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Database: UniProt
Entry: A0A101WL78_9FIRM
LinkDB: A0A101WL78_9FIRM
Original site: A0A101WL78_9FIRM 
ID   A0A101WL78_9FIRM        Unreviewed;       314 AA.
AC   A0A101WL78;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KUO75090.1};
DE   Flags: Fragment;
GN   ORFNames=APF81_02500 {ECO:0000313|EMBL:KUO75090.1};
OS   Desulfosporosinus sp. BRH_c37.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO75090.1, ECO:0000313|Proteomes:UP000053148};
RN   [1] {ECO:0000313|EMBL:KUO75090.1, ECO:0000313|Proteomes:UP000053148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO75090.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-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:KUO75090.1}.
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DR   EMBL; LOEW01000164; KUO75090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101WL78; -.
DR   Proteomes; UP000053148; 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   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   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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}.
FT   DOMAIN          1..88
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KUO75090.1"
SQ   SEQUENCE   314 AA;  33577 MW;  1DB0A05246447816 CRC64;
     FPPEPYEVET SSVGGCFAIG DSDSKSFEYG PTRTFLLGFE MVLPTGEILD IGNKCIKNVS
     GLDFIHFAVG SQGTFGIFTK LLVKLLPAPE AKKAVLGTFA SLHKANATFN TLIKRNVLST
     RMNLINASLA KKAKPGTEGQ LVIIDLQGFK ESGKNIANEV AAVLTLGGGS DVKIIEDEVE
     YDQVINGWLK VRADLNAKPE QTVEFAVGPM KMPQALAQLE ALTGDLGAYP GVIVEGLLGY
     VCLALPEGTD KLALATKVNK LAMSLGGNVR GLLGHKLKAE AYNDAEMWNE TTSLLSELRH
     RFDPKGILNP GVSL
//
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