ID A0A439CSR3_9PEZI Unreviewed; 441 AA.
AC A0A439CSR3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN ORFNames=EKO27_g9896 {ECO:0000313|EMBL:RWA05215.1};
OS Xylaria grammica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA05215.1, ECO:0000313|Proteomes:UP000286045};
RN [1] {ECO:0000313|EMBL:RWA05215.1, ECO:0000313|Proteomes:UP000286045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHI A82 {ECO:0000313|EMBL:RWA05215.1,
RC ECO:0000313|Proteomes:UP000286045};
RA Buettner E., Kellner H.;
RT "Draft genome sequence of Xylaria grammica IHI A82.";
RL Submitted (DEC-2018) 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 -!- SIMILARITY: Belongs to the globin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00238}.
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:RWA05215.1}.
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DR EMBL; RYZI01000465; RWA05215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A439CSR3; -.
DR STRING; 363999.A0A439CSR3; -.
DR Proteomes; UP000286045; 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 GO; GO:0062197; P:cellular response to chemical stress; IEA:UniProt.
DR CDD; cd08922; FHb-globin; 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; 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; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000286045}.
FT DOMAIN 15..133
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 148..296
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 224..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 49698 MW; A718B934A6EBF178 CRC64;
MLTRREAELV NETIPALRQH GEHISTVFYK SMLRDHPELN HYFNSVNMHT GRQPRALTAL
ILAFASNIVN ISELTDKLER VAQKHASLVI HPEHYEIVAK YLIRAFSAVL GPAMTPEVNV
AWTKAYWMMA KMLTGREQII YKDFGAWANW RPFTISAKTA ETSEGDIVSF TLTPVDGQPL
PPFKPGQYVT VRLKIKGHKY YQLRQYSLSD APRPDSYRVT VKRDIGASPE TLPDPRQFTS
FDDGPPISSA ASSASDSSIG SVRPHRPGLV SNVLIDDFQV GDGVELTHPA GEFFLDTNDP
NTSPVILISA GVGAAPLYPM LKAVSEQGYG RPVSWIQASR HDAPFREKVE KIAALDPNVK
VKFFRSRLAD GDVISLTSRF QEDFSRLNWE DLWLTNNLAQ YFVCGPEKFM NEIGNHLQKN
RVDPSRIRYE LYSVGSFEMK R
//
