ID H2ZYB7_LATCH Unreviewed; 236 AA.
AC H2ZYB7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00012608};
DE EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608};
GN Name=LOC102358749 {ECO:0000313|Ensembl:ENSLACP00000002388.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000002388.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000002388.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) +
CC N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00043836};
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DR EMBL; AFYH01264298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2ZYB7; -.
DR STRING; 7897.ENSLACP00000002388; -.
DR Ensembl; ENSLACT00000002408.1; ENSLACP00000002388.1; ENSLACG00000002134.1.
DR eggNOG; KOG1335; Eukaryota.
DR GeneTree; ENSGT00550000074844; -.
DR HOGENOM; CLU_016755_3_2_1; -.
DR InParanoid; H2ZYB7; -.
DR OMA; IPRRACQ; -.
DR TreeFam; TF300414; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000002134; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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 PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 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.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 2..142
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 161..230
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 236 AA; 25515 MW; 1EE10B1DB8C72830 CRC64;
GSVWQRLGSE VTAVEFLGHV GGIGIDMEIS KNFQRILQKQ GLKFKLNTKV TGATRRSDGK
VDVAIEAAAG GKADVLTCDV LLVCVGRRPF TKDLGLQELG LELDSRGRIP VDNRFQTKIP
NVYAIGDVIA GPMLAHKAED EGIICVEGMA GGAVHIDYNC VPSVIYTHPE VAWVGKSEEQ
LKEENIPYKI GKFPFAANSR AKTNADTDGM VKIISHKETD RMLGAHILGS CGAWEL
//
