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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

Miscellaneous

The active site is a redox-active disulfide bond.

Catalytic activityi

Protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei51FADBy similarity1
Binding sitei114FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei203NADBy similarity1
Binding sitei237NAD; via amide nitrogenBy similarity1
Binding sitei307FADBy similarity1
Binding sitei315FAD; via amide nitrogenBy similarity1
Active sitei439Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi34 – 42FADBy similarity9
Nucleotide bindingi180 – 184NADBy similarity5
Nucleotide bindingi264 – 267NADBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandFAD, 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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680261 – 465Dihydrolipoyl dehydrogenaseAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi42 ↔ 47Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliO84561.
SMRiO84561.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
InParanoidiO84561.
KOiK00382.
OMAiTMSEAVM.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 3 hits.
InterProiView protein in InterPro
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR001100. Pyr_nuc-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
PfamiView protein in Pfam
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
PIRSFiPIRSF000350. Mercury_reductase_MerA. 1 hit.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiView protein in PROSITE
PS00076. PYRIDINE_REDOX_1. 1 hit.

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.
PATRICifig|272561.5.peg.608.

Similar proteinsi

Entry informationi

Entry nameiDLDH_CHLTR
AccessioniPrimary (citable) accession number: O84561
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: September 27, 2017
This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families