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Database: UniProt
Entry: B1MIX1_MYCA9
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ID   B1MIX1_MYCA9            Unreviewed;       384 AA.
AC   B1MIX1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE            EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN   OrderedLocusNames=MAB_4269 {ECO:0000313|EMBL:CAM64342.1};
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP
OS   104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium
OS   abscessus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM64342.1, ECO:0000313|Proteomes:UP000007137};
RN   [1] {ECO:0000313|EMBL:CAM64342.1, ECO:0000313|Proteomes:UP000007137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 /
RC   TMC 1543 {ECO:0000313|Proteomes:UP000007137};
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(2009).
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: 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; CU458896; CAM64342.1; -; Genomic_DNA.
DR   RefSeq; WP_005086445.1; NZ_MLCG01000001.1.
DR   AlphaFoldDB; B1MIX1; -.
DR   GeneID; 66969704; -.
DR   KEGG; mab:MAB_4269; -.
DR   OMA; GARYRCE; -.
DR   Proteomes; UP000007137; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; 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; 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; 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.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000356}; Iron {ECO:0000256|RuleBase:RU000356};
KW   Metal-binding {ECO:0000256|RuleBase:RU000356};
KW   Monooxygenase {ECO:0000313|EMBL:CAM64342.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000313|EMBL:CAM64342.1};
KW   Oxygen transport {ECO:0000256|RuleBase:RU000356};
KW   Transport {ECO:0000256|RuleBase:RU000356}.
FT   DOMAIN          141..241
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   384 AA;  43220 MW;  ECFCE3C29D898EC7 CRC64;
     MGLEDVEALH DLVGGVELSG NKLVRSFYSR WFAIDPTVGD LFPADMSAQR EHFRQALQFV
     LWEMASYRTE GLVNFLAQLG RDHRKFGATD SQYDTMRQAL LDTTREVLQP IWDQRMEATA
     TEVYTVMIEV MRSAAASDIG QPWWDGKVIE FHRTSRDLAL IRLKLNAPMP YHCGQYVHVQ
     VPQSPRNWRY LSLAIPPDPE GYIEFHVRAV PGGLVSGDIV NKTKVGDTWR ISPPLGALSV
     NRDGGDILMV AGSTGIAPLR CLIMELSQWA ENPRVHLFYG ARYPQELYDL WTLWHIASTN
     PWLSVTPVTE YPRNPDWATE YHDPTPPRGL HVRQTGLLSE VVTAYGGWGD RQILIGGSAS
     MIQATKEALV SRGADASRIQ HDPL
//
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