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Database: UniProt
Entry: A0A0X3V2D3_9ACTN
LinkDB: A0A0X3V2D3_9ACTN
Original site: A0A0X3V2D3_9ACTN 
ID   A0A0X3V2D3_9ACTN        Unreviewed;       475 AA.
AC   A0A0X3V2D3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE            EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN   ORFNames=ADL22_16200 {ECO:0000313|EMBL:KUL38945.1};
OS   Streptomyces sp. NRRL F-4489.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL38945.1, ECO:0000313|Proteomes:UP000053256};
RN   [1] {ECO:0000313|EMBL:KUL38945.1, ECO:0000313|Proteomes:UP000053256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL38945.1,
RC   ECO:0000313|Proteomes:UP000053256};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC       {ECO:0000256|ARBA:ARBA00006401}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUL38945.1}.
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DR   EMBL; LLZI01000221; KUL38945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X3V2D3; -.
DR   STRING; 1609095.ADL22_16200; -.
DR   OrthoDB; 3213438at2; -.
DR   Proteomes; UP000053256; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; 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   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053256}.
FT   DOMAIN          108..180
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   DOMAIN          198..298
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  51308 MW;  982AB7F4503C0BC7 CRC64;
     MHQSRRSPRP LPGGRPVPPA RDTVGDEYHA LLARHDAMRL RRRILGQGRS PAPDLTPAYD
     GAADQRLITQ YLDLVTPFGE LIAHLYDEMF ARRPSLRSLF PASMEFQRAH LARAFWYLIE
     NLHRTDEVAA YFRQLGHDHR KLGVRPAHYE AFETALRAAL RRSAGPRWAE AVEEAWVRML
     RFAVASMVAG AEAALAEPPC WRGTVTAHER RRPDLAVLRV RVHEPYPYRA GQYAAVESPL
     MPQAWRHYSL ACAPRADGEL EFHIRQTGPG GVSEALVSRT EPGDILRLGP AHGTMALGPE
     DHAGEVLMVA GGTGWAPVKA LLEEWAGRRR GAGGLPVRPA GRVHLFVGAR SRAELYDAGA
     LAQLAARNRW LRVVRVLDEE AARGAGRSPG EYGPLAEAVA RDGSWAGALA FVSGPAAMVG
     ATVARLTAAG LPAGRIRHDP LPDALPAAAA RATAYAADAG SAGGVDDAAM TGAAR
//
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