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Protein

Dihydrolipoyl dehydrogenase

Gene

LPD

Organism
Trypanosoma cruzi
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei59 – 591FADBy similarity
Binding sitei124 – 1241FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei213 – 2131NADBy similarity
Binding sitei248 – 2481NAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei282 – 2821NAD; via amide nitrogenBy similarity
Binding sitei323 – 3231FADBy similarity
Active sitei456 – 4561Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 5010FADBy similarity
Nucleotide bindingi153 – 1553FADBy similarity
Nucleotide bindingi190 – 1978NADBy similarity
Nucleotide bindingi330 – 3334FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

FAD, Flavoprotein, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
Gene namesi
Name:LPD
OrganismiTrypanosoma cruzi
Taxonomic identifieri5693 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Dihydrolipoyl dehydrogenasePRO_0000068009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 55Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP90597.
PRIDEiP90597.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi353153.XP_812294.1.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 176Combined sources
Helixi21 – 3212Combined sources
Beta strandi37 – 4711Combined sources
Helixi48 – 536Combined sources
Helixi55 – 7319Combined sources
Helixi75 – 784Combined sources
Helixi83 – 853Combined sources
Helixi90 – 11526Combined sources
Beta strandi118 – 12811Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi141 – 15111Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi167 – 1715Combined sources
Helixi173 – 1775Combined sources
Beta strandi184 – 1896Combined sources
Helixi193 – 20412Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi214 – 2196Combined sources
Helixi224 – 23714Combined sources
Beta strandi241 – 2433Combined sources
Beta strandi247 – 2537Combined sources
Beta strandi255 – 2639Combined sources
Beta strandi269 – 27911Combined sources
Beta strandi283 – 2853Combined sources
Helixi292 – 2954Combined sources
Beta strandi318 – 3203Combined sources
Helixi322 – 3243Combined sources
Beta strandi325 – 3284Combined sources
Helixi332 – 34615Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi364 – 3729Combined sources
Helixi375 – 3806Combined sources
Beta strandi385 – 3917Combined sources
Helixi392 – 3943Combined sources
Helixi396 – 4005Combined sources
Beta strandi407 – 4137Combined sources
Turni414 – 4163Combined sources
Beta strandi418 – 4269Combined sources
Helixi429 – 44113Combined sources
Helixi446 – 4505Combined sources
Helixi460 – 47112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QAEX-ray1.90A/B10-477[»]
ProteinModelPortaliP90597.
SMRiP90597. Positions 10-477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP90597.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG1335. Eukaryota.
COG1249. LUCA.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P90597-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRRCAVKLN PYDVVVIGGG PGGYVASIKA AQLGMKTACV EKRGALGGTC
60 70 80 90 100
LNVGCIPSKA LLHATHVYHD AHANFARYGL MGGEGVTMDS AKMQQQKERA
110 120 130 140 150
VKGLTGGVEY LFKKNKVTYY KGEGSFETAH SIRVNGLDGK QEMFETKKTI
160 170 180 190 200
IATGSEPTEL PFLPFDEKVV LSSTGALALP RVPKTMVVIG GGVIGLELGS
210 220 230 240 250
VWARLGAKVT VVEFAPRCAP TLDEDVTNAL VGALAKNEKM KFMTSTKVVG
260 270 280 290 300
GTNNGDSVSL EVEGKNGKRE TVTCEALLVS VGRRPFTGGL GLDKINVAKN
310 320 330 340 350
ERGFVKIGDH FETSIPDVYA IGDVVDKGPM LAHKAEDEGV ACAEILAGKP
360 370 380 390 400
GHVNYGVIPA VIYTMPEVAS VGKSEEELKK EGVAYKVGKF PFNANSRAKA
410 420 430 440 450
VSTEDGFVKV LVDKATDRIL GVHIVCTTAG ELIGEACLAM EYGASSEDVG
460 470
RTCHAHPTMS EALKEACMAL VAKTINF
Length:477
Mass (Da):50,491
Last modified:May 1, 1997 - v1
Checksum:i3A02415DFAB7E0EA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671V → L in allele 1 and allele 2.
Natural varianti144 – 1441F → L in allele 1 and allele 2.
Natural varianti208 – 2081K → E in allele 1 and allele 2.
Natural varianti256 – 2561D → G in allele 1.
Natural varianti268 – 2681K → R in allele 2.
Natural varianti376 – 3761E → D in allele 1 and allele 2.
Natural varianti474 – 4741T → S in allele 1 and allele 2.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89112 mRNA. Translation: CAA61483.1.
Y11262 Genomic DNA. Translation: CAA72132.1.
Y11261 Genomic DNA. Translation: CAA72131.1.
PIRiS13863.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89112 mRNA. Translation: CAA61483.1.
Y11262 Genomic DNA. Translation: CAA72132.1.
Y11261 Genomic DNA. Translation: CAA72131.1.
PIRiS13863.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QAEX-ray1.90A/B10-477[»]
ProteinModelPortaliP90597.
SMRiP90597. Positions 10-477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi353153.XP_812294.1.

Proteomic databases

PaxDbiP90597.
PRIDEiP90597.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1335. Eukaryota.
COG1249. LUCA.

Miscellaneous databases

EvolutionaryTraceiP90597.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: Y.

Entry informationi

Entry nameiDLDH_TRYCR
AccessioniPrimary (citable) accession number: P90597
Secondary accession number(s): P90598, P90599
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1997
Last modified: November 11, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.