ID   B8J2X1_DESDA            Unreviewed;       461 AA.
AC   B8J2X1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ACL49890.1};
GN   OrderedLocusNames=Ddes_1994 {ECO:0000313|EMBL:ACL49890.1};
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL49890.1};
RN   [1] {ECO:0000313|EMBL:ACL49890.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL49890.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001358; ACL49890.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8J2X1; -.
DR   STRING; 525146.Ddes_1994; -.
DR   KEGG; dds:Ddes_1994; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_9_2_7; -.
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:SF2; 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;
FT   DOMAIN          37..217
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   461 AA;  49522 MW;  EBD18771A91A8332 CRC64;
     MASQALIRDF EDLIGKENVF SSEADRQSYS YDSAVLTPVV PALVLRPTTA EQLGACVKKL
     YDNGLPMTVR GAGTNLSGGT IPDNSDSVVI LTTGLNRILE INSDDLYAVV EPGVITAQFA
     AEVAKKNLFY PPDPGSQAVS TIGGNIAENA GGLRGLKYGV TKDYLMGIEF FDATGEMVKS
     GSRTVKCVTG YNLAGMMVQS EGTLGIISQA ILKLVPPPKA SKALMAVFEN VQDAAEAVAG
     IIAAHVVPCT LEFLDNNTIV RVDDFTKAGL PREAGAILLI EVDGHPAQVA DDAEAVERVL
     KANRATAVHV PKDADEKFKL WEARRMALPV LARCRPTTVL EDATVPRSQI PAMMKAVNEI
     AAKYKVEVGT FGHAGDGNLH PTFLCDKRDK DEFHRVEEAI DEMFDVALKL HGTLSGEHGI
     GTAKAKWMEK ETSRGTILFS QRLRRALDPK GLFNATKLVG I
//