ID Q6F275_MESFL Unreviewed; 602 AA.
AC Q6F275;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 126.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN OrderedLocusNames=Mfl042 {ECO:0000313|EMBL:AAT75398.1};
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Entomoplasmataceae; Mesoplasma.
OX NCBI_TaxID=265311 {ECO:0000313|EMBL:AAT75398.1, ECO:0000313|Proteomes:UP000006647};
RN [1] {ECO:0000313|EMBL:AAT75398.1, ECO:0000313|Proteomes:UP000006647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1
RC {ECO:0000313|Proteomes:UP000006647};
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) 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|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; AE017263; AAT75398.1; -; Genomic_DNA.
DR RefSeq; WP_011182939.1; NC_006055.1.
DR RefSeq; YP_053282.1; NC_006055.1.
DR AlphaFoldDB; Q6F275; -.
DR STRING; 265311.Mfl042; -.
DR PaxDb; 265311-Mfl042; -.
DR EnsemblBacteria; AAT75398; AAT75398; Mfl042.
DR GeneID; 2898168; -.
DR KEGG; mfl:Mfl042; -.
DR PATRIC; fig|265311.5.peg.42; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_2_14; -.
DR OMA; DAKYGEW; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000006647; 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: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 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};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003692};
KW Reference proteome {ECO:0000313|Proteomes:UP000006647}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 602 AA; 64145 MW; 02B3FD52E2C66F83 CRC64;
MFKVKFADIG EGLTEGKVAE VLVKLGQEIK EGDALFFVET DKVNSEIPAP VGGKIAKVLI
SEGQEIKVGD VVIEIDDGSA TVEAAPAAEE ENASVVGSTP VSNDLIPSRG PAPTQNVAAQ
PTPAPVATKH TDIEESFDVI VVGAGIGGYV SAIKTAQLGL KTLIIEKQYY GGVCLNVGCI
PTKSLLRTAK VFEDIVHKAA NLGIDMKTKD EPSINWNKAL ERKDGVVNKL TGGVKVLLTK
NGVKQIIGEA SALDKNTISV NGKKYHCDNL IIASGSVPNE LPLPGFAEGR ESGFLIDSTK
ILSLPKIPKT LTVIGGGVIG IEFGCLFAAL GTKVTVIEGA PKILPMLDQD VTALMTKTLK
EKYKIEIFTN AKVKEVKGKS VVFEIDGKEQ TVKSDYCLES IGRKTVTKGF DGIGLELSER
KSIIANDYGE TNLEGVYAIG DVTSKIMLAH VASHAGIVTA NRIALKANKP DAHDIKMDYS
KIPSCIYSHP EIAMIGKTEQ QLKEEGVEYK TFKFPFAAIG KALADDDTTG FVKIICEPKY
KTLLGAHIIG NRATDMISEF TTLIECEGTI TELARAIHPH PTMSEAIGEA AEALESGKSL
NL
//