ID   S6H889_9GAMM            Unreviewed;       486 AA.
AC   S6H889;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Glycolate oxidase subunit D {ECO:0000313|EMBL:EPJ44158.1};
GN   ORFNames=OFPII_37320 {ECO:0000313|EMBL:EPJ44158.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ44158.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ44158.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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:EPJ44158.1}.
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DR   EMBL; ASZJ01000176; EPJ44158.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6H889; -.
DR   PATRIC; fig|1330036.3.peg.3573; -.
DR   Proteomes; UP000014822; 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; 3.30.70.2740; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF1; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 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   Reference proteome {ECO:0000313|Proteomes:UP000014822}.
FT   DOMAIN          45..223
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   486 AA;  51882 MW;  598D0840FFBA4C33 CRC64;
     MVDSSVKNIS KQQLAKLFKT FINPDFVIVD SETQKPYECD GLSMYCEMPM LVVLPERISE
     VQKVLRICHQ YNIPIVPRGA GTGLCAGAMP SASGVVLSMA KFDQIIAIDP LARTARLEPG
     VTNLAISEAA SEFGLYYAPD PSSQVACTIG GNVAENSGGV HCLKYGLTIH NVLRLKILTV
     EGDLLTFGSE GLDCAGLDML AIFIGSEGLL GVVTEVLVKL LPVPEKAQVV MAGFGTIVAA
     GDAVAAVIAQ GIIPAGLEMM DEHAIIAAEA YVNAGYPLES KALLLCELDG TEGEVEQYIA
     VVAGIFKDLG AQSIRISSSA AERALLWQGR KSAFPAIGRI SPDYYCMDGT IPRGQLANVL
     TAMERRASAL GLRVANVFHA GDGNLHPLIL FDDSVPGEFQ KAEQLGAWIL EYCVAVGGSI
     TGEHGVGVEK IRQMPIQFTD REIAQFHALK NAFDPLATLN PGKGIPLLKN CQEYRALRQI
     HSGEQL
//