ID K9YCC6_HALP7 Unreviewed; 404 AA.
AC K9YCC6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:AFZ44055.1};
GN OrderedLocusNames=PCC7418_1887 {ECO:0000313|EMBL:AFZ44055.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ44055.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003945; AFZ44055.1; -; Genomic_DNA.
DR AlphaFoldDB; K9YCC6; -.
DR STRING; 65093.PCC7418_1887; -.
DR KEGG; hao:PCC7418_1887; -.
DR PATRIC; fig|65093.3.peg.2000; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_024775_0_1_3; -.
DR Proteomes; UP000010481; 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:UP000010481}.
FT DOMAIN 6..392
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 404 AA; 44992 MW; 096D92E2854D3987 CRC64;
MIYDQVIIGG GIVGLATAMQ LAQKSPKARI LLLEKETDLA AHQTSHNSGV IHSGIYYKPG
SFKAKFCRDG SRSMVEFCQE HNLDYEVCGK VIIATQEQEL PRLERLYQRG LENGISVKKL
RGEAIQELEP HVRCLAGIRV NSTGITDYKK VCQKYAQILR DRAGELKFNT QVTQLQKTAD
GYVIETNQGD FQAKFIINCA GLHSDRVAKL GAVNPQAKII PFRGEYYELK PEKRYLVKNL
IYPVPNPNFP FLGVHFTRMI DGSVHAGPNA VLSFKREGYQ KTDWDRRDLI ESLTYPGLWK
LAAKYGAIGV AEMIRSWSKT AFVRSLQRLI PEIQPEDVIP ISAGVRAQAL KQNGALVDDF
LMIEGRKALH ICNAPSPAAT ASLEIGKAIA DRVLAMEMTV QTCS
//
