ID M0CCW4_9EURY Unreviewed; 455 AA.
AC M0CCW4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:ELZ21111.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:ELZ21111.1};
GN ORFNames=C475_19173 {ECO:0000313|EMBL:ELZ21111.1};
OS Halosimplex carlsbadense 2-9-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halosimplex.
OX NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ21111.1, ECO:0000313|Proteomes:UP000011626};
RN [1] {ECO:0000313|EMBL:ELZ21111.1, ECO:0000313|Proteomes:UP000011626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ21111.1,
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 -!- 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 -!- 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:ELZ21111.1}.
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DR EMBL; AOIU01000043; ELZ21111.1; -; Genomic_DNA.
DR RefSeq; WP_006885499.1; NZ_AOIU01000043.1.
DR AlphaFoldDB; M0CCW4; -.
DR STRING; 797114.C475_19173; -.
DR PATRIC; fig|797114.5.peg.3884; -.
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 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:ELZ21111.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011626}.
FT DOMAIN 4..311
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 340..446
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 455 AA; 48977 MW; 4D5FDC86F669A68F CRC64;
MADYDVLVVG GGTGNNVAAA AADAGLETAL VEKGPLGGTC LNRGCNPSKM LIQAATAANH
VREAGRFFLD ATLDDVDYAA IVDDMDETLA PIAEGMEDRY RDKEHLTLYR DEAVFVDERT
VEVGSETVSA DKVVVAAGSR PLVPPIDGLD EVEYMTSTEA LYRREQPDSL VILGGGYIAV
ELGYFFESLG TDVTIVEMMD TLVPREDPDV AETFTEIARE RHEIYTGHRA TEVTSDGDGV
TVHTETEDGE TAAATGEALL VALGRRPNTD TLAVDAAGIE TDEKGFVVTN DRLETSAENV
WAQGDIADNA MFKHSGDYET QVTVENVVHG GDRRADFTAM PHAIFTEPQM AGVGKTEDEL
REEGREYVVG RADLPDTPMG RAKKLDEGFV KVLAAPDGEI LGCHMLGYEA STMIHEVVVA
MRVGSGQVSD ITDIIHAHPT LNKVVEYAFQ DVTLS
//
