ID A0A0N0N061_9ACTN Unreviewed; 396 AA.
AC A0A0N0N061;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN ORFNames=OK006_3368 {ECO:0000313|EMBL:KPI13929.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI13929.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI13929.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI13929.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-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=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 -!- 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:KPI13929.1}.
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DR EMBL; LJCU01000109; KPI13929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0N061; -.
DR PATRIC; fig|1592326.3.peg.3795; -.
DR Proteomes; UP000037912; Unassembled WGS sequence.
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:KPI13929.1};
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:KPI13929.1};
KW Oxygen transport {ECO:0000256|RuleBase:RU000356};
KW Transport {ECO:0000256|RuleBase:RU000356}.
FT DOMAIN 2..137
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 152..262
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 396 AA; 42639 MW; 7AEE4E0E8AED2B09 CRC64;
MLSEPSAATV RATLPAVGAA IGEIADRFYE RLFAAHPELL RDLFNRGNQA SGTQRRALAG
SIAAFATHLV ERPDERPDVL LNRIAHKHAS LGIAPEQYAT VREHLFAAIA EVLGDAVTPE
VEAAWDEVYW LMANALIAIE RRLYAQHGDG RGRWRAWEVV ERVEETADVA TFRLRPADGG
PLPDFRAGQY VSVRVELPDG AHQIRQYSLS SAPGSPVRQI GVKRVHGEAS GPDGEVSNHL
HTRVHVGSTI ELSAPYGDLV LDDTDAPVLL ASAGIGVTPV IAMLEQLALT GHHAPVTVVH
ADRSPADHAL RADHEAYAAK LADAAVHFWY EQDAEGAGRP GRADLSSVAV ASGTRAYLCG
PLPFMRAVRG QLIDKGVAPA DIHYEVFGPD LWLAQG
//
