ID   FHBA_DICDI              Reviewed;         397 AA.
AC   Q9UAG7; Q54D74;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   23-SEP-2008, entry version 51.
DE   RecName: Full=Flavohemoprotein A;
DE            EC=1.14.12.17;
DE   AltName: Full=Flavohemoglobin A;
DE   AltName: Full=DdFHa;
DE   AltName: Full=Hemoglobin-like protein A;
DE   AltName: Full=Nitric oxide dioxygenase A;
DE            Short=NO oxygenase A;
DE            Short=NOD A;
GN   Name=fhbA; ORFNames=DDB_0191099;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RC   STRAIN=AX3-1;
RX   PubMed=10791894; DOI=10.1247/csf.25.47;
RA   Iijima M., Shimizu H., Tanaka Y., Urushihara H.;
RT   "Identification and characterization of two flavohemoglobin genes in
RT   Dictyostelium discoideum.";
RL   Cell Struct. Funct. 25:47-55(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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 cell from
CC       various noxious nitrogen compounds. Therefore, plays a central
CC       role in the inducible response to nitrosative stress.
CC   -!- FUNCTION: In the presence of oxygen and NADH, it has NADH oxidase
CC       activity, which leads to the generation of superoxide and
CC       H(2)O(2). Under anaerobic conditions, it also exhibits nitric
CC       oxide reductase and FAD reductase activities. However, all these
CC       reactions are much lower than NOD activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 NO + 2 O(2) + NAD(P)H = 2 NO(3)(-) +
CC       NAD(P)(+).
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 heme B group per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Accumulates in macrocysts.
CC   -!- INDUCTION: By submerged conditions, in growing cells.
CC   -!- DOMAIN: Consists of two distinct domains; a 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; AB025583; BAA83810.1; -; mRNA.
DR   EMBL; AAFI02000190; EAL61168.1; -; Genomic_DNA.
DR   RefSeq; XP_629622.1; -.
DR   HSSP; P04252; 2VHB.
DR   GeneID; 3386245; -.
DR   KEGG; ddi:DDB_0191099; -.
DR   dictyBase; DDB0191099; fhbA.
DR   InterPro; IPR001834; Cyt_B5_reductase.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR012292; Globin.
DR   InterPro; IPR000971; Globin_subset.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
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; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; Detoxification; FAD; Flavoprotein; Heme;
KW   Iron; Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport;
KW   Transport.
FT   CHAIN         1    397       Flavohemoprotein A.
FT                                /FTId=PRO_0000327849.
FT   DOMAIN      151    266       FAD-binding FR-type.
FT   NP_BIND     208    211       FAD (By similarity).
FT   NP_BIND     279    284       NADP (By similarity).
FT   NP_BIND     390    393       FAD (By similarity).
FT   REGION        1    141       Globin (By similarity).
FT   REGION      150    397       Reductase (By similarity).
FT   REGION      272    397       NAD or NADP-binding (By similarity).
FT   ACT_SITE     94     94       Charge relay system (By similarity).
FT   ACT_SITE    136    136       Charge relay system (By similarity).
FT   METAL        84     84       Iron (heme proximal ligand) (By
FT                                similarity).
FT   BINDING     189    189       FAD (By similarity).
FT   SITE         30     30       Involved in heme-bound ligand
FT                                stabilization and O-O bond activation (By
FT                                similarity).
FT   SITE         83     83       Influences the redox potential of the
FT                                prosthetic heme and FAD groups (By
FT                                similarity).
FT   SITE        389    389       Influences the redox potential of the
FT                                prosthetic heme and FAD groups (By
FT                                similarity).
SQ   SEQUENCE   397 AA;  43925 MW;  9641037821908183 CRC64;
     MSLSQQSISI IKATVPVLQV HGVNITTTFY RNMFKANPQL LNIFNHSNQR EGKQQNALAN
     TVLQAAIHID KLNELNLAPI VHKHVALGVL PEHYPIVGTN LLGAIKEVLQ DAATDEILGA
     WGEAYGVIAQ AFIDAEAALY KVTEEQIGGW RDTREFIVDR KVEESSNIIS FYFKPADGKP
     IATYIPGQYI TIKVPLTLEN GEQRTHIRHY SLSDTPSEQY YRISVKKEDA LKKSDPNGVV
     SNHLHANVKV GDKVLLSPPA GDYVVDQLSS NPILLVSGGV GITPLLSMAK ATLAKQPERE
     VTFVHSSKNK QYQPFANELS QLEKSNKVKV STVHSETDGQ ITKDKLEKFI NPSQIKDTKV
     FICGPVSFMS AINKQLIELG YPKENISYEI FGPLTNV
//