ID A0A0L8LKZ4_9ACTN Unreviewed; 627 AA.
AC A0A0L8LKZ4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN ORFNames=ADK74_31960 {ECO:0000313|EMBL:KOG38741.1};
OS Streptomyces decoyicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=249567 {ECO:0000313|EMBL:KOG38741.1, ECO:0000313|Proteomes:UP000037606};
RN [1] {ECO:0000313|Proteomes:UP000037606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2666 {ECO:0000313|Proteomes:UP000037606};
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA Blagden T., Winegar R.A.;
RL Submitted (JUL-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:KOG38741.1}.
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DR EMBL; LGUU01000272; KOG38741.1; -; Genomic_DNA.
DR RefSeq; WP_030075797.1; NZ_LGUU01000272.1.
DR AlphaFoldDB; A0A0L8LKZ4; -.
DR PATRIC; fig|249567.6.peg.7037; -.
DR Proteomes; UP000037606; 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 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; PR00371; FPNCR.
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}.
FT DOMAIN 251..376
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 387..487
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 67722 MW; 7D866D3573834F7A CRC64;
MDAPTTTSAD SGSSGGSSGN WGWFTPPAKK SSDEQQERQN SQDRPQDEDG RAEPDGRSER
HDRRDRHERN ARDERNDREQ IPSRPVNSIR PVGTAAERER EPEQQPQAPA SRHAAARPSG
AAVYLEQPFA PAYPEQPATY PEQPATYPEQ PAADPGYAAP APAYAPPRRE AEPPRGREPE
PVHESARPTG APAVSVPTGA VPAAEPRVQN EAPAAAPSAF TPKARPAAPA PEPSLDALQA
SASSATPASP DAVLIRRTMA EIEPVADKVT SYFYALLFVQ YPDLRALFPA SMDTQRDRLF
KALLTAAQHV DDADVLTAYL SNLGRGHRKY GTQPDHYPAV GECLLNALAR YATSSWGPET
QAAWVRAYTA ISQIMIDAAA EDEAVAPAWW QAEVVSHELR TPDIAVVMVR PDQPYPFLAG
QYASVETPWW PRVWRHYSFA SAPRSDGLLS FHVKAVPAGW VSNAMVHRAR PGDVIRLGAP
GGSMTVDHST RSGLLCVGGG TGIAPIKALV EDVAEHGVRR PVEVFYGARS DHDLYDLDTM
LRLEQTHPWL SVRPVVATGP AARGGTSSET GQLPDAVRQY GPFREYDAYL SGPPGLIRSG
VDALVGVGIP TERIRHDSVD QLVSAGD
//
