ID R7Q7D2_CHOCR Unreviewed; 495 AA.
AC R7Q7D2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN ORFNames=CHC_T00010287001 {ECO:0000313|EMBL:CDF33929.1};
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF33929.1, ECO:0000313|Proteomes:UP000012073};
RN [1] {ECO:0000313|Proteomes:UP000012073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT "Genome structure and metabolic features in the red seaweed Chondrus
RT crispus shed light on evolution of the Archaeplastida.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
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|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 -!- 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 EMBL; HG001662; CDF33929.1; -; Genomic_DNA.
DR RefSeq; XP_005713748.1; XM_005713691.1.
DR AlphaFoldDB; R7Q7D2; -.
DR STRING; 2769.R7Q7D2; -.
DR EnsemblPlants; CDF33929; CDF33929; CHC_T00010287001.
DR GeneID; 17321461; -.
DR Gramene; CDF33929; CDF33929; CHC_T00010287001.
DR KEGG; ccp:CHC_T00010287001; -.
DR OMA; CAQLGMK; -.
DR OrthoDB; 5473641at2759; -.
DR PhylomeDB; R7Q7D2; -.
DR Proteomes; UP000012073; Unassembled WGS sequence.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; 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: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 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
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:UP000012073}.
FT DOMAIN 27..352
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 372..485
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 474
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 138
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 167..169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 204..211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 337
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 343..346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 64..69
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 495 AA; 52326 MW; 526FCA7AAD7794AA CRC64;
MALLFRARSG DMRALLRRSF ASAAPQDLVI IGGGPGGYAA AIKAAQLGLK VTCVEKRGAL
GGTCLNVGCI PSKALLHSSH LFEEAKNSFG KHGIDINGGV DINLPAMMKH KMDSVNGLTK
GIEGLFKKNK VTYVRGAGKL GGPGEVAVEL IDGGQDKIQA KNIMIATGSE VAKLPPVPVD
EEVIVSSTGA LKLDKVPEKM IVIGGGVIGL EMGSVWRRLG SQVTVVEFLD RIVPGVDKEI
ADSFFRILKK QKMKFKLGTK VVASRKEGGK VLLDIEASKG GKADTLEADV VLVATGRRPF
THGLGLEEAG VKMDKMGRID VDDSFRTSVP NVYAIGDVIK GPMLAHKAED EGLICAEIIA
GVGTGHLDYN CVPGVIYTHP EVATVGKTEE ELKEDGVEYS KGTFPFMANS RARTNDVGGD
FAQGMVKVLA DKKTDKLLGM HIVGPNAGEL IAEGVLAIEY GASTEDIART CHAHPTLSEA
TREAAMATHG KPIHF
//
