DLDH_TRYCR
ID DLDH_TRYCR Reviewed; 477 AA.
AC P90597; P90598; P90599;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
GN Name=LPD;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Y;
RX PubMed=9057840; DOI=10.1111/j.1432-1033.1997.00739.x;
RA Schoeneck R., Billaut-Mulot O., Numrich P., Ouaissi M.A.,
RA Krauth-Siegel R.L.;
RT "Cloning, sequencing and functional expression of dihydrolipoamide
RT dehydrogenase from the human pathogen Trypanosoma cruzi.";
RL Eur. J. Biochem. 243:739-747(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC lipoyl-L-lysyl-[protein] + H(+) + 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; X89112; CAA61483.1; -; mRNA.
DR EMBL; Y11262; CAA72132.1; -; Genomic_DNA.
DR EMBL; Y11261; CAA72131.1; -; Genomic_DNA.
DR PIR; S13863; S13863.
DR PDB; 2QAE; X-ray; 1.90 A; A/B=10-477.
DR PDBsum; 2QAE; -.
DR AlphaFoldDB; P90597; -.
DR SMR; P90597; -.
DR PRIDE; P90597; -.
DR VEuPathDB; TriTrypDB:BCY84_01530; -.
DR VEuPathDB; TriTrypDB:C3747_120g73; -.
DR VEuPathDB; TriTrypDB:C4B63_20g178; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_2745; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0036060; -.
DR VEuPathDB; TriTrypDB:TcCL_NonESM01841; -.
DR VEuPathDB; TriTrypDB:TcCLB.507089.270; -.
DR VEuPathDB; TriTrypDB:TcCLB.511025.110; -.
DR VEuPathDB; TriTrypDB:TCDM_02689; -.
DR VEuPathDB; TriTrypDB:TcG_00055; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_005316; -.
DR VEuPathDB; TriTrypDB:TcYC6_0050100; -.
DR EvolutionaryTrace; P90597; -.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
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 Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD;
KW Oxidoreductase; Redox-active center.
FT CHAIN 1..477
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068009"
FT ACT_SITE 456
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 41..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 153..155
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 190..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 330..333
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 50..55
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT VARIANT 67
FT /note="V -> L (in allele 1 and allele 2)"
FT VARIANT 144
FT /note="F -> L (in allele 1 and allele 2)"
FT VARIANT 208
FT /note="K -> E (in allele 1 and allele 2)"
FT VARIANT 256
FT /note="D -> G (in allele 1)"
FT VARIANT 268
FT /note="K -> R (in allele 2)"
FT VARIANT 376
FT /note="E -> D (in allele 1 and allele 2)"
FT VARIANT 474
FT /note="T -> S (in allele 1 and allele 2)"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 55..73
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 90..115
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 224..237
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 269..279
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 332..346
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 364..372
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 375..380
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 396..400
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:2QAE"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:2QAE"
FT STRAND 418..426
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 429..441
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 446..450
FT /evidence="ECO:0007829|PDB:2QAE"
FT HELIX 460..471
FT /evidence="ECO:0007829|PDB:2QAE"
SQ SEQUENCE 477 AA; 50491 MW; 3A02415DFAB7E0EA CRC64;
MFRRCAVKLN PYDVVVIGGG PGGYVASIKA AQLGMKTACV EKRGALGGTC LNVGCIPSKA
LLHATHVYHD AHANFARYGL MGGEGVTMDS AKMQQQKERA VKGLTGGVEY LFKKNKVTYY
KGEGSFETAH SIRVNGLDGK QEMFETKKTI IATGSEPTEL PFLPFDEKVV LSSTGALALP
RVPKTMVVIG GGVIGLELGS VWARLGAKVT VVEFAPRCAP TLDEDVTNAL VGALAKNEKM
KFMTSTKVVG GTNNGDSVSL EVEGKNGKRE TVTCEALLVS VGRRPFTGGL GLDKINVAKN
ERGFVKIGDH FETSIPDVYA IGDVVDKGPM LAHKAEDEGV ACAEILAGKP GHVNYGVIPA
VIYTMPEVAS VGKSEEELKK EGVAYKVGKF PFNANSRAKA VSTEDGFVKV LVDKATDRIL
GVHIVCTTAG ELIGEACLAM EYGASSEDVG RTCHAHPTMS EALKEACMAL VAKTINF
