ID A0A1H2DBL4_9ACTN Unreviewed; 402 AA.
AC A0A1H2DBL4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN ORFNames=SAMN04489716_9079 {ECO:0000313|EMBL:SDT80140.1};
OS Actinoplanes derwentensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT80140.1, ECO:0000313|Proteomes:UP000198688};
RN [1] {ECO:0000313|EMBL:SDT80140.1, ECO:0000313|Proteomes:UP000198688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT80140.1,
RC ECO:0000313|Proteomes:UP000198688};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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=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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT629758; SDT80140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2DBL4; -.
DR STRING; 113562.SAMN04489716_9079; -.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000198688; Chromosome i.
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; cd14782; FHb-globin_2; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 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; PTHR43396; FLAVOHEMOPROTEIN; 1.
DR PANTHER; PTHR43396:SF3; FLAVOHEMOPROTEIN; 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 Dioxygenase {ECO:0000313|EMBL:SDT80140.1};
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 Oxidoreductase {ECO:0000313|EMBL:SDT80140.1};
KW Oxygen transport {ECO:0000256|RuleBase:RU000356};
KW Reference proteome {ECO:0000313|Proteomes:UP000198688};
KW Transport {ECO:0000256|RuleBase:RU000356}.
FT DOMAIN 9..141
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 153..262
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 402 AA; 44382 MW; D429C74566BBF2C3 CRC64;
MLSDRARPVI QATLPVVGEH IEEIAQRFYA HMFAAHPEFK DGMFNRGNQA EGSQPKALAG
SVAVFAGTLL AVPEQFPDRL LTRIAHKHAS LGIRPDQYPV VHDHLMWAVG DVLGDAVTPE
VAAAWDEVYW LMAYALINQE RGLYSARGVT AERVWRQWRV AEKIQETGDV VTFVMRRIDD
RLVKTSLPGQ YVSVLAEMAD GVRQPRQFSL TRADDGEHRY FAVKRVHGGG KPDGEVSNLL
HDRIQPGDEL TMSVPYGDVV LDDSGRPVVF ASAGIGVAPM AGMLSHMVAA SSHLTVTMLH
ADTNESSFPL RRQIADDLAH LPKSRIYTWY ENGAHSDLPV TGVFAGTMNL AQVELPDSAV
YYLCGPLPFL QAVRGALIDH GIPARDIQYE MFGPDLWHAD TE
//
