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Database: UniProt
Entry: A0A2A5WFZ4_9GAMM
LinkDB: A0A2A5WFZ4_9GAMM
Original site: A0A2A5WFZ4_9GAMM 
ID   A0A2A5WFZ4_9GAMM        Unreviewed;       381 AA.
AC   A0A2A5WFZ4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:PDH35188.1};
GN   ORFNames=CNF02_00215 {ECO:0000313|EMBL:PDH35188.1};
OS   OM182 bacterium MED-G28.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; OMG group; OM182 clade.
OX   NCBI_TaxID=1986256 {ECO:0000313|EMBL:PDH35188.1, ECO:0000313|Proteomes:UP000219329};
RN   [1] {ECO:0000313|EMBL:PDH35188.1, ECO:0000313|Proteomes:UP000219329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED-G28 {ECO:0000313|EMBL:PDH35188.1};
RA   Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA   Rodriguez-Valera F.;
RT   "Fine stratification of microbial communities through a metagenomic profile
RT   of the photic zone.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PDH35188.1}.
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DR   EMBL; NTJZ01000001; PDH35188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5WFZ4; -.
DR   Proteomes; UP000219329; 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          5..373
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   381 AA;  42008 MW;  F078459B6AE2828D CRC64;
     MDKFDVCIAG AGVVGLAIAY QLSKSARYAN ASIVLLEREP SFGQITSSRN SEVIHAGIYY
     ATDSLKANLC VAGKKLLYDH LQKFELPHRK LGKLIVAQKT EEEALEAVKE KAHENGVTDL
     CWIDTHQLRK LEPEVRGHAA LLSPSTGIID SHSYMQNLLN LAESQGVIFA SRSEVIAVHQ
     EPKSFLINTV LTHTHGLEPY DFHCTEFINC AGLNAQELAL KTEGMNPKYV PRLHLCKGDY
     FSYSGGSPFS HLIYPMPEAN HIGLGIHSTI DIAGQLRFGP DTEFVDNQSY TIDAGKSNRF
     VNSIKRYFPT VDPAKLHPSY AGIRPKIVGP EDDAGDFQIQ DSSIHGIKGL VQLFGMESPA
     LTASLAIGEY VIDQMNREAR R
//
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