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Database: UniProt
Entry: V9XHI9_9NOCA
LinkDB: V9XHI9_9NOCA
Original site: V9XHI9_9NOCA 
ID   V9XHI9_9NOCA            Unreviewed;       386 AA.
AC   V9XHI9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE            EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN   ORFNames=Y013_10680 {ECO:0000313|EMBL:AHD21110.1}, Y013_14800
GN   {ECO:0000313|EMBL:AHD21838.1};
OS   Rhodococcus pyridinivorans SB3094.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD21838.1, ECO:0000313|Proteomes:UP000018781};
RN   [1] {ECO:0000313|EMBL:AHD21838.1, ECO:0000313|Proteomes:UP000018781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB3094 {ECO:0000313|EMBL:AHD21838.1,
RC   ECO:0000313|Proteomes:UP000018781};
RX   PubMed=24874690;
RA   Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA   Nielsen P.H., Nielsen J.L.;
RT   "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT   Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL   Genome Announc. 2:e00525-14(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate;
CC         Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.14.12.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000126};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate;
CC         Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.14.12.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00001762};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- SIMILARITY: Belongs to the globin family.
CC       {ECO:0000256|RuleBase:RU000356}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC       {ECO:0000256|ARBA:ARBA00006401}.
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DR   EMBL; CP006996; AHD21110.1; -; Genomic_DNA.
DR   EMBL; CP006996; AHD21838.1; -; Genomic_DNA.
DR   RefSeq; WP_024101900.1; NC_023150.1.
DR   AlphaFoldDB; V9XHI9; -.
DR   GeneID; 29940627; -.
DR   KEGG; rpy:Y013_10680; -.
DR   KEGG; rpy:Y013_14800; -.
DR   PATRIC; fig|1435356.3.peg.2140; -.
DR   eggNOG; COG0543; Bacteria.
DR   eggNOG; COG1017; Bacteria.
DR   HOGENOM; CLU_026437_2_1_11; -.
DR   Proteomes; UP000018781; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0008941; F:nitric oxide dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd19753; Mb-like_oxidoreductase; 1.
DR   CDD; cd06187; O2ase_reductase_like; 1.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   PANTHER; PTHR47354:SF5; PROTEIN RFBI; 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   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000356}; Iron {ECO:0000256|RuleBase:RU000356};
KW   Metal-binding {ECO:0000256|RuleBase:RU000356};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxygen transport {ECO:0000256|RuleBase:RU000356};
KW   Transport {ECO:0000256|RuleBase:RU000356}.
FT   DOMAIN          55..135
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   DOMAIN          143..243
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   386 AA;  42581 MW;  9E2F582148C384C8 CRC64;
     MEAFAIARVQ LSFASIIATP TGAERFATAF YNAMWSESTG IRSLFPAGME SMRQRFATAV
     GWVVARLHEP GTVDRFLAQL ARDHRKYGVE PLHYRVAGNA LLAAVRECTP LILWTAALER
     TWAEVVDGVV ETMATAAATD DLPASWGATV VGHERVLPDL AIIRLEADSS IPYYAGQYMS
     VQIPQRPHMW RYLSAAIPPN PYGQIEFHVR RVSTGWVSPA LVGETAVGDR WTIGPPLGGL
     HVDRESGRDV LMIASGTGLA PMRAQIMEMA MRGDNPRVHL FYGGKYPCDL YDLETLWQIA
     TTNPWLTIVP VLEEKENPWW HPVPAKEPPT GLNRPMYGKL GKVAGQFGTW ADRQIQIAGS
     PSMIRTTLYA LSAAGTPRQN ISFDPL
//
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