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 04-NOV-2026, entry version 214. 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 {ECO:0000269|PubMed:11751864}; GN Name=hmp; Synonyms=fsrB, hmpA; OrderedLocusNames=b2552, JW2536; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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, AND COFACTOR. 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 {ECO:0000269|PubMed:10915782, ECO:0000269|PubMed:10922365, CC ECO:0000269|PubMed:11139382, ECO:0000269|PubMed:11517313, CC ECO:0000269|PubMed:11751864, ECO:0000269|PubMed:12826671, CC ECO:0000269|PubMed:9724711, ECO:0000269|PubMed:9756889, CC ECO:0000269|PubMed:9826660, ECO:0000269|PubMed:9873011}. 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 (PubMed:8612736, PubMed:8704956, CC PubMed:9770277). Under anaerobic conditions, HMP also exhibits nitric CC oxide reductase and FAD reductase activities. However, all these CC reactions are much lower than NOD activity (PubMed:10094495, CC PubMed:8704956). {ECO:0000269|PubMed:10094495, CC ECO:0000269|PubMed:8612736, ECO:0000269|PubMed:8704956, CC ECO:0000269|PubMed:9770277}. 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. {ECO:0000269|PubMed:12663656, ECO:0000269|PubMed:12783887, CC ECO:0000269|PubMed:1601132, ECO:0000269|PubMed:8292013, CC ECO:0000269|PubMed:9168606, ECO:0000269|PubMed:9873011}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 nitric oxide + NADPH + 2 O2 = 2 nitrate + NADP(+) + H(+); 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=2 nitric oxide + NADH + 2 O2 = 2 nitrate + NAD(+) + H(+); 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. {ECO:0000269|PubMed:11964402}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Note=Binds 1 heme b group per subunit. {ECO:0000269|PubMed:11964402}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_CP009789.1. DR PDB; 1GVH; X-ray; 2.19 A; A=1-396. DR AlphaFoldDB; P24232; -. DR MDposit; P24232; -. DR SMR; P24232; -. DR BioGRID; 4259200; 15. DR FunCoup; P24232; 246. DR IntAct; P24232; 4. DR STRING; 511145.b2552; -. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR jPOST; P24232; -. DR PaxDb; 511145-b2552; -. DR EnsemblBacteria; AAC75605; AAC75605; b2552. DR GeneID; 75206245; -. DR GeneID; 947018; -. DR KEGG; ecj:JW2536; -. DR KEGG; eco:b2552; -. DR KEGG; ecoc:C3026_14130; -. 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; AAEQIHY; -. DR OrthoDB; 9801223at2; -. DR PhylomeDB; P24232; -. DR BioCyc; EcoCyc:EG10456-MONOMER; -. DR BioCyc; MetaCyc:EG10456-MONOMER; -. DR BRENDA; 1.14.12.17; 2026. DR SABIO-RK; P24232; -. DR EvolutionaryTrace; P24232; -. DR PRO; PR:P24232; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P24232; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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:0008941; F:nitric oxide dioxygenase [NAD(P)H] 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:0098869; P:cellular oxidant detoxification; IMP:UniProtKB. 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 CDD; cd06184; flavohem_like_fad_nad_binding; 1. DR CDD; cd14776; HmpEc-globin-like; 1. DR FunFam; 1.10.490.10:FF:000003; Flavohemoprotein; 1. DR FunFam; 2.40.30.10:FF:000034; Flavohemoprotein; 1. DR FunFam; 3.40.50.80:FF:000010; Flavohemoprotein; 1. DR Gene3D; 1.10.490.10; Globins; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 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 NCBIfam; NF009805; hmpA; 1. DR PANTHER; PTHR43396; FLAVOHEMOPROTEIN; 1. DR PANTHER; PTHR43396:SF3; FLAVOHEMOPROTEIN; 1. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00042; Globin; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00410; PHEHYDRXLASE. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF46458; Globin-like; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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 Reference proteome. FT CHAIN 1..396 FT /note="Flavohemoprotein" FT /id="PRO_0000052431" FT DOMAIN 1..136 FT /note="Globin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238" FT DOMAIN 150..255 FT /note="FAD-binding FR-type" 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 44 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 46 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 50 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 53 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 84 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" 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 /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 204 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 205 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 206 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 207 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 220 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 222 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 224 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P39662" FT BINDING 225 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 228 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 229 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 230 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 268..273 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 272 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" FT BINDING 393 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:11964402, FT ECO:0007744|PDB:1GVH" 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 68..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..284 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 //