ID   HMP_VIBPA               Reviewed;         394 AA.
AC   P40609;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2003, sequence version 2.
DT   25-NOV-2008, entry version 69.
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=VP2809;
OS   Vibrio parahaemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB22;
RA   McCarter L.L.;
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 / Serotype O3:K6;
RX   MEDLINE=22508454; PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; U09005; AAA62190.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC61072.1; -; Genomic_DNA.
DR   RefSeq; NP_799188.1; -.
DR   HSSP; P24232; 1GVH.
DR   GeneID; 1190359; -.
DR   GenomeReviews; BA000031_GR; VP2809.
DR   KEGG; vpa:VP2809; -.
DR   NMPDR; fig|223926.1.peg.2809; -.
DR   HOGENOM; P40609; -.
DR   BioCyc; VPAR223926:VP2809-MON; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion 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; 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   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    394       Flavohemoprotein.
FT                                /FTId=PRO_0000052450.
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     387    390       FAD (By similarity).
FT   REGION        1    136       Globin.
FT   REGION      147    394       Reductase.
FT   REGION      259    394       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        386    386       Influences the redox potential of the
FT                                prosthetic heme and FAD groups (By
FT                                similarity).
FT   CONFLICT    118    118       D -> G (in Ref. 1; AAA62190).
SQ   SEQUENCE   394 AA;  44410 MW;  2B65A6A71C8AB7AE CRC64;
     MLSNQTIEIV KATAPLIAET GPKLTAHFYD RMFTHNPELK DIFNMSNQRN GDQREALFNA
     ICAYAANIEN LPALLGAVEK IAHKHTSFLI TKDQYQIVGK HLIATIDELF NPGQEVLDAW
     AEAYGVLANV FIQREEQIYQ ANASQEGGWR GLREFELVGK QLESEHICSF VFKPTDGSKV
     TKYKPGQYLG IYINSDKFEN QEIRQYSLSS SVQENTYRIS VKREQGGKVS NYLHDELNIG
     DKVKLAAPAG DFFMDVDTNT PVVLISAGVG LTPTLSMLES LTEHHAPVTW VHATENSKHH
     AFKEHVNQLV TAKENMNALI WYNQPTAEDK IGEDFHFTGF VNLHEIEAAL KQDNVQVYFC
     GPVGFMQHVA KQLQELGVPQ EQFHYECFGP HKVV
//