ID C0EL33_NEIFL Unreviewed; 468 AA.
AC C0EL33;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:EEG34254.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:EEG34254.1};
GN ORFNames=NEIFLAOT_00639 {ECO:0000313|EMBL:EEG34254.1};
OS Neisseria flavescens NRL30031/H210.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546264 {ECO:0000313|EMBL:EEG34254.1, ECO:0000313|Proteomes:UP000004457};
RN [1] {ECO:0000313|EMBL:EEG34254.1, ECO:0000313|Proteomes:UP000004457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRL30031/H210 {ECO:0000313|EMBL:EEG34254.1,
RC ECO:0000313|Proteomes:UP000004457};
RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) 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 -!- 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:EEG34254.1}.
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DR EMBL; ACEN01000016; EEG34254.1; -; Genomic_DNA.
DR RefSeq; WP_004464205.1; NZ_ACEN01000016.1.
DR AlphaFoldDB; C0EL33; -.
DR GeneID; 49971165; -.
DR eggNOG; COG1249; Bacteria.
DR Proteomes; UP000004457; 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 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 FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000313|EMBL:EEG34254.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004457}.
FT DOMAIN 7..326
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 349..457
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 447
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 143..145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 180..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 311
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 468 AA; 50989 MW; 6FA5E2CF88E7B2ED CRC64;
MKKIQADVVV LGGGTAGMGA FRNARLQTDN VYLIENNVFG TTCARVGCMP SKLLIAAAEA
RHHALHTDPF GVHLDKDSVT VNGEEVMRRV KSERDRFVGF VVSDVEEWPA DKRIMGTAKF
VDEHTVQIDD HTQITAKSFV IATGSRPVIF PQWEVLGDRL IVNDDVFSWD TLPKSVAVFG
PGVIGLELGQ ALHRLGVKVE IFGVAGAIGG ISDPVVVEEA KTVFGEELTL HLDAKTEVKL
DAEGNVEVHW EQDGEKGVFH AEYALAAAGR RPNVDNIGLE NLNIEKDARG VPVADPLTMQ
TSIPHIFIAG DASNQLPLLH EASDQGKIAG HNAAIFPNIE GGLRRSVIGV VFTSPQIATI
GLKYTQVAAK YQPDEFVIGE VSFRNQGRSR VMLVNKGHMR LYAEKATGRF IGAEVVGPAA
EHLAHLMAWA HQMKMTIPQM LDMPFYHPVI EEGLRTALRD ADAKLKQA
//
