ID B6H5S5_PENRW Unreviewed; 349 AA.
AC B6H5S5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Pc14g00970 protein {ECO:0000313|EMBL:CAP74238.1};
GN ORFNames=Pc14g00970 {ECO:0000313|EMBL:CAP74238.1}, PCH_Pc14g00970
GN {ECO:0000313|EMBL:CAP74238.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP74238.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP74238.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000189-1};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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DR EMBL; AM920429; CAP74238.1; -; Genomic_DNA.
DR RefSeq; XP_002560091.1; XM_002560045.1.
DR AlphaFoldDB; B6H5S5; -.
DR STRING; 500485.B6H5S5; -.
DR GeneID; 8310333; -.
DR KEGG; pcs:Pc14g00970; -.
DR VEuPathDB; FungiDB:PCH_Pc14g00970; -.
DR eggNOG; KOG3923; Eukaryota.
DR HOGENOM; CLU_034311_3_0_1; -.
DR OMA; HDSTPWE; -.
DR OrthoDB; 2902754at2759; -.
DR BioCyc; PCHR:PC14G00970-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c14.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF16; D-AMINO ACID OXIDASE (AFU_ORTHOLOGUE AFUA_5G11290); 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000189-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000189-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT DOMAIN 4..328
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 158
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 176
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 349 AA; 39356 MW; C486D76CBA4AFC6B CRC64;
MSKITILGAG ITGMGIASQL PKNTEITILG DFLPGDAMDQ RYVSQWAGAI WLGVHDSTPW
EQGMQLNSFS ELWRIAERHP ESGIRQIEMT EIMDIGDPAK VWYQGKVPGF RFLSPSELPK
GAKFGMAFQT LVITPPTFLS WFRQHLEKQG VRFQRTYVKS LRDLRGMGHD VLINATGFGA
MKLLDVEEKR ITPVRQQNIR LRKDGYNRCY IRRGPDGYYS TAFARGDGTI YMGGIKSLGD
TDFASYEDQR KEILQRQHHN QPDVFPSPNP LEYDIITDHV GVFPIIESQN GGVRVEKQVL
HGQKVIHAYG QEAGGYTFSF GLGQQVSEYV QEYLTELPKP AETPIPSKL
//
