ID HMP_BACHK Reviewed; 402 AA. AC Q6HLA6; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 16-JUN-2009, entry version 38. 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; OrderedLocusNames=BT9727_1331; OS Bacillus thuringiensis subsp. konkukian. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=180856; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). 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 -!- 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; AE017355; AAT63914.1; -; Genomic_DNA. DR RefSeq; YP_035665.1; -. DR GeneID; 2855081; -. DR GenomeReviews; AE017355_GR; BT9727_1331. DR KEGG; btk:BT9727_1331; -. DR NMPDR; fig|281309.1.peg.1305; -. DR HOGENOM; Q6HLA6; -. DR OMA; Q6HLA6; KHRSLGI. DR BioCyc; BTHU281309:BT9727_1331-MON; -. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme 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; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR012292; Globin. 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 PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS01033; GLOBIN; 1. PE 3: Inferred from homology; KW Complete proteome; Detoxification; FAD; Flavoprotein; Heme; Iron; KW Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Transport. FT CHAIN 1 402 Flavohemoprotein. FT /FTId=PRO_0000052423. FT DOMAIN 150 260 FAD-binding FR-type. FT NP_BIND 204 207 FAD (By similarity). FT NP_BIND 273 278 NADP (By similarity). FT NP_BIND 394 397 FAD (By similarity). FT REGION 1 136 Globin. FT REGION 147 402 Reductase. FT REGION 264 402 NAD or NADP-binding. FT ACT_SITE 95 95 Charge relay system (By similarity). FT ACT_SITE 135 135 Charge relay system (By similarity). FT METAL 85 85 Iron (heme proximal ligand) (By FT similarity). FT BINDING 188 188 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 393 393 Influences the redox potential of the FT prosthetic heme and FAD groups (By FT similarity). SQ SEQUENCE 402 AA; 45041 MW; F76860E408AC3132 CRC64; MLSEKTIEIV KSTVPLLQEK GVEITTRFYE ILFSEHPELL NIFNHTNQKK GRQQQALANA VYAAATYIDN LEAIIPVVKQ IGHKHRSLGI KAEHYPIVGT CLLRAIKEVA GAPDEVLNAW GEAYGVIADA FISIEAEMYE EAAHKEGGWK DFRNFVVVKK VKESDVITSF YLKPEDGGKV SSFIPGQYVT VQINIEGETY THNRQYSLSD APGKEYYRIS VKKEKGVDTP DGKVSNYLHD HVKEGDMLPV SAPAGDFVLN MDSTLPVVLI SGGVGITPMM SMLNTLIEQD SKRNVCFVHA AINSNTHAMK EHVEAVDNEY EQVKAYTCYS APTEKDLEMK NFDKEGFVER EWLQTIIPTT EAEFYFCGPV PFMKHINAVL TDLGVKQEHI HYEFFGPAAS LQ //