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Dihydrolipoyl dehydrogenase (EC 1.8.1.4)

 A0A024R713_HUMAN        Unreviewed;       509 AA.
A0A024R713;
09-JUL-2014, integrated into UniProtKB/TrEMBL.
09-JUL-2014, sequence version 1.
30-AUG-2017, entry version 27.
RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
Name=DLD {ECO:0000313|EMBL:EAW83422.1};
ORFNames=hCG_17110 {ECO:0000313|EMBL:EAW83422.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000313|EMBL:EAW83422.1};
[1] {ECO:0000313|EMBL:EAW83422.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11181995; DOI=10.1126/science.1058040;
Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D.,
Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q.,
Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G.,
Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S.,
Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J.,
Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R.,
Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A.,
Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K.,
Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V.,
Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z.,
Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A.,
Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V.,
Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B.,
Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J.,
Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C.,
Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L.,
Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S.,
Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A.,
Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D.,
Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L.,
Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N.,
Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S.,
Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F.,
Kline L., Koduru S., Love A., Mann F., May D., McCawley S.,
McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K.,
Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N.,
Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M.,
Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F.,
Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A.,
Mi H., Lazareva B., Hatton T., Narechania A., Diemer K.,
Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R.,
Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J.,
Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H.,
Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D.,
Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A.,
Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S.,
Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L.,
Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W.,
McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M.,
Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
"The sequence of the human genome.";
Science 291:1304-1351(2001).
[2] {ECO:0000313|EMBL:EAW83422.1}
NUCLEOTIDE SEQUENCE.
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
{ECO:0000256|RuleBase:RU003692}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000256|RuleBase:RU003692};
Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003692};
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
{ECO:0000256|RuleBase:RU003692}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000256|RuleBase:RU003692}.
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EMBL; CH471070; EAW83422.1; -; Genomic_DNA.
RefSeq; NP_000099.2; NM_000108.4.
UniGene; Hs.131711; -.
ProteinModelPortal; A0A024R713; -.
SMR; A0A024R713; -.
PaxDb; A0A024R713; -.
PRIDE; A0A024R713; -.
GeneID; 1738; -.
KEGG; hsa:1738; -.
CTD; 1738; -.
eggNOG; KOG1335; Eukaryota.
eggNOG; COG1249; LUCA.
KO; K00382; -.
OMA; TMSEAVM; -.
OrthoDB; EOG091G05AA; -.
PhylomeDB; A0A024R713; -.
GenomeRNAi; 1738; -.
Bgee; ENSG00000091140; -.
ExpressionAtlas; A0A024R713; baseline and differential.
GO; GO:0043159; C:acrosomal matrix; IEA:Ensembl.
GO; GO:0005929; C:cilium; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:Ensembl.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl.
GO; GO:0043544; F:lipoamide binding; IEA:Ensembl.
GO; GO:0051287; F:NAD binding; IEA:Ensembl.
GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0051068; P:dihydrolipoamide metabolic process; IEA:Ensembl.
GO; GO:0007369; P:gastrulation; IEA:Ensembl.
GO; GO:0009106; P:lipoate metabolic process; IEA:Ensembl.
GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IEA:Ensembl.
GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
3: Inferred from homology;
FAD {ECO:0000256|RuleBase:RU003692};
Flavoprotein {ECO:0000256|RuleBase:RU003692};
NAD {ECO:0000256|RuleBase:RU003692};
Oxidoreductase {ECO:0000256|RuleBase:RU003692};
Pyruvate {ECO:0000313|EMBL:EAW83422.1};
Redox-active center {ECO:0000256|RuleBase:RU003692}.
DOMAIN 43 370 FAD/NAD-binding_dom.
{ECO:0000259|Pfam:PF07992}.
DOMAIN 389 497 Pyr_redox_dim.
{ECO:0000259|Pfam:PF02852}.
SEQUENCE 509 AA; 54177 MW; 7613492C516F3835 CRC64;
MQSWSRVYCS LAKRGHFNRI SHGLQGLSAV PLRTYADQPI DADVTVIGSG PGGYVAAIKA
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL
DKMMEQKSTA VKALTGGIAH LFKQNKVVHV NGYGKITGKN QVTATKADGG TQVIDTKNIL
IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT
AVEFLGHVGG VGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSIEAASGGK
AEVITCDVLL VCIGRRPFTK NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK
FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI
ARVCHAHPTL SEAFREANLA ASFGKSINF


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