ID   HMP_PSEAE               Reviewed;         393 AA.
AC   Q9I0H4;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-NOV-2008, 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; Synonyms=fhp; OrderedLocusNames=PA2664;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE004091; AAG06052.1; -; Genomic_DNA.
DR   PIR; F83311; F83311.
DR   RefSeq; NP_251354.1; -.
DR   HSSP; P04252; 1VHB.
DR   GeneID; 882373; -.
DR   GenomeReviews; AE004091_GR; PA2664.
DR   KEGG; pae:PA2664; -.
DR   PseudoCAP; PA2664; -.
DR   HOGENOM; Q9I0H4; -.
DR   BioCyc; PAER208964:PA2664-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    393       Flavohemoprotein.
FT                                /FTId=PRO_0000052439.
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     384    387       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        383    383       Influences the redox potential of the
FT                                prosthetic heme and FAD groups (By
FT                                similarity).
SQ   SEQUENCE   393 AA;  43658 MW;  6384A119B51AD82B CRC64;
     MLSNAQRALI KATVPLLETG GEALITHFYR TMLGEYPEVR PLFNQAHQAS GDQPRALANG
     VLMYARHIDQ LQELGPLVAK VVNKHVSLQV LPEHYPIVGT CLLRAIREVL GEQIATDEVL
     EAWGAAYQQL ADLLIEAEES VYAASAQADG GWRGVRRFRV ARKQAESEEI TSFYLEPVDG
     QPLLAFQPGQ YIGLRLDIDG EEVRRNYSLS AASNGREYRI SVKREAGGRV SNYLHDRVAE
     GDELDLFPPA GDFVLRDSDK PLVLITAGVG ITPALAMLQE ALPQARPIRF IHCARHGGVH
     AFRDWIEDVS AQHEQVEHFF CYSEPRAGDS ADAEGLLSRE KLADWLPQER DLDAYFLGPR
     PFMAQVKRHL ADLGVPSQQC HYEFFGPAAA LDA
//