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Database: UniProt
Entry: Q6F275_MESFL
LinkDB: Q6F275_MESFL
Original site: Q6F275_MESFL 
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
//
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