Reviewed, UniProtKB/Swiss-Prot P90597 (DLDH_TRYCR)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase

Gene names

Name:

LPD

Organism

Trypanosoma cruzi

Taxonomic identifier

5693 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Schizotrypanum

Protein attributes

Sequence length	477 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer By similarity.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Polymorphism
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 477

477

Dihydrolipoyl dehydrogenase

PRO_0000068009

Regions

Nucleotide binding

41 – 50

10

FAD By similarity

Nucleotide binding

153 – 155

3

FAD By similarity

Nucleotide binding

190 – 197

8

NAD By similarity

Nucleotide binding

330 – 333

4

FAD By similarity

Sites

Active site

456

1

Proton acceptor By similarity

Binding site

59

1

FAD By similarity

Binding site

124

1

FAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

213

1

NAD By similarity

Binding site

248

1

NAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

282

1

NAD; via amide nitrogen By similarity

Binding site

323

1

FAD By similarity

Amino acid modifications

Disulfide bond

50 ↔ 55

Redox-active By similarity

Natural variations

Natural variant

67

1

V → L in allele 1 and allele 2.

Natural variant

144

1

F → L in allele 1 and allele 2.

Natural variant

208

1

K → E in allele 1 and allele 2.

Natural variant

256

1

D → G in allele 1.

Natural variant

268

1

K → R in allele 2.

Natural variant

376

1

E → D in allele 1 and allele 2.

Natural variant

474

1

T → S in allele 1 and allele 2.

Secondary structure

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477

Helix Strand Turn

Details...

Beta strand

12 – 17

6

Helix

25 – 32

8

Beta strand

37 – 40

4

Turn

50 – 52

3

Helix

56 – 73

18

Helix

75 – 77

3

Helix

90 – 101

12

Helix

109 – 115

7

Beta strand

118 – 120

3

Beta strand

126 – 128

3

Beta strand

131 – 134

4

Beta strand

142 – 151

10

Beta strand

167 – 171

5

Beta strand

184 – 189

6

Helix

201 – 204

4

Beta strand

208 – 212

5

Beta strand

214 – 219

6

Helix

224 – 230

7

Helix

234 – 237

4

Beta strand

241 – 243

3

Beta strand

258 – 263

6

Beta strand

270 – 279

10

Turn

293 – 296

4

Beta strand

318 – 320

3

Helix

332 – 337

6

Helix

341 – 346

6

Beta strand

360 – 362

3

Beta strand

364 – 370

7

Helix

375 – 380

6

Helix

392 – 394

3

Helix

396 – 400

5

Turn

414 – 416

3

Beta strand

423 – 426

4

Helix

436 – 441

6

Turn

446 – 448

3

Helix

460 – 471

12

Sequences

	Sequence		Length	Mass (Da)
	P90597-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 3A02415DFAB7E0EA	FASTA	477	50,491
	10 20 30 40 50 60 MFRRCAVKLN PYDVVVIGGG PGGYVASIKA AQLGMKTACV EKRGALGGTC LNVGCIPSKA 70 80 90 100 110 120 LLHATHVYHD AHANFARYGL MGGEGVTMDS AKMQQQKERA VKGLTGGVEY LFKKNKVTYY 130 140 150 160 170 180 KGEGSFETAH SIRVNGLDGK QEMFETKKTI IATGSEPTEL PFLPFDEKVV LSSTGALALP 190 200 210 220 230 240 RVPKTMVVIG GGVIGLELGS VWARLGAKVT VVEFAPRCAP TLDEDVTNAL VGALAKNEKM 250 260 270 280 290 300 KFMTSTKVVG GTNNGDSVSL EVEGKNGKRE TVTCEALLVS VGRRPFTGGL GLDKINVAKN 310 320 330 340 350 360 ERGFVKIGDH FETSIPDVYA IGDVVDKGPM LAHKAEDEGV ACAEILAGKP GHVNYGVIPA 370 380 390 400 410 420 VIYTMPEVAS VGKSEEELKK EGVAYKVGKF PFNANSRAKA VSTEDGFVKV LVDKATDRIL 430 440 450 460 470 GVHIVCTTAG ELIGEACLAM EYGASSEDVG RTCHAHPTMS EALKEACMAL VAKTINF

References

[1]

"Cloning, sequencing and functional expression of dihydrolipoamide dehydrogenase from the human pathogen Trypanosoma cruzi." Schoeneck R., Billaut-Mulot O., Numrich P., Ouaissi M.A., Krauth-Siegel R.L. Eur. J. Biochem. 243:739-747(1997) [PubMed: 9057840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: Y.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X89112 mRNA. Translation: CAA61483.1.
Y11262 Genomic DNA. Translation: CAA72132.1.
Y11261 Genomic DNA. Translation: CAA72131.1.

PIR

S13863.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QAE	X-ray	1.90	A/B	10-477	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.8.1.4. 884.

Family and domain databases

InterPro

IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

PANTHER

PTHR22912:SF20. Lipoamide_DH. 1 hit.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.
PR00945. HGRDTASE.

ProDom

PD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01350. lipoamide_DH. 1 hit.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DLDH_TRYCR

Accession

Primary (citable) accession number: P90597
Secondary accession number(s): P90598, P90599

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	May 1, 1997
Last modified:	September 22, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)