CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018883
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutaryl-CoA dehydrogenase, mitochondrial 
Protein Synonyms/Alias
 GCD 
Gene Name
 GCDH 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32SSAAQTEKGGRTQSQubiquitination[1]
163GSEEQRQKYLPQLAKubiquitination[1]
202AHYNSSNKSYTLNGTubiquitination[1]
240IRGFLLEKGMRGLSAubiquitination[1]
371PEMVSLLKRNNCGKAubiquitination[1]
377LKRNNCGKALDIARQubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive. 
Sequence Annotation
 NP_BIND 177 186 FAD.
 NP_BIND 212 214 FAD.
 NP_BIND 387 391 FAD (By similarity).
 NP_BIND 416 418 FAD.
 REGION 138 139 Substrate binding.
 REGION 287 294 Substrate binding.
 ACT_SITE 414 414 Proton acceptor (Probable).
 BINDING 186 186 Substrate; via carbonyl oxygen.
 BINDING 319 319 FAD (By similarity).
 BINDING 330 330 FAD (By similarity).
 BINDING 415 415 Substrate; via amide nitrogen.
 BINDING 434 434 FAD; via carbonyl oxygen.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Disease mutation; FAD; Flavoprotein; Glutaricaciduria; Mitochondrion; Oxidoreductase; Polymorphism; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 438 AA 
Protein Sequence
MALRGVSVRL LSRGPGLHVL RTWVSSAAQT EKGGRTQSQL AKSSRPEFDW QDPLVLEEQL 60
TTDEILIRDT FRTYCQERLM PRILLANRNE VFHREIISEM GELGVLGPTI KGYGCAGVSS 120
VAYGLLAREL ERVDSGYRSA MSVQSSLVMH PIYAYGSEEQ RQKYLPQLAK GELLGCFGLT 180
EPNSGSDPSS METRAHYNSS NKSYTLNGTK TWITNSPMAD LFVVWARCED GCIRGFLLEK 240
GMRGLSAPRI QGKFSLRASA TGMIIMDGVE VPEENVLPGA SSLGGPFGCL NNARYGIAWG 300
VLGASEFCLH TARQYALDRM QFGVPLARNQ LIQKKLADML TEITLGLHAC LQLGRLKDQD 360
KAAPEMVSLL KRNNCGKALD IARQARDMLG GNGISDEYHV IRHAMNLEAV NTYEGTHDIH 420
ALILGRAITG IQAFTASK 438 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0000062; F:fatty-acyl-CoA binding; IEA:Compara.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:Compara.
 GO:0004361; F:glutaryl-CoA dehydrogenase activity; EXP:Reactome.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0019395; P:fatty acid oxidation; IEA:Compara.
 GO:0046949; P:fatty-acyl-CoA biosynthetic process; IEA:Compara.
 GO:0006554; P:lysine catabolic process; TAS:Reactome.
 GO:0006568; P:tryptophan metabolic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006089; Acyl-CoA_DH_CS.
 IPR006092; Acyl-CoA_DH_N.
 IPR006090; Acyl-CoA_Oxase/DH_1.
 IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
 IPR009075; AcylCo_DH/oxidase_C.
 IPR013786; AcylCoA_DH/ox_N.
 IPR009100; AcylCoA_DH/oxidase. 
Pfam
 PF00441; Acyl-CoA_dh_1
 PF02770; Acyl-CoA_dh_M
 PF02771; Acyl-CoA_dh_N 
SMART
  
PROSITE
 PS00072; ACYL_COA_DH_1
 PS00073; ACYL_COA_DH_2 
PRINTS