ID HMP_BACSU Reviewed; 399 AA. AC P49852; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 25-NOV-2008, entry version 72. DE RecName: Full=Flavohemoprotein; DE AltName: Full=Hemoglobin-like protein; DE AltName: Full=Flavohemoglobin; DE AltName: Full=Nitric oxide dioxygenase; DE Short=NO oxygenase; DE Short=NOD; DE EC=1.14.12.17; GN Name=hmp; Synonyms=ane3, ykiA; OrderedLocusNames=BSU13040; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPTIONAL REGULATION. RC STRAIN=168; RX MEDLINE=96272254; PubMed=8682784; RA Lacelle M., Kumano M., Kurita K., Yamane K., Zuber P., Nakano M.M.; RT "Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus RT subtilis."; RL J. Bacteriol. 178:3803-3808(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Devine K.M.; RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] RP TRANSCRIPTIONAL REGULATION. RX PubMed=11872732; DOI=10.1128/JB.184.6.1783-1787.2002; RA Nakano M.M.; RT "Induction of ResDE-dependent gene expression in Bacillus subtilis in RT response to nitric oxide and nitrosative stress."; RL J. Bacteriol. 184:1783-1787(2002). CC -!- FUNCTION: Is involved in NO detoxification in an aerobic process, CC termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) CC and NAD(P)H to convert NO to nitrate, which protects the bacterium CC from various noxious nitrogen compounds. Therefore, plays a CC central role in the inducible response to nitrosative stress (By CC similarity). CC -!- CATALYTIC ACTIVITY: 2 NO + 2 O(2) + NAD(P)H = 2 NO(3)(-) + CC NAD(P)(+). CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per CC subunit (By similarity). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- INDUCTION: By nitric oxide, nitrite, and under oxygen-limited CC conditions. CC -!- DOMAIN: Consists of two distinct domains; an N-terminal heme- CC containing oxygen-binding domain and a C-terminal reductase domain CC with binding sites for FAD and NAD(P)H. CC -!- SIMILARITY: Belongs to the globin family. Two-domain CC flavohemoproteins subfamily. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D78189; BAA11258.1; -; Genomic_DNA. DR EMBL; AJ002571; CAA05584.1; -; Genomic_DNA. DR EMBL; Z99110; CAB13161.1; -; Genomic_DNA. DR PIR; B69642; B69642. DR RefSeq; NP_389187.1; -. DR HSSP; P04252; 1VHB. DR GeneID; 939891; -. DR GenomeReviews; AL009126_GR; BSU13040. DR KEGG; bsu:BSU13040; -. DR NMPDR; fig|224308.1.peg.1306; -. DR SubtiList; BG11418; hmp. DR HOGENOM; P49852; -. DR BioCyc; BSUB224308:BSU1306-MON; -. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008941; F:nitric oxide dioxygenase activity; IEA:HAMAP. DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. DR GO; GO:0005344; F:oxygen transporter activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0015671; P:oxygen transport; IEA:HAMAP. DR GO; GO:0009636; P:response to toxin; IEA:UniProtKB-KW. DR HAMAP; MF_01252; -; 1. DR InterPro; IPR001709; FPN_cyt_redctse. DR InterPro; IPR012292; Globin. DR InterPro; IPR013316; Globin_annelid-type. DR InterPro; IPR000971; Globin_subset. DR InterPro; IPR008333; OxRdtase_FAD-bd. DR InterPro; IPR001433; OxRdtase_FAD/NAD_bd. DR InterPro; IPR001221; Phe_hydroxylase. DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00042; Globin; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00371; FPNCR. DR PRINTS; PR00410; PHEHYDRXLASE. DR PRINTS; PR01907; WORMGLOBIN. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS01033; GLOBIN; 1. PE 2: Evidence at transcript level; KW Complete proteome; Detoxification; FAD; Flavoprotein; Heme; Iron; KW Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Transport. FT CHAIN 1 399 Flavohemoprotein. FT /FTId=PRO_0000052424. FT DOMAIN 152 255 FAD-binding FR-type. FT NP_BIND 206 209 FAD (By similarity). FT NP_BIND 268 273 NADP (By similarity). FT NP_BIND 388 391 FAD (By similarity). FT REGION 1 140 Globin. FT REGION 149 399 Reductase. FT REGION 259 399 NAD or NADP-binding. FT ACT_SITE 95 95 Charge relay system (By similarity). FT ACT_SITE 137 137 Charge relay system (By similarity). FT METAL 85 85 Iron (heme proximal ligand) (By FT similarity). FT BINDING 190 190 FAD (By similarity). FT SITE 29 29 Involved in heme-bound ligand FT stabilization and O-O bond activation (By FT similarity). FT SITE 84 84 Influences the redox potential of the FT prosthetic heme and FAD groups (By FT similarity). FT SITE 387 387 Influences the redox potential of the FT prosthetic heme and FAD groups (By FT similarity). SQ SEQUENCE 399 AA; 44729 MW; FFD3DD6C973301CF CRC64; MLDNKTIEII KSTVPVLQQH GETITGRFYD RMFQDHPELL NIFNQTNQKK KTQRTALANA VIAAAANIDQ LGNIIPVVKQ IGHKHRSIGI KPEHYPIVGK YLLIAIKDVL GDAATPDIMQ AWEKAYGVIA DAFIGIEKDM YEQAEEQAGG WKEYKPFVIA KKERESKEIT SFYLKPEDSK PLPEFQAGQY ISIKVRIPDS EYTHIRQYSL SDMPGKDYYR ISVKKDGVVS SYLHDGLQEG DSIEISAPAG DFVLDHASQK DLVLISAGVG ITPMISMLKT SVSKQPERQI LFIHAAKNSE YHALRHEVEE AAKHSAVKTA FVYREPTEED RAGDLHFHEG QIDQQFLKEL IANTDADYYI CGSPSFITAM HKLVSELGSA PESIHYELFG PQLSLAQSV //