ID   K8GPQ3_9CYAN            Unreviewed;       368 AA.
AC   K8GPQ3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:EKQ69709.1};
GN   ORFNames=OsccyDRAFT_2351 {ECO:0000313|EMBL:EKQ69709.1};
OS   Leptolyngbyaceae cyanobacterium JSC-12.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX   NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ69709.1, ECO:0000313|Proteomes:UP000001332};
RN   [1] {ECO:0000313|EMBL:EKQ69709.1, ECO:0000313|Proteomes:UP000001332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ69709.1,
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:EKQ69709.1}.
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DR   EMBL; AJUB01000010; EKQ69709.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8GPQ3; -.
DR   STRING; 864702.OsccyDRAFT_2351; -.
DR   PATRIC; fig|864702.5.peg.2528; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_043129_0_0_3; -.
DR   OrthoDB; 9801699at2; -.
DR   Proteomes; UP000001332; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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          7..310
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   368 AA;  41832 MW;  C81398B39DDFD097 CRC64;
     MPRTYTIAVI GGGFYGCSVA IHLAQQGADV VLFERLPDLL TRASYHNQAR LHNGYHYPRS
     FTTAYRSRLN FQRFLQEFRP AIATEFIKLY AIARVGSKVS PRQFETFCQT IEAPLRPARS
     GFVELFSPRL ISSVYETQEY AFDAAVLRRL LRERLAQAGV SLKLATPVIA VEPNHLNQVI
     VIEATGKGLE VDYVFNCTYS GLNAIAGITP SRLRLKHEIA EIALVQLPDE LRDVSVTVMD
     GPFFSFMPFP DRGLSTFSHV RYTPQSTWTE AVDDYLNPYQ AFDSFERRSH FAFMVRDAQR
     YMPCLAHMVY QDSLFEVKTV LMKNEGDDGR PILFEVDPVQ PRIISMLGSK IDNIYDALEA
     VDQYLRAV
//