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Database: UniProt
Entry: B2IB57_BEII9
LinkDB: B2IB57_BEII9
Original site: B2IB57_BEII9 
ID   B2IB57_BEII9            Unreviewed;       480 AA.
AC   B2IB57;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00016961, ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
GN   OrderedLocusNames=Bind_1508 {ECO:0000313|EMBL:ACB95141.1};
OS   Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS   8712).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Beijerinckia.
OX   NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB95141.1, ECO:0000313|Proteomes:UP000001695};
RN   [1] {ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA   Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT   "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT   9039.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB95141.1, ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RX   PubMed=20601475; DOI=10.1128/JB.00656-10;
RA   Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C.,
RA   Dunfield P.F.;
RT   "Complete genome sequence of Beijerinckia indica subsp. indica.";
RL   J. Bacteriol. 192:4532-4533(2010).
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|ARBA:ARBA00001492,
CC         ECO:0000256|RuleBase:RU003692};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3,
CC         ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3,
CC       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; CP001016; ACB95141.1; -; Genomic_DNA.
DR   RefSeq; WP_012384498.1; NC_010581.1.
DR   AlphaFoldDB; B2IB57; -.
DR   STRING; 395963.Bind_1508; -.
DR   KEGG; bid:Bind_1508; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_2_5; -.
DR   OMA; WASMLND; -.
DR   OrthoDB; 9776382at2; -.
DR   Proteomes; UP000001695; Chromosome.
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:SF217; 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|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
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:UP000001695}.
FT   DOMAIN          5..341
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          361..469
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        459
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         195..202
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         218
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         326
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         332..335
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        42..47
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   480 AA;  50854 MW;  5A606C71B8683E02 CRC64;
     MAAAYDVLII GGGPGGYVTA IRSAQLGLKT AVVEREHLGG ICLNWGCIPT KALLRSAEIY
     HYLQHPKDYG LTIEGKIGFD PAAVVKRSRG VSAQLNGGVG FLLKKNKVDV IWGEATITKV
     GEVTVAATKK TIVQPQNPIP KGVLGEGTYS AKNIIVATGA RPRVLPGLEP DGKTIWTYFE
     AMVPESFPKS LIVMGSGAIG IEFASFYHTM GAEVTVVEVL PQIMPVEDAE IAGLARKQFE
     KQGIKILTGT KVTKIEKNAQ GLTATLEDSK GAISTLSAEK MISAVGVVGN SENLGLEKLG
     VKIDRGIISV DGFGRTNVPG IFAIGDVAGP PMLAHKAEHE GVICVEAIKG LHPHPMDKSM
     IPGCTYCQPQ VASVGLTEAK AKEAGYTVKV GRFPFVGNGK AIALGEPDGL IKTIFDAKTG
     KLLGAHMVGA EVTELIQGFV VAMNLETTEE ELMHTVFPHP TLSEMMHESV LDAYGRVIHM
//
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