ID   K8GNJ7_9CYAN            Unreviewed;       405 AA.
AC   K8GNJ7;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Putative dehydrogenase {ECO:0000313|EMBL:EKQ70562.1};
GN   ORFNames=OsccyDRAFT_0858 {ECO:0000313|EMBL:EKQ70562.1};
OS   Leptolyngbyaceae cyanobacterium JSC-12.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX   NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ70562.1, ECO:0000313|Proteomes:UP000001332};
RN   [1] {ECO:0000313|EMBL:EKQ70562.1, ECO:0000313|Proteomes:UP000001332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ70562.1,
RC   ECO:0000313|Proteomes:UP000001332};
RG   DOE Joint Genome Institute;
RA   Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT   "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL   Submitted (OCT-2012) 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:EKQ70562.1}.
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DR   EMBL; AJUB01000005; EKQ70562.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8GNJ7; -.
DR   STRING; 864702.OsccyDRAFT_0858; -.
DR   PATRIC; fig|864702.5.peg.900; -.
DR   eggNOG; COG0579; Bacteria.
DR   HOGENOM; CLU_024775_0_1_3; -.
DR   Proteomes; UP000001332; 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:UP000001332}.
FT   DOMAIN          4..391
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   405 AA;  44836 MW;  C7DE2A38786526E0 CRC64;
     MMYDFAIIGG GIVGLSTGMA LGQCYPNARI LVLEKESQWA FHQTGNNSGV IHSGIYYKPG
     SFKAKFCRDG CRSMVEFCQK HHLPYEVCGK VIVATEEREL PLLENLYQRG LQNGIEVARI
     TAEEVKEVEP YVSCLAGIRV FSTGITDYKQ VANKYAELIQ LQGGDLRLNT QVLKIVKTPQ
     AMVLETSQGS FETQFVINCA GLYSDRVARL GGIDPHAKIV PFRGEYYELV PEKRYLVNTL
     IYPVPNPAFP FLGVHFTKMI DGSVHAGPNA VLSLKREGYH KTDFDFRDFL EVMTYPAFWK
     LASKYADEGI KEMIRSLSKA VFVRSLQRLI PDVRMEDVIP THAGVRAQAL MDNGSLVDDF
     LILNGDRSIH VCNAPSPAAT SSIEIGRAIA AQVPAPTTHP IAISA
//