ID Q07WL2_SHEFN Unreviewed; 476 AA.
AC Q07WL2;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00016961, ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
GN OrderedLocusNames=Sfri_3775 {ECO:0000313|EMBL:ABI73602.1};
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI73602.1, ECO:0000313|Proteomes:UP000000684};
RN [1] {ECO:0000313|EMBL:ABI73602.1, ECO:0000313|Proteomes:UP000000684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI73602.1,
RC ECO:0000313|Proteomes:UP000000684};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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,
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000447; ABI73602.1; -; Genomic_DNA.
DR RefSeq; WP_011639189.1; NC_008345.1.
DR AlphaFoldDB; Q07WL2; -.
DR STRING; 318167.Sfri_3775; -.
DR KEGG; sfr:Sfri_3775; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_1_6; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000000684; Chromosome.
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:SF160; DIHYDROLIPOYL DEHYDROGENASE; 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}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
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:UP000000684}.
FT DOMAIN 8..329
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 348..456
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 446
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 183..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 320..323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 45..50
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 476 AA; 50663 MW; 163C5B4C6582B29E CRC64;
MSNEIKTQVV VLGAGPAGYS AAFRAADLGL DTIIVERFST LGGVCLNVGC IPSKALLHVA
KVIEEAKAVA DHGVVFGEPK IDLDKLRGFK NKVISQLTGG LGGMSKMRKV NVVNGFGKFT
GPNSLEVTAE DGTVTVVQFE QAIIAAGSRP IKLPFIPHED PRIWDSTDAL ELKEVPGKLL
VMGGGIIGLE MGTVYSSLGS EIDVVEMFDQ VIPAADKDVV RVFTKQIKKK FNLILETKVT
AVEAKDDGIY VTMEGKKAPA EPVRYDAVLV AIGRSPNGKS LAAEKAGVNV DERGFINVDK
QLRTNVPHIY AIGDIVGQPM LAHKGVHEGH VAAEVIAGMK HYFDPKVIPS IAYTDPEVAW
VGLTEKEAKE QGVAYETATF PWAASGRAIA SDCSEGMTKL IFDKETHRII GGAIVGVNGG
ELLGEIGLAI EMGCDAEDLA LTIHAHPTLY ESIGLAAEMY EGSITDLPNP KAVKKK
//
