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Protein

Dihydrolipoyl dehydrogenase

Gene

lpdA

Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).By similarity

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 sitei51 – 511FADBy similarity
Binding sitei114 – 1141FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei203 – 2031NADBy similarity
Binding sitei237 – 2371NAD; via amide nitrogenBy similarity
Binding sitei307 – 3071FADBy similarity
Binding sitei315 – 3151FAD; via amide nitrogenBy similarity
Active sitei439 – 4391Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 429FADBy similarity
Nucleotide bindingi180 – 1845NADBy similarity
Nucleotide bindingi264 – 2674NADBy 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
E3 component of 2-oxoglutarate dehydrogenase complex
Gene namesi
Name:lpdA
Ordered Locus Names:CT_557
OrganismiChlamydia trachomatis (strain D/UW-3/Cx)
Taxonomic identifieri272561 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000431 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Dihydrolipoyl dehydrogenasePRO_0000068026Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 47Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi272561.CT557.

Structurei

3D structure databases

ProteinModelPortaliO84561.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
InParanoidiO84561.
KOiK00382.
OMAiVEVMPTI.
OrthoDBiEOG6QCD6D.

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.

O84561-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEAFDCVVI GAGPGGYVAA ITAAQAGLKT ALIEKREAGG TCLNRGCIPS
60 70 80 90 100
KALLAGAEVV TQIRHADQFG IHVEGFSINY PAMVQRKDSV VRSIRDGLNG
110 120 130 140 150
LIRSNKITVF SGRGSLISST EVKILGENPS VIKAHSIILA TGSEPRAFPG
160 170 180 190 200
IPFSAESPRI LCSTGVLNLK EIPQKMAIIG GGVIGCEFAS LFHTLGSEVS
210 220 230 240 250
VIEASSQILA LNNPDISKTM FDKFTRQGLR FVLEASVSNI EDIGDRVRLT
260 270 280 290 300
INGNVEEYDY VLVSIGRRLN TENIGLDKAG VICDERGVIP TDATMRTNVP
310 320 330 340 350
NIYAIGDITG KWQLAHVASH QGIIAARNIA GHKEEIDYSA VPSVIFTFPE
360 370 380 390 400
VASVGLSPTA AQQQKIPVKV TKFPFRAIGK AVAMGEADGF AAIISHETTQ
410 420 430 440 450
QILGAYVIGP HASSLISEIT LAVRNELTLP CIYETIHAHP TLAEVWAESA
460
LLAVDTPLHM PPAKK
Length:465
Mass (Da):49,491
Last modified:November 1, 1998 - v1
Checksum:i56449CCD2AB61477
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001273 Genomic DNA. Translation: AAC68159.1.
PIRiE71500.
RefSeqiNP_220072.1. NC_000117.1.
WP_009871921.1. NC_000117.1.

Genome annotation databases

EnsemblBacteriaiAAC68159; AAC68159; CT_557.
GeneIDi884341.
KEGGictr:CT_557.
PATRICi20380724. VBIChlTra43535_0608.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001273 Genomic DNA. Translation: AAC68159.1.
PIRiE71500.
RefSeqiNP_220072.1. NC_000117.1.
WP_009871921.1. NC_000117.1.

3D structure databases

ProteinModelPortaliO84561.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272561.CT557.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC68159; AAC68159; CT_557.
GeneIDi884341.
KEGGictr:CT_557.
PATRICi20380724. VBIChlTra43535_0608.

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
InParanoidiO84561.
KOiK00382.
OMAiVEVMPTI.
OrthoDBiEOG6QCD6D.

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. "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
    Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
    Science 282:754-759(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: D/UW-3/Cx.

Entry informationi

Entry nameiDLDH_CHLTR
AccessioniPrimary (citable) accession number: O84561
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: November 11, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.