UniProt: M0CER7

Database: UniProt
Entry: M0CER7_9EURY

LinkDB:  M0CER7_9EURY 
Original site:  M0CER7_9EURY

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   M0CER7_9EURY            Unreviewed;       479 AA.
AC   M0CER7;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:ELZ21133.1};
DE            EC=1.8.1.4 {ECO:0000313|EMBL:ELZ21133.1};
GN   ORFNames=C475_19283 {ECO:0000313|EMBL:ELZ21133.1};
OS   Halosimplex carlsbadense 2-9-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halosimplex.
OX   NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ21133.1, ECO:0000313|Proteomes:UP000011626};
RN   [1] {ECO:0000313|EMBL:ELZ21133.1, ECO:0000313|Proteomes:UP000011626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ21133.1,
RC   ECO:0000313|Proteomes:UP000011626};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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:ELZ21133.1}.
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DR   EMBL; AOIU01000043; ELZ21133.1; -; Genomic_DNA.
DR   RefSeq; WP_006885521.1; NZ_AOIU01000043.1.
DR   AlphaFoldDB; M0CER7; -.
DR   STRING; 797114.C475_19283; -.
DR   PATRIC; fig|797114.5.peg.3904; -.
DR   eggNOG; arCOG01068; Archaea.
DR   OrthoDB; 27922at2157; -.
DR   Proteomes; UP000011626; Unassembled WGS sequence.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR   PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 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   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011626}.
FT   DOMAIN          5..332
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          355..462
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   479 AA;  51242 MW;  3C0D973B352AAD0B CRC64;
     MEEFDFLVIG SGSGLDVASV AASQGQSVAV VEKGPLGGTC LNRGCIPSKH LLYHADVMET
     VEHADEFEIE ATVDDVDFAA IVRNVNEDVQ EDSESIRRGL ESSSQHALFD GEARFVDERT
     VEVSDGDDDG ARLRAETVLI AAGTRPGIPN VDGIDDVAYL TSTEALQLET PPDRLVIVGG
     GYIAAELGHF FDTFGSDVTV VGRRPNLLPE ADEEVAEAFT ERYADRFTVH TGHAATGVSE
     DDGEITVEAR PYEYGDEPGV VDDGESVTVT GDELLVAAGR VPNTDTLNLD ATSVETDDRG
     FVATDEYLRT DADGVWALGD IVGEYLLKHS ANHEAKAVAR NIFGSELEPV DYSAMPFAVF
     ASPEVAGVGA LEQDLREAGR DYATNTYRYE ETARGDAMKA DGFVKVLVDL DGGILGCHIV
     GPDASTLIQE VVVAMKAGSG TVRDIRESVH IHPALPEVVQ RAFSGQFSRG GNGHDHHHH
//

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