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Database: UniProt
Entry: Q07J73_RHOP5
LinkDB: Q07J73_RHOP5
Original site: Q07J73_RHOP5 
ID   Q07J73_RHOP5            Unreviewed;       368 AA.
AC   Q07J73;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ABJ08011.1};
GN   OrderedLocusNames=RPE_4085 {ECO:0000313|EMBL:ABJ08011.1};
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ08011.1};
RN   [1] {ECO:0000313|EMBL:ABJ08011.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53 {ECO:0000313|EMBL:ABJ08011.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) 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}.
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DR   EMBL; CP000463; ABJ08011.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07J73; -.
DR   STRING; 316055.RPE_4085; -.
DR   KEGG; rpe:RPE_4085; -.
DR   eggNOG; COG0579; Bacteria.
DR   HOGENOM; CLU_024775_1_1_5; -.
DR   OrthoDB; 9801699at2; -.
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          6..363
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   368 AA;  38703 MW;  277CC38C055A945E CRC64;
     MDQVECVVVG AGVVGLAIAR RLAQFGREVV ILEAADTIGT VTSSRNSEVI HAGIYYPAHS
     LMARLCVGGR RQLYDYCHDH GVLHRRCGKL IVATSAAETD KLASIRAHAE ANGVDDLQSL
     SGEAARALEP ALACAAALLS PSTGIIDSHA LMLALRGDAE EAGAAFAFHA PLLRARVVAG
     GFELDVGGAE PMTLGCRLLI NAAGLDAPAL ARTIDAMPAD SIPTAYYAKG NYFSCGARAP
     FSRLIYPVPE PGGLGVHLTL DLAGQARFGP DVEWIEAIDY QVDPARAERF YPAIRRYWPA
     LPDGALMPGY AGIRPKIVPK TIAVQDFAIQ GPQQHGVEGL INLFGIESPG LTACLAIADF
     VGDLASQA
//
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