ID X7EG91_9RHOB Unreviewed; 597 AA.
AC X7EG91;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
GN ORFNames=OCH239_19115 {ECO:0000313|EMBL:ETX14912.1};
OS Roseivivax halodurans JCM 10272.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449350 {ECO:0000313|EMBL:ETX14912.1, ECO:0000313|Proteomes:UP000022447};
RN [1] {ECO:0000313|EMBL:ETX14912.1, ECO:0000313|Proteomes:UP000022447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10272 {ECO:0000313|EMBL:ETX14912.1,
RC ECO:0000313|Proteomes:UP000022447};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax halodurans JCM 10272 Genome Sequencing.";
RL Submitted (JAN-2014) 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|RuleBase:RU003692};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003692};
CC Note=Binds 1 FAD per subunit. {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 -!- 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:ETX14912.1}.
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DR EMBL; JALZ01000007; ETX14912.1; -; Genomic_DNA.
DR RefSeq; WP_037260987.1; NZ_JALZ01000007.1.
DR AlphaFoldDB; X7EG91; -.
DR STRING; 1449350.OCH239_19115; -.
DR PATRIC; fig|1449350.3.peg.1727; -.
DR eggNOG; COG1249; Bacteria.
DR OrthoDB; 9776382at2; -.
DR Proteomes; UP000022447; 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 CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01350; lipoamide_DH; 1.
DR PANTHER; PTHR22912:SF160; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 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:RU003692};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003692}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003692};
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:UP000022447}.
FT DOMAIN 1..74
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 35..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 62953 MW; 13BD7B64A0ACBFCA CRC64;
MDIKVPDIGD FSGVPVITVL VSVGDTVEKE DPLIELESDK ATMEVPSSHA GKVTEIKVKE
GDKVSEGDVI ITLEAADDAG AEDEKADEPK GQGGEQGGGY GDRGSDQKQD APKSVQPAGG
DQGKGDVHGE VVVLGSGPGG YSAAFRAADL GKKVVLIERY PSLGGVCLNV GCIPSKALLH
VSKVITEAEE MGSHGVSFGK PKIDLKELRE FKDGVVGKLT GGLDGLAKQR KVEVVRGLGK
FTGPNMIAVE GDEGTTKVSF DQCIIAAGSE PVELPFIPHD DPRVVDSTGA LELEDIPKRM
LVLGGGIIGL EMACVYDALG SKITVVELMD QIIPGADKDL VKPLMQRIKG RYENIFLKTK
VTGMEAQKKG LKVTFEDEKG ESFTDTFDKV LVAVGRKPNG KLIDAENAGV AVDERGFIAV
DEFQRTGQSH IFAIGDVVGQ PMLAHKAVHE GKVAAEVAAG ENRAFDARVI PSVAYTDPEV
AWCGLTETQA KEKGIKVEKG VFPWAASGRS LSNGRSEGMT KLLFDPEDQR VIGAAIVGTA
AGDLISEAAL AIEMGADAID LGHTIHPHPT LSETVNFAAE MFEGTITDLM PPKKKKG
//
