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Database: UniProt
Entry: A0A1F3A5L7_9PROT
LinkDB: A0A1F3A5L7_9PROT
Original site: A0A1F3A5L7_9PROT 
ID   A0A1F3A5L7_9PROT        Unreviewed;       376 AA.
AC   A0A1F3A5L7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:OFX01281.1};
GN   ORFNames=A3D94_15585 {ECO:0000313|EMBL:OFX01281.1};
OS   Alphaproteobacteria bacterium RIFCSPHIGHO2_12_FULL_66_14.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1797225 {ECO:0000313|EMBL:OFX01281.1, ECO:0000313|Proteomes:UP000176194};
RN   [1] {ECO:0000313|EMBL:OFX01281.1, ECO:0000313|Proteomes:UP000176194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the L2HGDH family.
CC       {ECO:0000256|ARBA:ARBA00037941}.
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:OFX01281.1}.
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DR   EMBL; MEMN01000121; OFX01281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3A5L7; -.
DR   STRING; 1797225.A3D94_15585; -.
DR   Proteomes; UP000176194; Unassembled WGS sequence.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43104:SF4; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          14..371
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   376 AA;  39684 MW;  58C7D7450F4E9E7E CRC64;
     MSSSPFETPP ESVDCVVIGA GVVGLAIARA LALAGREVIV VEAAEGIGTE TSSRNSEVIH
     AGIYYPKDSL MARTCVEGRH LLYAYCAEHG VPHLNCGKLI VATNEAESEK LTEIKGRAEA
     NGVEGMRLLS AAEARTMEPS LHCTAALLSP RTGIVDSHSY MLALQGDAES RGAMFAFHSP
     VKQGRVVEGG VEIEVGGTEP MNLRCRLVVN SAGLHAPGLA QKIAGLPSDR IPPAYYAKGN
     YFTLAGRSPF SRLIYPVPVP GGLGVHITVD LGGQAKFGPD VEWIDGIDYT VDPHRADKFY
     AAVRRYWPDL KDGALQPGYA GIRPKIVPQG APAQDFTIQG PGEHGVAGLI NLFGIESPGL
     TASLALAERV RDIAAA
//
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