UniProt: A0A346PV71

Database: UniProt
Entry: A0A346PV71_9EURY

LinkDB:  A0A346PV71_9EURY 
Original site:  A0A346PV71_9EURY

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
All databases (16)   

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ID   A0A346PV71_9EURY        Unreviewed;       503 AA.
AC   A0A346PV71;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=AArcMg_3442 {ECO:0000313|EMBL:AXR83416.1};
OS   Natrarchaeobaculum sulfurireducens.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrarchaeobaculum.
OX   NCBI_TaxID=2044521 {ECO:0000313|EMBL:AXR83416.1, ECO:0000313|Proteomes:UP000258613};
RN   [1] {ECO:0000313|Proteomes:UP000258613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AArc-Mg {ECO:0000313|Proteomes:UP000258613};
RA   Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA   Golyshin P.N., Rojo D., Ciordia S., Mena M.D.C., Ferrer M., Messina E.,
RA   Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT   "Phenotypic and genomic properties of facultatively anaerobic sulfur-
RT   reducing natronoarchaea from hypersaline soda lakes.";
RL   Submitted (FEB-2018) 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=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003692};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; CP027033; AXR83416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A346PV71; -.
DR   KEGG; nag:AArcMg_3442; -.
DR   Proteomes; UP000258613; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003692}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
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:UP000258613}.
FT   DOMAIN          36..362
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          381..490
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   503 AA;  52930 MW;  32E22AB221122CAB CRC64;
     MTVSGDTTDD IYATKRDRIE RRTRLMVVGD VTTGTDVVVI GAGPGGYVAA IRAGQLDLDV
     TLVEKAAYGG TCLNHGCIPS KALITATDVA HEARHAEEMG IHADPAIDMA GMVGWKDGVV
     DQLTSGVEKL CKANQVNLLE GTATFAGENT VRISHSGEGQ GSETLEFEHA IIATGSRPIE
     IPNFSFDDEP VLNSRQALAL ESIPDSLVIV GAGYIGMELA TVFAKLGTDV TVVEMLESIL
     PGYDDDLKRP VKQRANDLGI DFEFGYTAAK WHEHGDGIRV VAEPADRTEA DESLDLDAET
     VLVAVGREPV SDTLDLEAVG VETDERGFIK TDSRARTNVD HVFAVGDVAG EPMLAHKGSA
     EGQVAAEVIA GEPAALDHQA IPAVVFTDPE IATVGMTERE AEDAGFETAV GQFPFRASGR
     ALTTGDTDGF VKIVADEDEG YVLGASIVGP EASELIAELG LAVELGATLE DVASTIHAHP
     TLAESVMEAA ENALGHAIHT LNR
//

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