Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei59FADBy similarity1
Binding sitei124FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei213NADBy similarity1
Binding sitei248NAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei282NAD; via amide nitrogenBy similarity1
Binding sitei323FADBy similarity1
Active sitei456Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi41 – 50FADBy similarity10
Nucleotide bindingi153 – 155FADBy similarity3
Nucleotide bindingi190 – 197NADBy similarity8
Nucleotide bindingi330 – 333FADBy similarity4

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000680091 – 477Dihydrolipoyl dehydrogenaseAdd BLAST477

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 17Combined sources6
Helixi21 – 32Combined sources12
Beta strandi37 – 47Combined sources11
Helixi48 – 53Combined sources6
Helixi55 – 73Combined sources19
Helixi75 – 78Combined sources4
Helixi83 – 85Combined sources3
Helixi90 – 115Combined sources26
Beta strandi118 – 128Combined sources11
Beta strandi131 – 136Combined sources6
Beta strandi141 – 151Combined sources11
Beta strandi155 – 157Combined sources3
Beta strandi167 – 171Combined sources5
Helixi173 – 177Combined sources5
Beta strandi184 – 189Combined sources6
Helixi193 – 204Combined sources12
Beta strandi208 – 212Combined sources5
Beta strandi214 – 219Combined sources6
Helixi224 – 237Combined sources14
Beta strandi241 – 243Combined sources3
Beta strandi247 – 253Combined sources7
Beta strandi255 – 263Combined sources9
Beta strandi269 – 279Combined sources11
Beta strandi283 – 285Combined sources3
Helixi292 – 295Combined sources4
Beta strandi318 – 320Combined sources3
Helixi322 – 324Combined sources3
Beta strandi325 – 328Combined sources4
Helixi332 – 346Combined sources15
Beta strandi360 – 362Combined sources3
Beta strandi364 – 372Combined sources9
Helixi375 – 380Combined sources6
Beta strandi385 – 391Combined sources7
Helixi392 – 394Combined sources3
Helixi396 – 400Combined sources5
Beta strandi407 – 413Combined sources7
Turni414 – 416Combined sources3
Beta strandi418 – 426Combined sources9
Helixi429 – 441Combined sources13
Helixi446 – 450Combined sources5
Helixi460 – 471Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QAEX-ray1.90A/B10-477[»]
ProteinModelPortaliP90597.
SMRiP90597.
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)DescriptionActionsGraphical viewLength
Natural varianti67V → L in allele 1 and allele 2. 1
Natural varianti144F → L in allele 1 and allele 2. 1
Natural varianti208K → E in allele 1 and allele 2. 1
Natural varianti256D → G in allele 1. 1
Natural varianti268K → R in allele 2. 1
Natural varianti376E → D in allele 1 and allele 2. 1
Natural varianti474T → S in allele 1 and allele 2. 1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QAEX-ray1.90A/B10-477[»]
ProteinModelPortaliP90597.
SMRiP90597.
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...

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 2, 2016
This is version 94 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.