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Database: UniProt
Entry: S5LYH0_9MOLU
LinkDB: S5LYH0_9MOLU
Original site: S5LYH0_9MOLU 
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
//
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