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Database: UniProt
Entry: W0JSQ5_9EURY
LinkDB: W0JSQ5_9EURY
Original site: W0JSQ5_9EURY 
ID   W0JSQ5_9EURY            Unreviewed;       463 AA.
AC   W0JSQ5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:AHG00302.1};
GN   ORFNames=HALLA_17340 {ECO:0000313|EMBL:AHG00302.1};
OS   Halostagnicola larsenii XH-48.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halostagnicola.
OX   NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG00302.1, ECO:0000313|Proteomes:UP000019024};
RN   [1] {ECO:0000313|EMBL:AHG00302.1, ECO:0000313|Proteomes:UP000019024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH-48 {ECO:0000313|EMBL:AHG00302.1,
RC   ECO:0000313|Proteomes:UP000019024};
RG   DOE Joint Genome Institute;
RA   Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JAN-2014) 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; CP007055; AHG00302.1; -; Genomic_DNA.
DR   RefSeq; WP_049953542.1; NZ_CP007055.1.
DR   AlphaFoldDB; W0JSQ5; -.
DR   STRING; 797299.HALLA_17340; -.
DR   GeneID; 25146169; -.
DR   KEGG; hlr:HALLA_17340; -.
DR   PATRIC; fig|797299.3.peg.2472; -.
DR   eggNOG; arCOG00754; Archaea.
DR   HOGENOM; CLU_613842_0_0_2; -.
DR   OrthoDB; 227302at2157; -.
DR   Proteomes; UP000019024; Chromosome.
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:SF2; 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;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019024}.
FT   DOMAIN          6..377
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          441..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  50840 MW;  4241F4C978EF6FBF CRC64;
     MSGKYDLVIV GGGISGASLL YTTAKFTDIE SIALIEKESE IAAINSHVTN NSQTLHFGDI
     ETNYTLEKAE DVKEGAELLA GYLENHDPDR EMHSKRSKMV LGVGDEEVAQ LEQRYEDEGF
     GELFPKLRAI DREEIAEIEP KVVEGRDPST EMLALQTPDG YVVDYGEATK SFVEQAEKEA
     NVDVYTGTEV EDITETLDGY TIGTTNGRFD CEATVVAAGS HSLQIAKELG YGQDKVLLPI
     AGSFFLADDF LNGKVYTLQM KKLPFAAVHG DADVHDDSIT RFGPTAKLVP TLERGRISTV
     KDFLDVFGLN AAAFLSYANI LSDRILLPYV LRNLVYDLPE VGPRQFLPHV QKVVPSAELE
     DIERAKGYGG VRPQIVDTKN KSLDMGEAKI VGDDIIFNIT PSPGASTCLK NAVQDTERVL
     EFLEGDYEFD EAALREATID NFPRIDDETE DTQTVASPAT DDD
//
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