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Database: UniProt
Entry: A8LZ06_SALAI
LinkDB: A8LZ06_SALAI
Original site: A8LZ06_SALAI 
ID   A8LZ06_SALAI            Unreviewed;       407 AA.
AC   A8LZ06;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE            EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN   OrderedLocusNames=Sare_3564 {ECO:0000313|EMBL:ABV99366.1};
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV99366.1};
RN   [1] {ECO:0000313|EMBL:ABV99366.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205 {ECO:0000313|EMBL:ABV99366.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) 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; CP000850; ABV99366.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8LZ06; -.
DR   STRING; 391037.Sare_3564; -.
DR   KEGG; saq:Sare_3564; -.
DR   PATRIC; fig|391037.6.peg.3592; -.
DR   eggNOG; COG0543; Bacteria.
DR   eggNOG; COG1017; Bacteria.
DR   HOGENOM; CLU_026437_2_1_11; -.
DR   OrthoDB; 3213438at2; -.
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; 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; 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   Transport {ECO:0000256|RuleBase:RU000356}.
FT   DOMAIN          2..133
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   DOMAIN          148..245
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          384..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  44388 MW;  826D939B4E4D50F0 CRC64;
     MDVTALRQSW NQVAAAGSRA AKYFYATLFV IAPETRTMFP VNMQYQEDKL LAALGHIITS
     LDDSAALTAF THRLGADHRR FHGVDLEGRP VPLADRHYMW VGQALLATLE HFVGPQWTPS
     LKASWAEAYQ AVAGLMLAGA AESEQHTPPS WRAEVITTER RRSDLSVITL RPNYRCDYLP
     GQSLPTQIPT LRTWRYLSPA NAPRPDGTIE FHVRAAGRFS THLVRRITVG DVLLLGHPVG
     ASLSAYDRAP HRPLLLIAGG TGLAPLRAIV EELQQGSGRP TTLVLGGYTP DDLYDHQTLL
     KLAASAPAMP RTDGSTAPWL RYVPTVELGW GWDGAVGRAV DVALRLGSWA EADILICGSP
     AMTQASITAL AASGVDPSRI MTESYDHSHY PPLSAAEARA PRNLNRE
//
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