CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014249
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
51SRPVFDWKDPLILEEacetylation[1]
65EQLTADEKLIRDTFRacetylation[2, 3]
163GSEEQRQKYLPGLAKacetylation[2]
170KYLPGLAKGELLGCFacetylation[3]
240IRGFILEKGMRGLSAacetylation[1, 2, 3, 4]
240IRGFILEKGMRGLSAsuccinylation[4]
253SAPRIEGKFSLRASAacetylation[2]
334ARNQLVQKKLADMLTacetylation[3]
357CLQLGRLKDQDKATPacetylation[1, 3]
361GRLKDQDKATPEMVSacetylation[1, 3]
371PEMVSMLKRNNCGKAacetylation[1, 3]
438IQAFTVGK*******acetylation[3]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
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. 
Sequence Annotation
 NP_BIND 177 186 FAD (By similarity).
 NP_BIND 177 180 FAD (By similarity).
 NP_BIND 212 214 FAD (By similarity).
 NP_BIND 387 391 FAD (By similarity).
 NP_BIND 416 418 FAD (By similarity).
 REGION 138 139 Substrate binding (By similarity).
 REGION 287 294 Substrate binding (By similarity).
 ACT_SITE 414 414 Proton acceptor (By similarity).
 BINDING 186 186 FAD (By similarity).
 BINDING 186 186 Substrate; via carbonyl oxygen (By
 BINDING 294 294 Substrate (By similarity).
 BINDING 319 319 FAD (By similarity).
 BINDING 330 330 FAD (By similarity).
 BINDING 415 415 Substrate; via amide nitrogen (By
 BINDING 416 416 FAD (By similarity).
 BINDING 434 434 FAD; via carbonyl oxygen (By similarity).  
Keyword
 Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 438 AA 
Protein Sequence
MSLRGVSARL LSRRSGLRFP RFPRTWSSAA AHTEKTQIRP AKSSRPVFDW KDPLILEEQL 60
TADEKLIRDT FRNYCQERLM SRILLANRNE VFHRDIVYEM GELGVLGPTI KGYGCAGVSS 120
VAYGLLTREL ERVDSGYRSM MSVQSSLVMH PIYTYGSEEQ RQKYLPGLAK GELLGCFGLT 180
EPNHGSDPGG METRARHNPS NQSYTLSGTK TWITNSPVAD LFIVWARCED NCIRGFILEK 240
GMRGLSAPRI EGKFSLRASA TGMIIMDSVE VPEENVLPNV SSLAGPFGCL NTARYGITWG 300
VLGAAEFCLH TARQYALDRI QFGVPLARNQ LVQKKLADML TEITLGLHAC LQLGRLKDQD 360
KATPEMVSML KRNNCGKALD IARQARDILG GNGISDEYHV IRHAMNLEAV NTYEGTHDIH 420
ALILGRAITG IQAFTVGK 438 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 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; IEA:Compara.
 GO:0019395; P:fatty acid oxidation; IEA:Compara.
 GO:0046949; P:fatty-acyl-CoA biosynthetic process; IEA:Compara.
 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