ID K9Z564_CYAAP Unreviewed; 395 AA.
AC K9Z564;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:AFZ54321.1};
GN OrderedLocusNames=Cyan10605_2235 {ECO:0000313|EMBL:AFZ54321.1};
OS Cyanobacterium aponinum (strain PCC 10605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ54321.1, ECO:0000313|Proteomes:UP000010480};
RN [1] {ECO:0000313|Proteomes:UP000010480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003947; AFZ54321.1; -; Genomic_DNA.
DR RefSeq; WP_015220046.1; NC_019776.1.
DR AlphaFoldDB; K9Z564; -.
DR STRING; 755178.Cyan10605_2235; -.
DR KEGG; can:Cyan10605_2235; -.
DR PATRIC; fig|755178.3.peg.2376; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_024775_0_1_3; -.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000010480; 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:UP000010480}.
FT DOMAIN 4..390
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 395 AA; 43970 MW; 040315988625BDB2 CRC64;
MTYDIAIIGG GIVGLATAMN LQQKYPQKKI ILVEKENHCA THQTGHNSGV IHSGVYYQPG
SYKAKLTTQG NRALVEFCQT HNIKYDVCGK LIVACKEKEL SQLENLYQRG LQNGIAVTKI
SREEAKEIEP YVNCIQAIKV PTAGIVDYKE VAKKYAEIFC NIGGEIRLNT KVVNLKYQDS
QHIIITNQGE ITSKYLVNCA GLYSDKIAIL GGINPKMKII PFRGEYYELK PEKRYLVKHL
IYPVPNPDFP FLGVHFTRLI DGNIHAGPNA VLSLKREGYK KTDFALGEFW ETVTYSGLWK
LVSKYYEEGI EEIIRSFSKT AFVRSLQTLI PEVQEDDIIP SPAGVRAQAL NQDGTLVQDF
ALLPTENALH VCNAPSPAAT ASLKIGEVIS QNVAF
//
