ID A0A0D1YM85_9EURO Unreviewed; 446 AA.
AC A0A0D1YM85;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Flavohemoprotein {ECO:0000256|ARBA:ARBA00014637};
DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
DE AltName: Full=Flavohemoglobin {ECO:0000256|ARBA:ARBA00030929};
DE AltName: Full=Hemoglobin-like protein {ECO:0000256|ARBA:ARBA00030024};
DE AltName: Full=Nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00033187};
GN ORFNames=PV11_04311 {ECO:0000313|EMBL:KIV82184.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV82184.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV82184.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV82184.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) 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=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. Two-domain flavohemoproteins
CC subfamily. {ECO:0000256|ARBA:ARBA00008414}.
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; KN846952; KIV82184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YM85; -.
DR STRING; 1016849.A0A0D1YM85; -.
DR HOGENOM; CLU_003827_12_0_1; -.
DR OrthoDB; 2096069at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; 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 GO; GO:0062197; P:cellular response to chemical stress; IEA:UniProt.
DR GO; GO:0051409; P:response to nitrosative stress; IEA:InterPro.
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 HAMAP; MF_01252; Hmp; 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; IPR023950; Hmp.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43396; FLAVOHEMOPROTEIN; 1.
DR PANTHER; PTHR43396:SF9; NITRIC OXIDE DIOXYGENASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599}.
FT DOMAIN 47..178
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 195..306
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 446 AA; 49004 MW; 34EBCF3093305F7B CRC64;
MLARRQLFKL ASSTKTTSSL RGAIPATVTM TSTAGFHSSP PRHELSAEHQ KIVKSTAPVL
AEHGVIITSH FYKRMLENHP ELKNIFNAAH QSTGTQPAAL AHAVWAYASN IDNLGALTTA
VSRIGHKHAS LGIRPDHYPI VGENLLASIK EVLGDAVNQP VLDAWAAAYQ QLADIFINFE
KDLYQKAEQT PGGWTGWRKF KVAHKVHESD EIISFYLEPV DGAKLPEFKS GQYISVRVFV
PELGVYQPRQ YSLSDIPDAK HFRISVKKES AKGLAPAGRI SNVLHENVPE GEEMDVSNPY
GDFTLDVETD VPVVLISGGV GITPMLSMLG TLVDHAPKRN VVFVHAARGG NVHAMKDHLS
KIMKDNSQVS KVIFYENVAE AEREGVDYDY KGRIELEKVK DKVLLPDANY YICGPIPFMQ
SQQKALEGLG VPSERIHSEV FGSGIA
//
