ID E4V8Y1_BIFBI Unreviewed; 496 AA.
AC E4V8Y1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Putative dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:EFR50073.1};
GN ORFNames=BBNG_00620 {ECO:0000313|EMBL:EFR50073.1};
OS Bifidobacterium bifidum NCIMB 41171.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=398513 {ECO:0000313|EMBL:EFR50073.1, ECO:0000313|Proteomes:UP000002776};
RN [1] {ECO:0000313|EMBL:EFR50073.1, ECO:0000313|Proteomes:UP000002776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 41171 {ECO:0000313|EMBL:EFR50073.1,
RC ECO:0000313|Proteomes:UP000002776};
RG The Broad Institute Genome Sequencing Platform;
RA Goulas T., Tzortzis G., Gibson G.R., Ward D., Mehta T., Young S., Jaffe D.,
RA Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., Sykes S.,
RA Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J., Nusbaum C.,
RA Birren B.;
RT "Annotation of Bifidobacterium bifidum strain NCIMB 41171.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
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; DS990229; EFR50073.1; -; Genomic_DNA.
DR RefSeq; WP_003812620.1; NZ_DS990229.1.
DR AlphaFoldDB; E4V8Y1; -.
DR GeneID; 56627128; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_2_11; -.
DR Proteomes; UP000002776; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 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:RU003691};
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:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}.
FT DOMAIN 5..350
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 370..483
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 474
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 199..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 496 AA; 52324 MW; A61A1854480103C3 CRC64;
MSEAFDIAII GGGPGGYSTA LRAAELGKRV AMIERDATLG GTCLNRGCIP SKALISATHA
IDSIRHAGEL GISATINGID YGTLHDYKKR IVDTMTQGLA GLLAHRGVTV FWGVASITGA
ARPITVHIAA PADGRDVQRS VRSDVPEDIG PSYDITAQDV VLAMGSVPRQ LPGEPFRGAI
IDSTRAMSMA MPHNAVIIGA GAIAAEFASM WNAAGCKVTM LIRKDRVLSG WDRRAGVTLT
RELKRHGIDV IDRSTVTHID TGVNMGALVH YTSAKDGGST EHIAEGEFVL VAIGRDPLTS
DGWIRDAGVT VDDHGFITTD GYGRTPVAGI WAVGDITEGH ALAHRAFEQG IIAAESIAGL
DPKPLDEDTI PQIVFSNPEA ASVGLTATDA KQRDDLSDIK ETVYPMMSNA RMMMSDSGGS
LSLVSGIRAQ QPGVRVVLGV HMVAPVASDI IAEAEQLVGN HTPLSDAARL IHPHPTFSET
LGETLLKADD RPLHTR
//
