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Database: UniProt
Entry: B1C6R7_9FIRM
LinkDB: B1C6R7_9FIRM
Original site: B1C6R7_9FIRM 
ID   B1C6R7_9FIRM            Unreviewed;       679 AA.
AC   B1C6R7;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00016961, ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   Name=lpdA {ECO:0000313|EMBL:EDS72704.1};
GN   ORFNames=ANASTE_00414 {ECO:0000313|EMBL:EDS72704.1};
OS   Anaerofustis stercorihominis DSM 17244.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Anaerofustis.
OX   NCBI_TaxID=445971 {ECO:0000313|EMBL:EDS72704.1, ECO:0000313|Proteomes:UP000005178};
RN   [1] {ECO:0000313|EMBL:EDS72704.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72704.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerofustis stercorihominis (DSM 17244).";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS72704.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72704.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2008) 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   -!- 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}.
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:EDS72704.1}.
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DR   EMBL; ABIL02000005; EDS72704.1; -; Genomic_DNA.
DR   RefSeq; WP_007048868.1; NZ_DS560015.1.
DR   AlphaFoldDB; B1C6R7; -.
DR   STRING; 445971.ANASTE_00414; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_2_9; -.
DR   OrthoDB; 9807946at2; -.
DR   Proteomes; UP000005178; 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; 2.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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:SF217; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
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};
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:UP000005178}.
FT   DOMAIN          2..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          120..196
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          80..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   679 AA;  72911 MW;  24ECF64E80CA5DDC CRC64;
     MGKYMLMPKL DMSMEEGQIL KWMCKVGDKT KRGDIVVEVE TGKVALEVDN PTADGTVLAL
     YVDEGDDVKV NTPIMYIGEE GEVPPTKEEA LGGGDKSEPK EEKKKAAPKK AKVSLDDFNG
     KFMLMPKLDM SMEEGQILKW MCKVGDETKR GDIVVEVETG KVALEVDNPT ADGTILALYA
     EEGEDVKVNE PIIFIGEKGS TPPTKEEAMI ITHPELADEA EDSAEDEVPS NKYDYDLAVI
     GAGPGGYVCA IRAAQLGAKV VIFEKEHIGG VCLNKGCIPT KAFVKNAEVL REVKHAGEMG
     IEVESFKTNW SKVIERKNGV VSKLTGGVSG LLKRHKVEVI MGEAVINTEH EILVGDKSYD
     VDNIVIACGS DSVMIPIEND NSVKVYDSEG MLNIDKLPED LVIIGGGVIG VELAGIMNEF
     GVHVTIVEML DSILAMADDD VIQVVDKELR NHGIDIITGV GASKLAGGNV VLSDGREIKA
     DAVLMSVGRK PVKVASNINI LVSERGFVEI DNKLRTSVDN IYAIGDVTGK VMLAHTASRQ
     GIVVAEDLYG EGATVDYSRI PSCVFTIPEV AWIGLNEKQA EELGIPYKSS KMPFAGVGKA
     LAMNDTTGFV KVITDERFDE IIGVHIVGLN ASDIVAQGAI AIDLEATSEE IANITFAHPT
     LSEGFMEACE GISGKMIHG
//
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