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Entry: A0A0M4QSD0_9MICC
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ID   A0A0M4QSD0_9MICC        Unreviewed;       390 AA.
AC   A0A0M4QSD0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE            EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN   ORFNames=AOC05_18310 {ECO:0000313|EMBL:ALE93816.1};
OS   Arthrobacter alpinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE93816.1, ECO:0000313|Proteomes:UP000062833};
RN   [1] {ECO:0000313|EMBL:ALE93816.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R3.8 {ECO:0000313|EMBL:ALE93816.1};
RA   See-Too W.S., Chan K.G.;
RT   "Complete genome of Arthrobacter alpinus strain R3.8.";
RL   Submitted (MAR-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   -!- 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; CP012677; ALE93816.1; -; Genomic_DNA.
DR   RefSeq; WP_062009084.1; NZ_CP012677.1.
DR   AlphaFoldDB; A0A0M4QSD0; -.
DR   KEGG; aaq:AOC05_18310; -.
DR   PATRIC; fig|656366.3.peg.3949; -.
DR   OrthoDB; 9801223at2; -.
DR   Proteomes; UP000062833; 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; 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; 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   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   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:UP000062833};
KW   Transport {ECO:0000256|RuleBase:RU000356}.
FT   DOMAIN          9..138
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   DOMAIN          151..256
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   390 AA;  42085 MW;  C286CF548B820B8C CRC64;
     MLSEKSRPLI TATLPLVGSR LGTITPNFYS RMLTAHPELL DGLFSRANQN NGEQQKALAG
     SIAGFASALV ANPDIIPEQL LSRIAHKHTA LGITEDQYDI VYKYLFEAIA EELADVITAE
     IADAWTEVYW LMANALIKIE KGLYALQAND KMWMPWTVIE KNPAGTDAMT FVLAPADDTP
     VTVARPGQFV SVKVALPDGL LQVRQYSLSA DVESTTRRVF TTKKDDGGEV SPVLHNNVQV
     GDVLELSNPY GDVTLDGEGP VVFATAGIGC TPSASALRSL AATGTDREVM VLHAEKNLAA
     WALRDQMTND VDAIDGAELQ LWLEEPTEGF HKGFMSLAGL DIPANASMYV CGPLPFMKAI
     RNQAIDAGIP STKIHYEVFG PDLWLAGAAS
//
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