ID F8DBZ8_HALXS Unreviewed; 487 AA.
AC F8DBZ8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:AEH35974.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:AEH35974.1};
GN OrderedLocusNames=Halxa_1341 {ECO:0000313|EMBL:AEH35974.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH35974.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|EMBL:AEH35974.1, ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(2012).
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}.
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DR EMBL; CP002839; AEH35974.1; -; Genomic_DNA.
DR RefSeq; WP_013878871.1; NC_015666.1.
DR AlphaFoldDB; F8DBZ8; -.
DR STRING; 797210.Halxa_1341; -.
DR GeneID; 10796311; -.
DR KEGG; hxa:Halxa_1341; -.
DR eggNOG; arCOG01068; Archaea.
DR HOGENOM; CLU_016755_1_2_2; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000006794; 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; 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:UP000006794}.
FT DOMAIN 4..320
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 351..459
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 467..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 51198 MW; 486A50FB9733D574 CRC64;
MDEYDIVVIG GGSGSQVATA AADRGLEAAV IERGPLGGAC ITRGCVPSKA LIHRADLADA
VRRAGEFGIA ADLQDVAYGE ITDAIHDTVY EKAARQERAL EESDSVALFR GEGRFVDEWT
IAVKPTDDSG DTREVRGDAI VLAVGSRPMV PPIDGLEDVD FLTSDDALFL DEQPDELAIV
GGGYIGAELG YFFGALGTDV SMIGRSERLI PGEDDDASAV VTDSLADYCD LYTGYEAAEV
AQGDGGGSVT ITAEPSDDDG EPVEIEADEL LLATGRRPNT DTLALEETSV ETDDKGYVET
DARLETAAEG IWALGDIVGE QPFKHAADYE AEVVMANVLN DAGREVDYGA MPHAIFTEPQ
VASVGRTEGE LEDEGREYES TTVPFDAAPL GLILGADDGF VKVLAAPDGE ILGCHVVGPQ
ASTLIQEVVV AMDSGDGTVD DVADPVHVHP ALSEAIYTAF DDLSSKEFSS APDWRDVAPS
GRSSEAE
//
