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Database: UniProt
Entry: F7I3R3_CALJA
LinkDB: F7I3R3_CALJA
Original site: F7I3R3_CALJA 
ID   F7I3R3_CALJA            Unreviewed;       509 AA.
AC   F7I3R3; F7GNE6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   Name=DLD {ECO:0000313|Ensembl:ENSCJAP00000046551.3};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000046551.3, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000046551.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000046551.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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:ARBA00001492,
CC         ECO:0000256|RuleBase:RU003692};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3,
CC         ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3,
CC       ECO:0000256|RuleBase:RU003692};
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000256|ARBA:ARBA00004230}. Cytoplasmic vesicle, secretory
CC       vesicle, acrosome {ECO:0000256|ARBA:ARBA00004218}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000256|RuleBase:RU003692}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003692}.
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DR   AlphaFoldDB; F7I3R3; -.
DR   Ensembl; ENSCJAT00000054397.4; ENSCJAP00000046551.3; ENSCJAG00000016418.5.
DR   GeneTree; ENSGT00550000074844; -.
DR   HOGENOM; CLU_016755_0_1_1; -.
DR   OMA; DAKYGEW; -.
DR   OrthoDB; 5473641at2759; -.
DR   Proteomes; UP000008225; Chromosome 8.
DR   Bgee; ENSCJAG00000016418; Expressed in heart and 6 other cell types or tissues.
DR   GO; GO:1902493; C:acetyltransferase complex; IEA:Ensembl.
DR   GO; GO:0043159; C:acrosomal matrix; IEA:Ensembl.
DR   GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IEA:Ensembl.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IEA:Ensembl.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0034604; F:pyruvate dehydrogenase (NAD+) activity; IEA:Ensembl.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:Ensembl.
DR   GO; GO:0007369; P:gastrulation; IEA:Ensembl.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:Ensembl.
DR   GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR   GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
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; IPR006258; Lipoamide_DH.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   NCBIfam; TIGR01350; lipoamide_DH; 1.
DR   PANTHER; PTHR22912:SF151; 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   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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   Cell projection {ECO:0000256|ARBA:ARBA00023069};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flagellum {ECO:0000256|ARBA:ARBA00022846};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT   DOMAIN          43..370
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          389..497
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        487
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         89
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         154
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         183..185
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         220..227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         314
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         355
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         361..364
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        80..85
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   509 AA;  54122 MW;  88A7A66EDABB0C21 CRC64;
     MQSWSRVYCS LAKRGHFSRV SHGLQGPSAV PLRTYADQPI DADVTVIGSG PGGYVAAIKA
     AQLGFKTVCV EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL
     DKMMEQKSTA VKALTGGIAH LFKQNKVVHV NGYGKITGKN QVTATKADGS TQVIDTKNIL
     IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT
     AVEFLGHVGG VGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSIEAASGGK
     AEVITCDVLL VCIGRRPFTK NLGLEELGIE LDPRGRIPVN TRFQSKIPNI YAIGDVVAGP
     MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK
     FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI
     ARVCHAHPTL SEAFREANLA ASFGKSINF
//
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