ID   HMP_DICD3               Reviewed;         395 AA.
AC   Q47266;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 64.
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;
DE   AltName: Full=Hemoprotein X;
GN   Name=hmp; Synonyms=hmpX;
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95291435; PubMed=7773389;
RA   Favey S., Labesse G., Vouille V., Boccara M.;
RT   "Flavohaemoglobin HmpX: a new pathogenicity determinant in Erwinia
RT   chrysanthemi strain 3937.";
RL   Microbiology 141:863-871(1995).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; X75893; CAA53500.1; -; Genomic_DNA.
DR   PIR; S44277; S44277.
DR   HSSP; P24232; 1GVH.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Cytoplasm; Detoxification; FAD; Flavoprotein; Heme; Iron;
KW   Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Transport.
FT   CHAIN         1    395       Flavohemoprotein.
FT                                /FTId=PRO_0000052434.
FT   DOMAIN      150    255       FAD-binding FR-type.
FT   NP_BIND     204    207       FAD (By similarity).
FT   NP_BIND     268    273       NADP (By similarity).
FT   NP_BIND     388    391       FAD (By similarity).
FT   REGION        1    138       Globin.
FT   REGION      147    395       Reductase.
FT   REGION      259    395       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        387    387       Influences the redox potential of the
FT                                prosthetic heme and FAD groups (By
FT                                similarity).
SQ   SEQUENCE   395 AA;  44315 MW;  05C43167559CF6E6 CRC64;
     MLDQQTIATI KSTIPLLAET GPALTAHFYQ RMFHHNPELK DIFNMSNQRN GDQREALFNA
     ICAYATHIEN LPALLPAVER IAQKHASFNI QPEQYQIVGT HLLATLEEMF QPGQAVLDAW
     GKRYGVLANV FIQRESDIYQ QSAGQNGGWH GIRPFRIVAK QPQSSLITSF TLEPVDGGPI
     AAFRPGQYLA VYIRDKRFEY QEIRQYSLTN EPNGRYYRIA VKRETMGSVS GYLHDVAREG
     DVIELAAPHG DFYLEVTPET PVALISAGVG QTPMLSMLHS LKNQQHQADI FWLHAAENTE
     VHAFADEIAD VAATLPQLQS YVWYREASSE AARSAHAFHG LMALKDLPTP LPMTNLHCYL
     CGPVAFMQFA ARQLLELGIT ESQIHYECFG PHKVI
//