CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018481
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycine dehydrogenase [decarboxylating], mitochondrial 
Protein Synonyms/Alias
 Glycine cleavage system P protein; Glycine decarboxylase 
Gene Name
 Gldc 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
78RHIGPGDKDRREMLQacetylation[1, 2]
111IRLKRPLKMEDPICEacetylation[1, 2]
342HAAFFAVKENLVRMMacetylation[1]
414QGLKHIAKRVHNATLacetylation[1]
452VQCGCSVKEVLGRAAacetylation[1, 2, 3, 4]
519GLLGSSFKRTSPFLTacetylation[1, 2, 3, 4, 5]
519GLLGSSFKRTSPFLTubiquitination[6]
641IRAYLDQKGERHRTVacetylation[1, 2, 4]
641IRAYLDQKGERHRTVubiquitination[6]
653RTVCLIPKSAHGTNPacetylation[4]
669SAHMAGMKIQPVEVDacetylation[2, 4]
687NIDVAHLKAMVDQHKacetylation[1, 2]
832MMGGKGLKEATEIAIacetylation[1]
832MMGGKGLKEATEIAIubiquitination[6]
847LNANYMAKRLEKHYRacetylation[2]
876ILDTRPFKKSANVEAacetylation[2]
877LDTRPFKKSANVEAVubiquitination[6]
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] 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]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] 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]
 [5] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity). 
Sequence Annotation
 MOD_RES 759 759 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Complete proteome; Direct protein sequencing; Mitochondrion; Oxidoreductase; Pyridoxal phosphate; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1025 AA 
Protein Sequence
MQLCARAWGL RLGRGAGGGH RLARGTGLSW AQRSRDSSGG GGGGGGGDRG AAGASRLLER 60
LLPRHDDFSR RHIGPGDKDR REMLQALGLA SIDELIEKTV PASIRLKRPL KMEDPICENE 120
ILETLHAIAS KNQIWRSYIG MGYYNCSVPQ TILRNLLENS GWVTQYTPYQ PEVSQGRLES 180
LLNYQTMVSD ITGLDMANAS LLDEATAAAE AMQLCHRHNK RKKFFVDPRC HPQTIAVVQT 240
RAKYRGVLVE LKLPHEMDFS GKDVCGVLFQ YPDTEGKVED FTELVDRAHQ TGSLTCCATD 300
LLALCILRPP GEFGVDIALG NSQRFGVPLG YGGPHAAFFA VKENLVRMMP GRMVGVTRDA 360
TGKEVYRLAL QTREQHIRRD KATSNICTAQ ALLANMAAMF AIYHGSQGLK HIAKRVHNAT 420
LILSEGLKRA GHQLQHDLFF DTLKVQCGCS VKEVLGRAAQ RQINFRLFDD GTLGISLDET 480
VTEKDLDDLL WIFGCESSAE LVAEGMGEER RGLLGSSFKR TSPFLTHQVF NSYHSETNLV 540
RYMKKLENKD ISLVHSMIPL GSCTMKLNSS SELAPITWRE FANIHPFVPL DQAQGYQQLF 600
QGLEKDLCEI TGYDRVSFQP NSGAQGEYAG LATIRAYLDQ KGERHRTVCL IPKSAHGTNP 660
ASAHMAGMKI QPVEVDRYGN IDVAHLKAMV DQHKENLAAI MITYPSTNGV FEENIGDVCA 720
LIHQHGGQVY LDGANMNAQV GICRPGDFGS DVSHLNLHKT FCIPHGGGGP GMGPIGVKKH 780
LSPFLPSHPV ISIKPTEGTW PVGTVSAAPW GSSSILPISW AYIKMMGGKG LKEATEIAIL 840
NANYMAKRLE KHYRVLFRGA RGYVAHEFIL DTRPFKKSAN VEAVDVAKRL QDYGFHAPTM 900
SWPVAGTLMI EPTESEDKAE LDRFCDAMIS IRQEIADIEE GRIDPRVNPL KMSPHSLTCV 960
TSSCWDRPYS REVAAFPLPF VKPENKFWPT IARIDDIYGD QHLVCTCPPM EVYESPFSEQ 1020
KRASS 1025 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; ISO:MGI.
 GO:0016829; F:lyase activity; IEA:InterPro.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006546; P:glycine catabolic process; IEA:InterPro. 
Interpro
 IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
 IPR020580; GDC-P_N.
 IPR020581; GDC_P.
 IPR003437; GDC_P_homo.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1. 
Pfam
 PF01212; Beta_elim_lyase
 PF02347; GDC-P 
SMART
  
PROSITE
  
PRINTS