ID   A0A0C1UDJ8_9ACTN        Unreviewed;       488 AA.
AC   A0A0C1UDJ8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=MB54_03540 {ECO:0000313|EMBL:KIE49838.1};
OS   marine actinobacterium MedAcidi-G2B.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1550401 {ECO:0000313|EMBL:KIE49838.1, ECO:0000313|Proteomes:UP000031352};
RN   [1] {ECO:0000313|EMBL:KIE49838.1, ECO:0000313|Proteomes:UP000031352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT   "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL   Submitted (SEP-2014) 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:KIE49838.1}.
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DR   EMBL; JUEO01000004; KIE49838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1UDJ8; -.
DR   STRING; 1550401.MB54_03540; -.
DR   Proteomes; UP000031352; 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;
FT   DOMAIN          46..225
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   488 AA;  52300 MW;  2E37278D9A46614D CRC64;
     MNFFKNINRS KQSDQLFREL CRDIGTARVH RDGASQLLYS RDGSAFPGGI PGVVCFPETT
     QHVIDCIKAA NRHDRSFVPR GAGTGLAGGA VPCDAPLVIS TTKMNSIFEV NYEKRFAWVG
     PGVVNLDLTK SLSGTGFHFA PDPSSQQSCT IGGNVANNSG GPHCLAYGVT NAHILAIEVV
     LPDGTLVQLG DVDGHASGYD LRGVFVGGEG TLGIATRIAV KLTPDPPEIC TLLLDFMDVA
     DAAKTVSAII ASGIVPAAIE MMDKRIVNVV EEFVKVGYPT DAAAVLIIEV DGLPEGVRIE
     VERIQSISLE YGARSVRVAS SDAEREQIWK GRKSAFGAVA QIQPGYYLHD TVIPRTKLVE
     VLEAVYEIAN RYELIVMNVF HAGDGNLHPL LVFDPQEPGI MERVLAAGEE IVQVSLDAGG
     VLSGEHGIGL EKIRFMENLF SEEDLAAQKL LKDAFDPDGR ANPFKVLPSG ASCSEVNHLN
     QLPDGAWV
//