ID   HMP_BURST               Reviewed;         393 AA.
AC   Q8GAZ4;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-MAR-2009, entry version 35.
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;
OS   Burkholderia sp. (strain TH2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=109791;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=22231657; PubMed=12270830;
RX   DOI=10.1128/JB.184.20.5714-5722.2002;
RA   Suzuki K., Ichimura A., Ogawa N., Hasebe A., Miyashita K.;
RT   "Differential expression of two catechol 1,2-dioxygenases in
RT   Burkholderia sp. strain TH2.";
RL   J. Bacteriol. 184:5714-5722(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; AB035325; BAC16771.1; -; Genomic_DNA.
DR   HSSP; P04252; 4VHB.
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; IPR012292; Globin.
DR   InterPro; IPR000971; Globin_subset.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   InterPro; IPR000951; Ph_dOase_redase_FPNCR.
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; PR00409; PHDIOXRDTASE.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   3: Inferred from homology;
KW   Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD;
KW   NADP; Oxidoreductase; Oxygen transport; Transport.
FT   CHAIN         1    393       Flavohemoprotein.
FT                                /FTId=PRO_0000052428.
FT   DOMAIN      153    256       FAD-binding FR-type.
FT   NP_BIND     205    208       FAD (By similarity).
FT   NP_BIND     268    273       NADP (By similarity).
FT   NP_BIND     385    388       FAD (By similarity).
FT   REGION        1    139       Globin.
FT   REGION      150    393       Reductase.
FT   REGION      260    393       NAD or NADP-binding.
FT   ACT_SITE     95     95       Charge relay system (By similarity).
FT   ACT_SITE    138    138       Charge relay system (By similarity).
FT   METAL        85     85       Iron (heme proximal ligand) (By
FT                                similarity).
FT   BINDING     191    191       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        384    384       Influences the redox potential of the
FT                                prosthetic heme and FAD groups (By
FT                                similarity).
SQ   SEQUENCE   393 AA;  43707 MW;  D17DB36399BB717B CRC64;
     MLSAEHRAIV KATVPLLESG GEALTTHFYK TMLAEYPSVR PLFNQAHQQS GDQPRALANA
     VLMYARHIDQ LEQLGGLVSQ IVNKHVALNI LPEHYPIVGA CLLRAIREVL GAEIATDAVI
     EAWGAAYQQL ADLLIGLEEN VYVEKETATG GWRGTRAFVV ARKVKESDEI TSFYLRPADG
     GELLEFHPGQ YIGLKLIVDG EEIRRNYSLS AAANGREYRI SVKREPNGKA SNYLHDSVNE
     GATLDLLTPS GDFTLEHNDK PLVLISGGVG ITPTLAMLNA ALQTSRPIHF IHATRHGGVH
     AFRDHIDELA ARHPQLKRFY VYEKPRHDDE AHHAEGYIDE ARLIEWLPAT RDVDVYFLGP
     KSFMQAVKRH LKTIGVPEKQ SRYEFFGPAS ALD
//