ID DLDH_MOUSE Reviewed; 509 AA.
AC O08749; Q3TG55; Q3U5W5; Q3UWP7; Q99LD3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-APR-2013, entry version 116.
DE RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE Flags: Precursor;
GN Name=Dld;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J;
RX PubMed=9169128; DOI=10.1006/geno.1997.4670;
RA Johnson M., Yang H.S., Johanning G.L., Patel M.S.;
RT "Characterization of the mouse dihydrolipoamide dehydrogenase (Dld)
RT gene: genomic structure, promoter sequence, and chromosomal
RT localization.";
RL Genomics 41:320-326(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 73-89; 216-259; 289-334; 316-334; 347-365; 421-428
RP AND 483-509, AND MASS SPECTROMETRY.
RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT "Substrate and functional diversity of lysine acetylation revealed by
RT a proteomics survey.";
RL Mol. Cell 23:607-618(2006).
CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
CC cleavage system as well as of the alpha-ketoacid dehydrogenase
CC complexes. Involved in the hyperactivation of spermatazoa during
CC capacitation and in the spermatazoal acrosome reaction.
CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC protein N(6)-(lipoyl)lysine + NADH.
CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC -!- SUBUNIT: Homodimer. Eukaryotic pyruvate dehydrogenase complexes
CC are organized about a core consisting of the oligomeric
CC dihydrolipoamide acetyl-transferase, around which are arranged
CC multiple copies of pyruvate dehydrogenase, dihydrolipoamide
CC dehydrogenase and protein X bound by non-covalent bonds (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: Acetylation of Lys-127 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- PTM: Tyrosine phosphorylated (By similarity).
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family.
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DR EMBL; U73445; AAC53170.1; -; mRNA.
DR EMBL; AK117104; BAE43405.1; -; mRNA.
DR EMBL; AK136193; BAE22867.1; -; mRNA.
DR EMBL; AK153399; BAE31961.1; -; mRNA.
DR EMBL; AK168875; BAE40693.1; -; mRNA.
DR EMBL; BC003368; AAH03368.1; -; mRNA.
DR IPI; IPI00874456; -.
DR RefSeq; NP_031887.2; NM_007861.4.
DR UniGene; Mm.3131; -.
DR ProteinModelPortal; O08749; -.
DR SMR; O08749; 38-509.
DR IntAct; O08749; 3.
DR PhosphoSite; O08749; -.
DR REPRODUCTION-2DPAGE; O08749; -.
DR SWISS-2DPAGE; O08749; -.
DR PaxDb; O08749; -.
DR PRIDE; O08749; -.
DR Ensembl; ENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664.
DR GeneID; 13382; -.
DR KEGG; mmu:13382; -.
DR UCSC; uc007nhg.2; mouse.
DR CTD; 1738; -.
DR MGI; MGI:107450; Dld.
DR eggNOG; COG1249; -.
DR GeneTree; ENSGT00550000074844; -.
DR HOGENOM; HOG000276708; -.
DR HOVERGEN; HBG002290; -.
DR KO; K00382; -.
DR OMA; VANSRAK; -.
DR NextBio; 283728; -.
DR Bgee; O08749; -.
DR CleanEx; MM_DLD; -.
DR Genevestigator; O08749; -.
DR GermOnline; ENSMUSG00000020664; Mus musculus.
DR GO; GO:0043159; C:acrosomal matrix; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:Compara.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IMP:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:0048240; P:sperm capacitation; IDA:MGI.
DR Gene3D; 3.30.390.30; -; 1.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR InterPro; IPR006258; Lipoamide_DH.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR PANTHER; PTHR22912:SF20; PTHR22912:SF20; 1.
DR Pfam; PF00070; Pyr_redox; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF55424; FAD/NAD-linked_reductase_dimer; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing;
KW Disulfide bond; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase;
KW Phosphoprotein; Redox-active center; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 35 Mitochondrion (By similarity).
FT CHAIN 36 509 Dihydrolipoyl dehydrogenase,
FT mitochondrial.
FT /FTId=PRO_0000030297.
FT NP_BIND 71 80 FAD (By similarity).
FT NP_BIND 183 185 FAD (By similarity).
FT NP_BIND 220 227 NAD (By similarity).
FT NP_BIND 361 364 FAD (By similarity).
FT ACT_SITE 487 487 Proton acceptor (By similarity).
FT BINDING 89 89 FAD (By similarity).
FT BINDING 154 154 FAD; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 243 243 NAD (By similarity).
FT BINDING 278 278 NAD; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 314 314 NAD; via amide nitrogen (By similarity).
FT BINDING 355 355 FAD (By similarity).
FT MOD_RES 127 127 N6-acetyllysine.
FT MOD_RES 143 143 N6-acetyllysine (By similarity).
FT MOD_RES 410 410 N6-acetyllysine (By similarity).
FT MOD_RES 417 417 N6-acetyllysine (By similarity).
FT DISULFID 80 85 Redox-active (By similarity).
FT CONFLICT 54 54 Y -> C (in Ref. 1; AAC53170).
FT CONFLICT 144 144 Q -> T (in Ref. 2; BAE22867).
FT CONFLICT 149 149 H -> L (in Ref. 2; BAE31961).
FT CONFLICT 283 283 K -> E (in Ref. 2; BAE40693).
SQ SEQUENCE 509 AA; 54272 MW; 2C381852BAAD0441 CRC64;
MQSWSRVYRS LAKKGHFNRI SHGLQGVSSV PLRTYADQPI EADVTVIGSG PGGYVAAIKS
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEIPEVRLNL
EKMMEQKHSA VKALTGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS TQVIDTKNIL
VATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT
AVEFLGHVGG IGIDMEISKN FQRILQRQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN NRFQTKIPNI YAIGDVVAGP
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEFKIGK
FPFAANSRAK TNADTDGMVK ILGHKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI
ARVCHAHPTL SEAFREANLA AAFGKPINF
//
