ID   A3K911_9RHOB            Unreviewed;       499 AA.
AC   A3K911;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Putative glycolate oxidase subunit protein {ECO:0000313|EMBL:EBA06394.1};
GN   ORFNames=SSE37_18190 {ECO:0000313|EMBL:EBA06394.1};
OS   Sagittula stellata E-37.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sagittula.
OX   NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA06394.1, ECO:0000313|Proteomes:UP000005713};
RN   [1] {ECO:0000313|EMBL:EBA06394.1, ECO:0000313|Proteomes:UP000005713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E-37 {ECO:0000313|EMBL:EBA06394.1,
RC   ECO:0000313|Proteomes:UP000005713};
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2006) 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:EBA06394.1}.
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DR   EMBL; AAYA01000016; EBA06394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3K911; -.
DR   eggNOG; COG0277; Bacteria.
DR   Proteomes; UP000005713; 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:UP000005713}.
FT   DOMAIN          65..243
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  52684 MW;  0EFF70758590D897 CRC64;
     MVATCGRDGA DGPEGGATMQ MPEPDGAILA RKARIVERLA AVSPRGVISE PAEVRAYECD
     ALTAYRCPPL AVVLPSSTEE VSAVLKVCHE EGVPVVPRGS GTSLAGGALP TADSVILGVS
     RMNAVLETDY ENRFIRVETG RTNLSVTGAV EEEDFFYAPD PSSQLACAIA GNIAMNSGGA
     HCLKYGVTTN NLMGVTMVLM DGTVVKLGGA HLDAGGLDLL GVICGSEGQL GVVTEATLRI
     LRKPEGARPV LIGYASNEVA GACVSDIIKA GVLPVAIEFM DAPCIRATED FAKAGYPDCE
     ALLIVEVEGS EPEIAEQLAK IKEIAQRHDP VELREAKSAD EAARIWLGRK SAFGAMGNIN
     DYMCLDGTIP VTELPFVLKR IGEMSAEFGL EVANVFHAGD GNMHPLILFN ANEPGQLELC
     ERFGAEILKL CVEVGGCLTG EHGVGIEKRD LMTHQYAPED LEAQMAVKDV FDPKWLLNPA
     KVFPLAASDG RRAVALAAE
//