ID A0A1G9CHX6_9ACTN Unreviewed; 391 AA.
AC A0A1G9CHX6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN ORFNames=SAMN05421874_108112 {ECO:0000313|EMBL:SDK51267.1};
OS Nonomuraea maritima.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=683260 {ECO:0000313|EMBL:SDK51267.1, ECO:0000313|Proteomes:UP000198683};
RN [1] {ECO:0000313|EMBL:SDK51267.1, ECO:0000313|Proteomes:UP000198683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5681 {ECO:0000313|EMBL:SDK51267.1,
RC ECO:0000313|Proteomes:UP000198683};
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 -!- 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; FNFB01000008; SDK51267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9CHX6; -.
DR STRING; 683260.SAMN05421874_108112; -.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000198683; 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; 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; 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; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
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:SDK51267.1};
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:SDK51267.1};
KW Oxygen transport {ECO:0000256|RuleBase:RU000356};
KW Reference proteome {ECO:0000313|Proteomes:UP000198683};
KW Transport {ECO:0000256|RuleBase:RU000356}.
FT DOMAIN 1..137
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 391 AA; 42483 MW; EB9962D64B607327 CRC64;
MLSEESAAVV RATLPLVGTH LDAIASRFYE TMFADRPELL DGLFNRGNQR SGDQRKALAG
AIAGFAGALL AHPDERPDAL LRRIAHKHAA VGVTDDQYVV VHKYLFGAIA EVLGDVVTPE
VAAAWDEVYW LMAGALIALE SRVHAETGTR PGHTWRTWTV AERREETADA VSLVLRPVGD
EPVPPTRPGQ YVSVRVRMPD GVHQLRQYSV SGQSADGLRR ITVKRVRGAD VPDGEVSSLL
HATVREGDEL TVSAPFGDVA LEDGDAPLVL VSAGIGCTPI TGMLEHLART GDSRQVLLLH
ADRSRADHAL REDMERLTDA LPAARRIFWY EDDHGLMDLD GVEIPQGAIV YLCGPVPFMR
VARGALLRAG VAARNLHYEV FGSDLWLPDA A
//
