CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-026172
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydrolipoyl dehydrogenase 
Protein Synonyms/Alias
  
Gene Name
 TTHA0287 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) 
NCBI Taxa ID
 300852 
Lysine Modification
Position
Peptide
Type
References
367GIPYKVGKFPYSASGacetylation[1]
Reference
 [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus.
 Okanishi H, Kim K, Masui R, Kuramitsu S.
 J Proteome Res. 2013 Aug 1;. [PMID: 23901841] 
Functional Description
  
Sequence Annotation
 NP_BIND 11 12 FAD.
 NP_BIND 31 32 FAD.
 NP_BIND 39 44 FAD.
 NP_BIND 177 178 NAD.
 NP_BIND 197 198 NAD.
 NP_BIND 308 310 FAD.
 BINDING 49 49 FAD.
 BINDING 111 111 FAD; via amide nitrogen and carbonyl
 BINDING 231 231 NAD; via amide nitrogen and carbonyl
 BINDING 302 302 FAD.
 BINDING 339 339 NAD; via carbonyl oxygen.
 BINDING 396 396 Phosphate.
 BINDING 421 421 Phosphate.
 BINDING 434 434 FAD; via carbonyl oxygen.  
Keyword
 3D-structure; Complete proteome; FAD; Flavoprotein; NAD; Nucleotide-binding; Oxidoreductase; Redox-active center; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 455 AA 
Protein Sequence
MYDLLVIGAG PGGYVAAIRA AQLGMKVGVV EKEKALGGTC LRVGCIPSKA LLETTERIYE 60
AKKGLLGAKV KGVELDLPAL MAHKDKVVQA NTQGVEFLFK KNGIARHQGT ARFLSERKVL 120
VEETGEELEA RYILIATGSA PLIPPWAQVD YERVVTSTEA LSFPEVPKRL IVVGGGVIGL 180
ELGVVWHRLG AEVIVLEYMD RILPTMDLEV SRAAERVFKK QGLTIRTGVR VTAVVPEAKG 240
ARVELEGGEV LEADRVLVAV GRRPYTEGLS LENAGLSTDE RGRIPVDEHL RTRVPHIYAI 300
GDVVRGPMLA HKASEEGIAA VEHMVRGFGH VDYQAIPSVV YTHPEIAAVG YTEEELKAQG 360
IPYKVGKFPY SASGRARAMG ETEGFIKVLA HAKTDRILGV HGIGARVGDV LAEAALALFF 420
KASAEDLGRA PHAHPSLSEI LKEAALAAWE RPIHL 455 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:EC.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro. 
Interpro
 IPR016156; FAD/NAD-linked_Rdtase_dimer.
 IPR013027; FAD_pyr_nucl-diS_OxRdtase.
 IPR006258; Lipoamide_DH.
 IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
 IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
 IPR012999; Pyr_OxRdtase_I_AS.
 IPR001327; Pyr_OxRdtase_NAD-bd_dom. 
Pfam
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2
 PF02852; Pyr_redox_dim 
SMART
  
PROSITE
 PS00076; PYRIDINE_REDOX_1 
PRINTS
 PR00368; FADPNR.