ID   A0A0F4YV87_TALEM        Unreviewed;       502 AA.
AC   A0A0F4YV87;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Glycolate oxidase {ECO:0000313|EMBL:KKA22187.1};
GN   ORFNames=T310_3786 {ECO:0000313|EMBL:KKA22187.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA22187.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA22187.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA22187.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KKA22187.1}.
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; LASV01000152; KKA22187.1; -; Genomic_DNA.
DR   RefSeq; XP_013328799.1; XM_013473345.1.
DR   AlphaFoldDB; A0A0F4YV87; -.
DR   STRING; 1408163.A0A0F4YV87; -.
DR   GeneID; 25316135; -.
DR   OrthoDB; 5474593at2759; -.
DR   Proteomes; UP000053958; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR   InterPro; IPR016170; Cytok_DH_C_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT   DOMAIN          61..244
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   502 AA;  56479 MW;  75BFD3D41ED4A83A CRC64;
     MDTTSKPPVA STDFPIRYDD PTYQHVHRTL LSGSLLRPLE PVLPQGMSQD DLDAALGQFV
     GVVGKDGVFV GKALEDYVDP YKLWEVEGKR RVPSAAVWYG GPAPRLTGSI ALDLHRMDRV
     IEVHDQYAYA VIKPGVTFTD LYNYCARNKL RVWPSVPSLR WGSVVGNTLD RGTGFTPTAT
     HHQHICGLEV MLADGDIVRT GQFAISNSPS SHLSKFTFGP SIEGLFLQSN LGIVTKLGIW
     LHPQPQAYMS CLFDMPDLED IETLVDIFGE LRRNGVLPNT VYVSNIVGAI PMWRIRELQT
     QLDMGYWSAK FGLYGPKDVI QAHYDELKRI VAEKAPRGRL RGEMFAGENG QLLDATAVPE
     PHGCFFVGIP SLWSLPMVRY RLPKDGTGIG AHTDYSAIIP SSGKTLLDWV QTAKKVCEAE
     AFDLLCDFFM HERHVIFVNM MAFDKSDARQ REAVNRIFHG LFREGKKRGF SNYRAHIDHM
     DLVAELYDFN DHAYQRFVER IK
//