyc; MetaCyc:EG10456-MON; -.
DR BRENDA; 1.14.12.17; 2026.
DR SABIO-RK; P24232; -.
DR EvolutionaryTrace; P24232; -.
DR PRO; PR:P24232; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR GO; GO:0005504; F:fatty acid binding; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0032843; F:hydroperoxide reductase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008941; F:nitric oxide dioxygenase activity; IDA:EcoCyc.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IBA:GO_Central.
DR GO; GO:0046210; P:nitric oxide catabolic process; IBA:GO_Central.
DR GO; GO:0051409; P:response to nitrosative stress; IMP:EcoCyc.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_01252; Hmp; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR023950; Hmp.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43396:SF3; PTHR43396:SF3; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Detoxification; Direct protein sequencing; FAD;
KW Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase;
KW Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..396
FT /note="Flavohemoprotein"
FT /id="PRO_0000052431"
FT DOMAIN 150..255
FT /note="FAD-binding FR-type"
FT REGION 1..138
FT /note="Globin"
FT REGION 147..396
FT /note="Reductase"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:11092893"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:11092893"
FT BINDING 85
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 204..207
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 268..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 389..392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT SITE 29
FT /note="Involved in heme-bound ligand stabilization and O-O
FT bond activation"
FT SITE 84
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT SITE 388
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT MUTAGEN 29
FT /note="Y->E,H: 15 to 35-fold reduction in NO dioxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:10777548"
FT MUTAGEN 29
FT /note="Y->F: 30-fold reduction in NO dioxygenase activity,
FT and 80-fold increase in the O(2) dissociation rate
FT constant."
FT /evidence="ECO:0000269|PubMed:10777548"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 92..110
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 114..144
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 150..162
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:1GVH"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 315..326
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:1GVH"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:1GVH"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:1GVH"
SQ 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
