ID S5LYH0_9MOLU Unreviewed; 629 AA.
AC S5LYH0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00016961, ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN Name=pdhD {ECO:0000313|EMBL:AGR41621.1};
GN ORFNames=STAIW_v1c10380 {ECO:0000313|EMBL:AGR41621.1};
OS Spiroplasma taiwanense CT-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276220 {ECO:0000313|EMBL:AGR41621.1, ECO:0000313|Proteomes:UP000014984};
RN [1] {ECO:0000313|EMBL:AGR41621.1, ECO:0000313|Proteomes:UP000014984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT-1 {ECO:0000313|EMBL:AGR41621.1};
RX PubMed=23873917; DOI=10.1093/gbe/evt108;
RA Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT "Comparison of metabolic capacities and inference of gene content evolution
RT in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL Genome Biol. Evol. 5:1512-1523(2013).
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|RuleBase:RU003692};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003692};
CC Note=Binds 1 FAD per subunit. {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}.
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DR EMBL; CP005074; AGR41621.1; -; Genomic_DNA.
DR RefSeq; WP_020834760.1; NC_021846.1.
DR AlphaFoldDB; S5LYH0; -.
DR STRING; 1276220.STAIW_v1c10380; -.
DR KEGG; stai:STAIW_v1c10380; -.
DR PATRIC; fig|1276220.3.peg.1055; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_2_14; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000014984; Chromosome.
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; 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:SF217; 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 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|RuleBase:RU003692};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003692}; Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003692};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003692}; Pyruvate {ECO:0000313|EMBL:AGR41621.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003692};
KW Reference proteome {ECO:0000313|Proteomes:UP000014984}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 629 AA; 67564 MW; A640231AFBBBA616 CRC64;
MFKVKFADIG EGLTEGTVTE VLVKIGDSVK MGDRLFNVET DKVTSDIYAP VDGKIAKILI
SANQEIKVGD VVIEIDDGKG EATAEPEKKA ETAEENASVV GATPVSNDLL SRGRAGRTVP
PKESIAAKVI EAVSGNTPMP GIVSGHGRTL KPAPKFSPKD TANHYDVIVI GAGVGGYVCA
IKCAQLGLNT LIIEKGNYGG VCLNIGCIPT KTLLKSADLY EQITKHADKY GIKVAQEGVK
ADWKAIQARK ADVVNKLTTG VKGLLKKNKV TTVEGFAKAI DKNTVEVDKK QYTCDNMIIA
TGSVPNHFTI PGAKEAIESG WLIDSTGALS LPKIPKSMVI IGGGVIGVEF ACVYKRLGTK
VTILQFLPTI LEMLDSDVSK EMTKELISRG NLEIITEATT KSFGKNEVIY EKDGKEIKLK
ADYCLQSVGR KVVTEGFENI GLQINERGHI VVNEYCETNI DGVYSIGDVT GKMMLAHVAS
HQGIIAANRI ARRLQKEHAE DLAMNFERVP SCIYTHPEVA SVGKTEDELR KAGVEYKAFK
FPFAAIGKAL ADGNTTGFVK LICEPKYKQV LGCHIISNTA TDMISEITTL MESEGTITEI
ARAIHPHPTL SEAIGEAAEA LESGKPINF
//