ID C6M316_NEISI Unreviewed; 595 AA.
AC C6M316;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 Name=lpdA {ECO:0000313|EMBL:EET45280.1};
GN ORFNames=NEISICOT_00907 {ECO:0000313|EMBL:EET45280.1};
OS Neisseria sicca ATCC 29256.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=547045 {ECO:0000313|EMBL:EET45280.1, ECO:0000313|Proteomes:UP000005365};
RN [1] {ECO:0000313|EMBL:EET45280.1, ECO:0000313|Proteomes:UP000005365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29256 {ECO:0000313|EMBL:EET45280.1,
RC ECO:0000313|Proteomes:UP000005365};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) 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|ARBA:ARBA00043836,
CC ECO:0000256|RuleBase:RU003692};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
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 -!- 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:EET45280.1}.
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DR EMBL; ACKO02000004; EET45280.1; -; Genomic_DNA.
DR RefSeq; WP_003756785.1; NZ_ACKO02000004.1.
DR AlphaFoldDB; C6M316; -.
DR STRING; 490.A6J88_09450; -.
DR eggNOG; COG1249; Bacteria.
DR Proteomes; UP000005365; 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; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
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:SF160; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 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}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
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}.
FT DOMAIN 3..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 568
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 304..311
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 327
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 395
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 436
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 442..445
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 157..162
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 595 AA; 62060 MW; 14DF5179239F3080 CRC64;
MSLVELKVPD IGGHENVDII AVEVNVGDTI AVDDTLITLE TDKATMDVPA EVAGVVKEVK
VKVGDKISEG GLIVVVEAEG AAAAPKAEAP AAAPAQEAPK AAAPAPQAAQ FGGSADAEYD
VVVLGGGPGG YSAAFAAADE GLKVAIVERY KTLGGVCLNV GCIPSKALLH NAAVIDEVRH
LAANGIKYPE PELDIDMLRG YKDGVVSRLT TGLAGMAKGR KVDVIQGDGQ FLDPHHLEVS
LTTGDVYEQA TLTGEKKIVA FKNCIIAAGS RVTKLPFIPE DPRIIDSSGA LALKEVPGKL
LIIGGGIIGL EMGTVYSTLG SRLDVVEMMD GLMQGADRDL VKVWQKQNEY RFDNIMINTK
TVAVEPKEDG VYVTFEGANA PKEPQRYDAV LVAAGRAPNG KLISAEKAGV AVTDRGFIEV
DKQMRTNVPH IYAIGDIVGQ PMLAHKAVHE GHVAAENCAG HKAYFDARVI PGVAYTAPEV
AWVGETELSA KASGRKITKA NFPWAASGRA IANGCDNGFT KLIFDAETGR IIGGGIVGPN
GGDMIGEICL AIEMGCDAED IGKTIHPHPT LGESIGMAAE VALGTCTDLP AQKKK
//
