UniProt: A0A1H0QJV5

Database: UniProt
Entry: A0A1H0QJV5_9RALS

LinkDB:  A0A1H0QJV5_9RALS 
Original site:  A0A1H0QJV5_9RALS

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (3)   
All databases (19)   

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ID   A0A1H0QJV5_9RALS        Unreviewed;       610 AA.
AC   A0A1H0QJV5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00016961, ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   ORFNames=SAMN04488595_105191 {ECO:0000313|EMBL:SDP17582.1};
OS   Ralstonia sp. 25mfcol4.1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=1761899 {ECO:0000313|EMBL:SDP17582.1, ECO:0000313|Proteomes:UP000199332};
RN   [1] {ECO:0000313|EMBL:SDP17582.1, ECO:0000313|Proteomes:UP000199332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=25MFCol4.1 {ECO:0000313|EMBL:SDP17582.1,
RC   ECO:0000313|Proteomes:UP000199332};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNJO01000005; SDP17582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0QJV5; -.
DR   STRING; 1761899.SAMN04488595_105191; -.
DR   OrthoDB; 178496at2; -.
DR   Proteomes; UP000199332; 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:SF224; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   610 AA;  63584 MW;  8228D4121603443D CRC64;
     MATIEVKVPQ LSESVSEATL LQWKKKPGEA VQRDEILVEL ETDKVTLEVP CPDNGVLTQI
     VKPDGATVHA DEVIAVVDTD AKATAAAPAA KPAPAPATAS ASAPAAASAT APAAAAPASV
     SAGATGGGAS PSAKADFDVI VIGSGPGGYI AAIRAAQLGK TVACIEEWKD EAGKPRLGGT
     CLNVGCIPSK ALLASSEHFE HAQHGMADHG VQIKGVSLDL AQMIRRKAAI VDKFTGGVEF
     LFRKNKVTWI KGHGKFKGRA PDGVVTVEAS DGGDTRPYTA RNVIIATGSK ARHLPGVPVD
     NKIVSDNEGA LSFDSVPKKL AVIGAGVIGL ELGSVWRRLG AEVTILEALP AFLGAVDEAI
     AREAAKLFKK QGLTIHLGVN IGEVKTKAKG GVTIAFKDQS GADQKLEADR LIVSIGRVPN
     TDNLGLDAVG LSADPRGFIP VDDNCRTSVA GIYAIGDVVR GPMLAHKAED EGVMVAEVID
     GQKPHIDYNC IPWVIYTEPE IAWVGKTEAQ LKAEGREYRT GQFPMQANGR AMGIGRPDGF
     VKMIADAKTD ELLGVHIISA NASDLIAEGV VAMEFKAASE DIGMICHPHP SLSEVMREAA
     LAVQKRALNM
//

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