ID A0A147EA47_9MICC Unreviewed; 400 AA.
AC A0A147EA47;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN ORFNames=AN277_0206620 {ECO:0000313|EMBL:OAX51846.1}, I6G21_05955
GN {ECO:0000313|EMBL:QPT52879.1};
OS Rothia kristinae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=37923 {ECO:0000313|EMBL:OAX51846.1, ECO:0000313|Proteomes:UP000053171};
RN [1] {ECO:0000313|EMBL:OAX51846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RUTW2-3 {ECO:0000313|EMBL:OAX51846.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171};
RA Waterworth S., Matcher G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:OAX51846.1, ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171}, and RUTW2-3
RC {ECO:0000313|EMBL:OAX51846.1};
RA Waterworth S.C., Walmsley T.A., Matongo T., Davies-Coleman M.T.,
RA Dorrington R.A.;
RT "Identification of putative biosynthetic pathways for the production of
RT bioactive secondary metabolites by the marine actinomycete Kocuria
RT kristinae RUTW2-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QPT52879.1, ECO:0000313|Proteomes:UP000594975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_864 {ECO:0000313|EMBL:QPT52879.1,
RC ECO:0000313|Proteomes:UP000594975};
RA Sproer C., Gronow S., Severitt S., Schroder I., Tallon L., Sadzewicz L.,
RA Zhao X., Boylan J., Ott S., Bowen H., Vavikolanu K., Mehta A.,
RA Aluvathingal J., Nadendla S., Lowell S., Myers T., Yan Y., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-2020) 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}.
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DR EMBL; LJBJ02000011; OAX51846.1; -; Genomic_DNA.
DR EMBL; CP065738; QPT52879.1; -; Genomic_DNA.
DR RefSeq; WP_058730278.1; NZ_NOIV01000004.1.
DR AlphaFoldDB; A0A147EA47; -.
DR STRING; 37923.BK826_05520; -.
DR GeneID; 44527411; -.
DR KEGG; rkr:I6G21_05955; -.
DR PATRIC; fig|37923.10.peg.1452; -.
DR Proteomes; UP000053171; Unassembled WGS sequence.
DR Proteomes; UP000594975; Chromosome.
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; 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 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 Oxygen transport {ECO:0000256|RuleBase:RU000356};
KW Reference proteome {ECO:0000313|Proteomes:UP000053171};
KW Transport {ECO:0000256|RuleBase:RU000356}.
FT DOMAIN 9..137
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 151..254
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 400 AA; 44003 MW; 400472F043623CE0 CRC64;
MLSEKSRPVV EATLPVIAER IPHITPVFYR DMFAARPDLM DGMFSRSSQL EGTQPRALAG
SIAVFAQWIV QHPDSYPEEV LSRVAHKHAS LGLRPEEYPT VYRYLFGAIA KDLGEAATEE
VVAAWTEVYW LMADALIALE KGLYAVQAND VMRAPFRLVR RVRAADDVAD LTFEPADDTP
MTPAQAGQYV SIFCRAEDGL LQPRQFTLLP SEPGQRRIAV KLDPAGEMTP IILDKLTEGD
VIEISNPYGD VTLGGFGDDG DGPLWLFSAG IGVTPMIAFV SELVRQGSQR EVTVVHTARD
FASWPLREEL AELVARLPHG RLISCTTASA EGDHAGRVRV PELDVPADAV AYLCGPLPFM
KDVRSQLVDA GVPGQRIRYE IFGPDQWMLH DQAREEPAAA
//
