ID   A0A0M2TZ98_9FIRM        Unreviewed;       459 AA.
AC   A0A0M2TZ98;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=FAD-binding protein {ECO:0000313|EMBL:KKM09112.1};
GN   ORFNames=SY88_20425 {ECO:0000313|EMBL:KKM09112.1};
OS   Clostridiales bacterium PH28_bin88.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM09112.1, ECO:0000313|Proteomes:UP000034222};
RN   [1] {ECO:0000313|EMBL:KKM09112.1, ECO:0000313|Proteomes:UP000034222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Robbins S., Tyson G.;
RT   "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL   Submitted (MAR-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:KKM09112.1}.
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DR   EMBL; LAKY01000069; KKM09112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2TZ98; -.
DR   STRING; 1605376.SY88_20425; -.
DR   PATRIC; fig|1605376.3.peg.2409; -.
DR   Proteomes; UP000034222; 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: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;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034222}.
FT   DOMAIN          38..217
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   459 AA;  49796 MW;  CD330E81BB21A408 CRC64;
     MLKHEVLKEI TLVVGKQNVF TEPEDLHCYA TDATLGVPVV LPEAVVKPAS AEEVSQILQI
     ANRELIPVVP RGAGTSLSGG AMPIQGGIVL ETTRMNKILE IDKDNLLAVV EPGVITAHLN
     QEAAKVGLFY PPDPGSVAFS TIGGNVAVGA GGLRGLKYGT TKDYVLGLEV VMPWGAIVKT
     GGRTVKNVTG YDLTKLMVGS EGTLGVITKI IVKLLPIPPA SRSMLAVFDD LNNAAETISA
     IIANRIIPAT LDIMDKNVIR AVEASSRVGL PVDAEAILLI EVDGVEQVVE QELNRIREIC
     HQHHVREMKV ARTAEEKEQV WAARRNTYGA LTKINNTDLV EDATVPRSKV PDMMRFIVDI
     AKRYNLTIAT LGHAGDGNIH PNIMFDRNDP DEVHRVEEAI KEIFETALRL GGTLSGEHGI
     GLTKRPFMRW EFGDGGIEVM SRIKKALDPN FILNPGKKF
//