GenomeNet

Database: UniProt
Entry: A0A168NA47_MUCCL
LinkDB: A0A168NA47_MUCCL
Original site: A0A168NA47_MUCCL 
ID   A0A168NA47_MUCCL        Unreviewed;       347 AA.
AC   A0A168NA47;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN   ORFNames=MUCCIDRAFT_78931 {ECO:0000313|EMBL:OAD06004.1};
OS   Mucor lusitanicus CBS 277.49.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD06004.1, ECO:0000313|Proteomes:UP000077051};
RN   [1] {ECO:0000313|EMBL:OAD06004.1, ECO:0000313|Proteomes:UP000077051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD06004.1,
RC   ECO:0000313|Proteomes:UP000077051};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:OAD06004.1}.
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; AMYB01000002; OAD06004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168NA47; -.
DR   STRING; 747725.A0A168NA47; -.
DR   VEuPathDB; FungiDB:QYA_78931; -.
DR   OrthoDB; 1385925at2759; -.
DR   Proteomes; UP000077051; 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; IPR023209; DAO.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR   PANTHER; PTHR11530:SF11; D-ASPARTATE OXIDASE; 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:UP000077051}.
FT   DOMAIN          4..336
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   BINDING         45..46
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         184
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ   SEQUENCE   347 AA;  39125 MW;  298321DA9AD775FB CRC64;
     MSDKIVVLGA GVTGLTSAIS LLRKGYKDVT VVSKHVPGDW SSEYTSPWAG ASILTVAAHD
     DYRLQEMDLY TMKEFERLSK EEPEAHVMPC KGIQYCEDPA LPGEDPHWVR KIYKDVKEIP
     KSELIPGVSY GYTFESFTAN VPKYLQWLVN TLRSLGGRLE RKSFESIQQA IEEFPEATVI
     VNCTGLGSYY LTDVKDHTMY PIRGQTVTVR APHIKTQHYI DASNRWTYII PRDDGTVICG
     GTVDRENRST SPDDAITKDI LERVYKLYPE ITHHKGPDHF DIVGVNVGFR PGRKGGIRLE
     KETRRRSNGQ KVTVCHNYGH SSHGYQSSWG SCAKLVELVS NERLSKL
//
DBGET integrated database retrieval system