ID   HMP_OCEIH               Reviewed;         406 AA.
AC   Q8ETH0;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 44.
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=OB0291;
OS   Oceanobacillus iheyensis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=182710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
RX   MEDLINE=22220767; PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya
RT   Ridge and its unexpected adaptive capabilities to extreme
RT   environments.";
RL   Nucleic Acids Res. 30:3927-3935(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   -!- 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.
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DR   EMBL; BA000028; BAC12247.1; -; Genomic_DNA.
DR   RefSeq; NP_691212.1; -.
DR   HSSP; P04252; 1VHB.
DR   GeneID; 1015481; -.
DR   GenomeReviews; BA000028_GR; OB0291.
DR   KEGG; oih:OB0291; -.
DR   NMPDR; fig|221109.1.peg.293; -.
DR   HOGENOM; Q8ETH0; -.
DR   OMA; Q8ETH0; KHRSLGI.
DR   BioCyc; OIHE221109:OB0291-MON; -.
DR   BRENDA; 1.14.12.17; 278212.
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    406       Flavohemoprotein.
FT                                /FTId=PRO_0000052436.
FT   DOMAIN      158    267       FAD-binding FR-type.
FT   NP_BIND     212    215       FAD (By similarity).
FT   NP_BIND     280    285       NADP (By similarity).
FT   NP_BIND     397    400       FAD (By similarity).
FT   REGION        5    144       Globin.
FT   REGION      155    406       Reductase.
FT   REGION      271    406       NAD or NADP-binding.
FT   ACT_SITE    101    101       Charge relay system (By similarity).
FT   ACT_SITE    143    143       Charge relay system (By similarity).
FT   METAL        91     91       Iron (heme proximal ligand) (By
FT                                similarity).
FT   BINDING     196    196       FAD (By similarity).
FT   SITE         35     35       Involved in heme-bound ligand
FT                                stabilization and O-O bond activation (By
FT                                similarity).
FT   SITE         90     90       Influences the redox potential of the
FT                                prosthetic heme and FAD groups (By
FT                                similarity).
FT   SITE        396    396       Influences the redox potential of the
FT                                prosthetic heme and FAD groups (By
FT                                similarity).
SQ   SEQUENCE   406 AA;  45811 MW;  226846AECD9F4276 CRC64;
     MSNTTVLLDK KTTEIIKATV PVLKEHGEAI TKHFYKILLE NNPELKNVFN QTNQRKGAQS
     KALANTVYAA AANIEKLEEI LPHVKQIAHK HVSLNIKPEQ YPIVGKYLLI AIKEVLGDAA
     TDEIIEAWEK AYFVIADIFI SVEKEMYNEK KNQIGGWTGF RDFKVIKKVK ESKEITSFYL
     KPDDNLPITT FIPGQYITIK AQIESEAYVH LRQYSLSTAP GKDYYRISVK REASNQPIGV
     VSNYLHTSVE VGSVLPISAP AGDFILDERD HRPLVLISGG VGLTPIMSML ESVVEHQPNR
     NVVFIHAAKS IDHQAMRKRV SEIAKSKEQV KQYVVYSNPT NRTDGDKQGY IDYEWLKEVI
     PTKDAAFYLC GPKPFMSAIN NDLQNMNIAQ NDIHMELFGP LEPIAK
//