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Database: UniProt
Entry: A0A135LFY9_PENPA
LinkDB: A0A135LFY9_PENPA
Original site: A0A135LFY9_PENPA 
ID   A0A135LFY9_PENPA        Unreviewed;       413 AA.
AC   A0A135LFY9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE            EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN   ORFNames=PGRI_017440 {ECO:0000313|EMBL:KXG47874.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG47874.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG47874.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG47874.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
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   -!- 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:KXG47874.1}.
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DR   EMBL; LHQR01000065; KXG47874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LFY9; -.
DR   STRING; 5078.A0A135LFY9; -.
DR   OMA; TEYYRIS; -.
DR   OrthoDB; 2096069at2759; -.
DR   Proteomes; UP000070168; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT   DOMAIN          4..135
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   DOMAIN          147..257
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   413 AA;  46142 MW;  9C809CD8D8D63776 CRC64;
     MSPEQVSVIT ATVPVLERYG QNITETFYRN MLAAHPELKS VFNMTNQQTG HQAKVLAGAL
     YAYAKSIRNL EALGPMLELI CHKHASLHIT PDQYDIVGKY LIEAMQEVLG DNFTSSVQYA
     WTAAYSQLAK IMIQKEASLN DQHEEWKDWR DFCIVTISRE SDEISSFYLS PVDGKPLPTF
     VPGQYVSVSV YVPQLGYTQA RQYSMSDVPS TEYYRISVKQ ERGQQFPPGV LSNVLHDIKA
     PGQIVKVSHP RGNFFLSSVS ETSPIVLVAG GVGITPLLSM LKFLTSTTST IKRPIHLIYA
     TRTTTARAFF KEIADTSRSN ATVRVTFFVG SPEAGDKAGC DYHHEGRLDL NRLDAQQDLF
     LNHTQTEYYI CGPSPFLEMV KRFLLVQRVE SSNIKMEVFG AGGFAETTSQ AHL
//
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