GenomeNet

Database: UniProt
Entry: D1AIV2_SEBTE
LinkDB: D1AIV2_SEBTE
Original site: D1AIV2_SEBTE 
ID   D1AIV2_SEBTE            Unreviewed;       563 AA.
AC   D1AIV2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 74.
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   OrderedLocusNames=Sterm_0026 {ECO:0000313|EMBL:ACZ06914.1};
OS   Sebaldella termitidis (strain ATCC 33386 / NCTC 11300).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Sebaldella.
OX   NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ06914.1, ECO:0000313|Proteomes:UP000000845};
RN   [1] {ECO:0000313|Proteomes:UP000000845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA   Woyke T., Wu D., Eisen J.A.;
RT   "The complete chromosome of Sebaldella termitidis ATCC 33386.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ06914.1, ECO:0000313|Proteomes:UP000000845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RX   PubMed=21304705;
RA   Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Beck B.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Chen F.;
RT   "Complete genome sequence of Sebaldella termitidis type strain (NCTC
RT   11300).";
RL   Stand. Genomic Sci. 2:220-227(2010).
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:ARBA00001492,
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; CP001739; ACZ06914.1; -; Genomic_DNA.
DR   RefSeq; WP_012859514.1; NC_013517.1.
DR   AlphaFoldDB; D1AIV2; -.
DR   STRING; 526218.Sterm_0026; -.
DR   KEGG; str:Sterm_0026; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_2_0; -.
DR   OMA; DAKYGEW; -.
DR   Proteomes; UP000000845; 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; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
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   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.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_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|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   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|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:UP000000845}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   ACT_SITE        537
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         153
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         218
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         280..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         303
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         367
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         405
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         411..414
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        144..149
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   563 AA;  61077 MW;  B752E5F243C0A8F4 CRC64;
     MSVEIIMPKA GMSMEEGTII KWLKEEGEAI KEGEPIVEIL TDKVNMEVEA ESSGYLLKKV
     RFENEVLPVF TVIGYIGEKG ESVSEVKEAE KKEEVKTETK TSDEKEYDVI VIGGGPAGYI
     SANKASQLGA KTALVEKREL GGTCLNRGCI PTKTYIKNIE ILEEAEKAES RGLDIKVTKN
     ISDLTKAVEF KNKVTKKLSQ GVGGLLRSYG VDVYSTAGKL GEGKKVTLED GQVLKGKKII
     LAGGSKTRYL NIPGIDSDKI LTSTTILDLN KVPERLVIVG GGVIGCEFAE IFRGYGTEVT
     IVEAMSNLLP FNDKEISQEL EKIFKKKGIK LLTDKQVTGF KDKGKEIETV LKSGESLSSD
     YVLFSIGREA DLSCVDGLEI KQDRGRLIVN EYMETSIAGV YAAGDINGLS MLAHSAFKMG
     ETAAGNALGG REEVRLDNTP KCVYTLPEIA SVGLTEEEAL KKYGKIRTGR FNFGANGRAI
     ASSEEEGFVK VICDDNYGEI LGVHVIGSKA TEMISAGVIL MEMEITIEEA SELIYAHPTF
     SEAILEACAD CLGKALHLPK KKM
//
DBGET integrated database retrieval system