ID D8IZW5_HERSS Unreviewed; 475 AA.
AC D8IZW5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
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:ADJ64455.1};
GN OrderedLocusNames=Hsero_2967 {ECO:0000313|EMBL:ADJ64455.1};
OS Herbaspirillum seropedicae (strain SmR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ64455.1, ECO:0000313|Proteomes:UP000000329};
RN [1] {ECO:0000313|EMBL:ADJ64455.1, ECO:0000313|Proteomes:UP000000329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SmR1 {ECO:0000313|EMBL:ADJ64455.1,
RC ECO:0000313|Proteomes:UP000000329};
RA Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA Weiss V.A., Yates M.A., Souza E.M.;
RT "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT fixing, plant-growth promoting beta-Proteobacteria.";
RL Submitted (APR-2010) 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=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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002039; ADJ64455.1; -; Genomic_DNA.
DR RefSeq; WP_013234927.1; NC_014323.1.
DR AlphaFoldDB; D8IZW5; -.
DR STRING; 757424.Hsero_2967; -.
DR KEGG; hse:Hsero_2967; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_1_4; -.
DR OrthoDB; 178496at2; -.
DR Proteomes; UP000000329; 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 NCBIfam; TIGR01350; lipoamide_DH; 1.
DR PANTHER; PTHR22912:SF224; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003692};
KW Flavoprotein {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|RuleBase:RU003692,
KW ECO:0000313|EMBL:ADJ64455.1};
KW Redox-active center {ECO:0000256|RuleBase:RU003692};
KW Reference proteome {ECO:0000313|Proteomes:UP000000329}.
FT DOMAIN 5..337
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 356..465
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 153..155
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 190..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 328..331
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 49..54
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 475 AA; 50111 MW; 18BC463FF3D921F9 CRC64;
MSKNFDVVVI GGGPGGYIAA IRAAQLGFNT ACIDEWKNEK GGPAPGGTCT NVGCIPSKAL
LQSSEHYEHA SHGFAEHGIE VKGLGLNLEK MLGRKNTVVK QNNDGILYLF KKNKVSFFHG
RGSFVKGDAN GYEIKVAGAA EETITAKHVI VATGSNARAL PGAEFDEKLI LSNTGALSIT
EVPKKLGVIG AGVIGLEMGS VWRRLGAEVT VLEALPTFLG AVDEQIAKEA QKLLTKQGLA
VNLGVKIGAI KAGKNSVSVE YTDAKGDAHT GEFDKLIVSI GRTPNTIGLN AEGVGLKLDE
RGFIAVDGDC KTNLPNVWAV GDVVRGPMLA HKAEEEGVAV AERIAGQHGH VNFNTIPWVI
YTSPEIAWVG KTEQQLKAEG VQYKAGTFPF LANGRARALG DTSGMVKFLA DAKTDEILGV
HIVGPMASEL ISEAVVAMEF RASSEDIARI CHAHPSLSEA TKEAALAVDK RALNF
//
