ID A0A1M4WDX2_STRHI Unreviewed; 409 AA.
AC A0A1M4WDX2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN ORFNames=SAMN05444320_1011101 {ECO:0000313|EMBL:SHE79375.1};
OS Streptoalloteichus hindustanus.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Streptoalloteichus.
OX NCBI_TaxID=2017 {ECO:0000313|EMBL:SHE79375.1, ECO:0000313|Proteomes:UP000184501};
RN [1] {ECO:0000313|EMBL:SHE79375.1, ECO:0000313|Proteomes:UP000184501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44523 {ECO:0000313|EMBL:SHE79375.1,
RC ECO:0000313|Proteomes:UP000184501};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQVN01000001; SHE79375.1; -; Genomic_DNA.
DR RefSeq; WP_073480109.1; NZ_FQVN01000001.1.
DR AlphaFoldDB; A0A1M4WDX2; -.
DR STRING; 2017.SAMN05444320_1011101; -.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000184501; 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 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:SHE79375.1};
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:SHE79375.1};
KW Oxygen transport {ECO:0000256|RuleBase:RU000356};
KW Reference proteome {ECO:0000313|Proteomes:UP000184501};
KW Transport {ECO:0000256|RuleBase:RU000356}.
FT DOMAIN 1..138
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 152..261
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 409 AA; 44281 MW; 504A445FD72C1BD2 CRC64;
MLSEESARVV RATAEVVAAH GEQITARFYE RMFAARPEML DLFNRGSQAN GEQRQALAAA
VVAFAGHAAG LRPVPLGTLL SRIAHKHASV GIAPNQYVIV GRHLMAAVAE VLGDAVTPEV
AAAWDEVYWA FACMLVAEEA RLYQRAGTGF ERPFHPHRVV RRETETADVE SFWLEPESGQ
PVQHQTGQYV SVAVRLPDNS RQIRQYTISS APGRDLLRIT VKRHREDGQR PAGLVSTQLH
DHVRAGDRLL VSPPFGDVVL PPGDSPLLLV TAGIGITPAA AVLDDLTARA SDREVVVAHA
DRSPASHALS AELLAAASRL PRHTVQLWYE ADHVAADVPA GTEVRSGRID PAELRVPDGA
RAVLCGPLPF MRQVRRGLLD RGVPADRIHY EVFGADAWLP RATSTAPVG
//
