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Database: UniProt
Entry: K9X3W3_9NOST
LinkDB: K9X3W3_9NOST
Original site: K9X3W3_9NOST 
ID   K9X3W3_9NOST            Unreviewed;       404 AA.
AC   K9X3W3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Putative dehydrogenase {ECO:0000313|EMBL:AFZ26751.1};
GN   ORFNames=Cylst_4686 {ECO:0000313|EMBL:AFZ26751.1};
OS   Cylindrospermum stagnale PCC 7417.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Cylindrospermum.
OX   NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ26751.1, ECO:0000313|Proteomes:UP000010475};
RN   [1] {ECO:0000313|EMBL:AFZ26751.1, ECO:0000313|Proteomes:UP000010475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ26751.1,
RC   ECO:0000313|Proteomes:UP000010475};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL   Submitted (JUN-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}.
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DR   EMBL; CP003642; AFZ26751.1; -; Genomic_DNA.
DR   RefSeq; WP_015209988.1; NC_019757.1.
DR   AlphaFoldDB; K9X3W3; -.
DR   STRING; 56107.Cylst_4686; -.
DR   KEGG; csg:Cylst_4686; -.
DR   PATRIC; fig|56107.3.peg.5151; -.
DR   eggNOG; COG0579; Bacteria.
DR   HOGENOM; CLU_024775_0_1_3; -.
DR   OrthoDB; 9801699at2; -.
DR   Proteomes; UP000010475; 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:UP000010475}.
FT   DOMAIN          3..389
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   404 AA;  44543 MW;  56383369E0455264 CRC64;
     MYDFAIIGGG IVGLSTGMAL GKNYPHARIL VLEKESQWAF HQTGNNSGVI HSGIYYKPGS
     FKAKFCRDGS RSMVEFCQEH EIEHEVCGKV IVATEESELP RLESLYKRGL DNGIEVQRIS
     PEAVKEIEPH VRCVGGIRVF STGIVNYKQV CQKYAELIQQ QGGELRLNTK VSKISASGEN
     QVLETSNGSF ETRFVINCAG LHSDRIAKLA QLTPLAKIIP FRGEYYELIP EKRHLVKTLI
     YPVPNPDFPF LGVHFTRMID SSVHAGPNAV LSLKREGYKK TDFDLRDFAE VITYPGFWKL
     AAKHADEGIQ EIIRSFSKAA FVRSLQKLIP EVQAADLIPT HAGVRAQALM NNGSLVDDFL
     IVQGQNSIHV CNAPSPAATS SVEIGKAIVA QIPQQAQLLT AINA
//
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