GenomeNet

Database: UniProt
Entry: F7VXP1_SORMK
LinkDB: F7VXP1_SORMK
Original site: F7VXP1_SORMK 
ID   F7VXP1_SORMK            Unreviewed;       388 AA.
AC   F7VXP1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=WGS project CABT00000000 data, contig 2.12 {ECO:0000313|EMBL:CCC10285.1};
GN   ORFNames=SMAC_02862 {ECO:0000313|EMBL:CCC10285.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC10285.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC10285.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC10285.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA   Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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}.
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:CCC10285.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CABT02000012; CCC10285.1; -; Genomic_DNA.
DR   RefSeq; XP_003348365.1; XM_003348317.1.
DR   AlphaFoldDB; F7VXP1; -.
DR   STRING; 771870.F7VXP1; -.
DR   GeneID; 10805823; -.
DR   KEGG; smp:SMAC_02862; -.
DR   VEuPathDB; FungiDB:SMAC_02862; -.
DR   eggNOG; KOG3923; Eukaryota.
DR   HOGENOM; CLU_034311_2_0_1; -.
DR   InParanoid; F7VXP1; -.
DR   OMA; LWWPYRI; -.
DR   OrthoDB; 1385925at2759; -.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
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; IPR006181; D-amino_acid_oxidase_CS.
DR   InterPro; IPR023209; DAO.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR   PANTHER; PTHR11530:SF26; FAD DEPENDENT OXIDOREDUCTASE SUPERFAMILY (AFU_ORTHOLOGUE AFUA_5G13940); 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.
DR   PROSITE; PS00677; DAO; 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:UP000001881}.
FT   DOMAIN          8..373
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   BINDING         55..56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         199
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         230
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ   SEQUENCE   388 AA;  42506 MW;  BC9127BF2ED36E1C CRC64;
     MSNKSKGHVV VIGAGVIGLS SALALLEANY TTTILAKDLP APFESIDPRG QINFTSPWGG
     AHNRWVPPFP TVPSTPLTAA QQSEHALRAR EHAFSLSTFH RMKHFQSQNQ AQQAGITFLK
     GIEYLETPGP EYLSLTAERA SQELGLPGTF RVLESHEFPD DKITWGCEYD TWCVNPMQYC
     LFLLGQIIAR GGKVFKREVR STAEVFQLFS DGVKEFGETL PKADAVVNAT GVGMGDDELV
     FPTRGQTCLV QEPCEATVTR QNADGSWTFC VPRGYGAGTI IGGTKEPDNW DPKPDPQARE
     RLLRAFEGTY PKMLAEGKTR LTPVRDIVGR RPTRKGGLRL EGEMVDGAGF VMHAYGLGGR
     GYELSWGVAE GVVEGIKGYL EKERGSRL
//
DBGET integrated database retrieval system