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Database: UniProt
Entry: A0A388KDW9_CHABU
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ID   A0A388KDW9_CHABU        Unreviewed;       650 AA.
AC   A0A388KDW9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CBR_g2805 {ECO:0000313|EMBL:GBG68254.1};
OS   Chara braunii (Braun's stonewort).
OC   Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC   Chara.
OX   NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG68254.1, ECO:0000313|Proteomes:UP000265515};
RN   [1] {ECO:0000313|EMBL:GBG68254.1, ECO:0000313|Proteomes:UP000265515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S276 {ECO:0000313|EMBL:GBG68254.1,
RC   ECO:0000313|Proteomes:UP000265515};
RX   PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA   Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA   Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA   Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA   Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA   Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA   Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA   Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA   Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA   Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA   Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA   Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA   Rensing S.A.;
RT   "The Chara Genome: Secondary Complexity and Implications for Plant
RT   Terrestrialization.";
RL   Cell 174:448-464(2018).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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:GBG68254.1}.
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DR   EMBL; BFEA01000098; GBG68254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A388KDW9; -.
DR   STRING; 69332.A0A388KDW9; -.
DR   EnsemblPlants; GBG68254; GBG68254; CBR_g2805.
DR   Gramene; GBG68254; GBG68254; CBR_g2805.
DR   OMA; WASMLND; -.
DR   Proteomes; UP000265515; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265515}.
FT   DOMAIN          164..499
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          518..629
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   650 AA;  67502 MW;  EF9C099DF90E8C70 CRC64;
     MAAGAATTVV GGVAMVGASG AAGSISFKAT SGIGGNRSPD GCALDGVKCA RASSSLAGGG
     GTLAAAAAAA FRLRSSPVIS RVNCAKCVRH RVSVGSSSSS SSCGSAFSSL RSEAFRGTPL
     CAPVEAAEEG RRCARAKGTA GGREKKSIYR LHVAAAAAGE SFDYDLVIIG AGVGGHGAAL
     HAVEQGLKTA IIEGDIVGGT CVNRGCVPSK ALLAVSGRMR ELRDEQHLKA LGIHVSGAGY
     DRQLVADHAQ NLATKIRNNL ANSMTALGVE ILTGTGSLQG PHRVKYGKVG YPDKQVTAKN
     IIIATGSVPF VPPGIEIDGK SVLTSDHALK LERVPDWVAI VGSGYIGLEF SDVYTALGSE
     VTFVEALETL MPGFDPEIGR MAQRLLINPR KIDYHTGVFA KKITPAKDGN PVVIELIDAK
     TKEDVDTLYV DAALIATGRA PYTKGLGLSN AGVETQRGFV PVDSRMRVLD KDGEVVPGLY
     CIGDANGKLM LAHAASAQGI SAVENMCGRD HEVNHLAVPA ACFTHPEISF VGLTEPQARS
     KAEEEGFAVG VAKTSFKANS KALAENEGEG MAKVIYRMDT GDILGLHIIG LHAADLIHEA
     SNAIALGQRI QDLKFAVHAH PTLSEVLDEL FKHAKLPQKE SLLEPQTVVA
//
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