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Protein

Dihydrolipoyl dehydrogenase

Gene
N/A
Organism
Clostridium magnum
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein predictedi

Functioni

Catalytic activityi

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

Cofactori

FADUniRule annotationNote: Binds 1 FAD per subunit.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Ligandi

FADUniRule annotation, Flavoprotein, NADUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenaseUniRule annotation (EC:1.8.1.4UniRule annotation)
OrganismiClostridium magnumImported
Taxonomic identifieri33954 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Structurei

3D structure databases

ProteinModelPortaliQ59299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 77Lipoyl-bindingInterPro annotationAdd BLAST76

Keywords - Domaini

Redox-active centerUniRule annotation

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR000089. Biotin_lipoyl.
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKIVVMPKL GLTMTEGTLV TWKKAEGDQV KVGEILFEVS TDKLTNEVES
60 70 80 90 100
SDEGIVRKLL VNEGDVVECL NPVAIIGSAD EDISSLLNGS SEGSGSAEQS
110 120 130 140 150
DTKAPKKEVE AVKGGDNLVV IGGGPGGYVA AIRAAQLGAK VTLIEKESLG
160 170 180 190 200
GTCLNVGCIP TKVLLHSSQL LTEMKEGDKL GIDIEGSIVV NWKHIQKRKK
210 220 230 240 250
IVIKKLVSGV SGLLTCNKVK VIKGTAKFES KDTILVTKED GVAEKVNFDN
260 270 280 290 300
AIIATGSMPF IPEIEGNKLS GVIDSTGALS LESNPESIAI IGGGVIGVEF
310 320 330 340 350
ASIFNSLGCK VSIIEMLPHI LPPMDREISE IAKAKLIRDG ININNNCKVT
360 370 380 390 400
RIEQGEDGLK VSFIGDKGEE SIDVEKVLIA VGRRSNIEGL DVEKIGVKTE
410 420 430 440 450
GGSIIVNDKM ETNVEGIYAI GDCTGKIMLA HVASDQGVVA AENIMGQNKK
460 470 480 490 500
MDYKTVPACV YTKPELASVG LTEEQAKEKG IDYKVGKFQL AANGKSLIMN
510 520 530 540 550
ETGGVIKIIT DKKYEEILGV HILGPRATDL ITEAALALRL EATLEEIITT
560 570
VHAHPTVGEA MKEAALAVNN QAIHMMNK
Length:578
Mass (Da):61,342
Last modified:November 1, 1996 - v1
Checksum:i31848A84AE2903E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31844 Genomic DNA. Translation: AAA21748.1.
PIRiI40794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31844 Genomic DNA. Translation: AAA21748.1.
PIRiI40794.

3D structure databases

ProteinModelPortaliQ59299.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR000089. Biotin_lipoyl.
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ59299_9CLOT
AccessioniPrimary (citable) accession number: Q59299
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: December 9, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.UniRule annotation

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.