CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006276
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycine dehydrogenase [decarboxylating] 
Protein Synonyms/Alias
 Glycine cleavage system P-protein; Glycine decarboxylase 
Gene Name
 gcvP 
Gene Synonyms/Alias
 b2903; JW2871 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
290HAAFFAAKDEYKRSMacetylation[1]
294FAAKDEYKRSMPGRIacetylation[1]
306GRIIGVSKDAAGNTAacetylation[1, 2]
454LDIDTLDKDVAHDSRacetylation[1]
823ILDIRPLKEETGISEacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 
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. 
Sequence Annotation
 MOD_RES 708 708 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Complete proteome; Direct protein sequencing; Oxidoreductase; Pyridoxal phosphate; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 957 AA 
Protein Sequence
MTQTLSQLEN SGAFIERHIG PDAAQQQEML NAVGAQSLNA LTGQIVPKDI QLATPPQVGA 60
PATEYAALAE LKAIASRNKR FTSYIGMGYT AVQLPPVILR NMLENPGWYT AYTPYQPEVS 120
QGRLEALLNF QQVTLDLTGL DMASASLLDE ATAAAEAMAM AKRVSKLKNA NRFFVASDVH 180
PQTLDVVRTR AETFGFEVIV DDAQKVLDHQ DVFGVLLQQV GTTGEIHDYT ALISELKSRK 240
IVVSVAADIM ALVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFAAK DEYKRSMPGR 300
IIGVSKDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV YHGPVGLKRI 360
ANRIHRLTDI LAAGLQQKGL KLRHAHYFDT LCVEVADKAG VLTRAEAAEI NLRSDILNAV 420
GITLDETTTR ENVMQLFNVL LGDNHGLDID TLDKDVAHDS RSIQPAMLRD DEILTHPVFN 480
RYHSETEMMR YMHSLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF AELHPFCPPE 540
QAEGYQQMIA QLADWLVKLT GYDAVCMQPN SGAQGEYAGL LAIRHYHESR NEGHRDICLI 600
PASAHGTNPA SAHMAGMQVV VVACDKNGNI DLTDLRAKAE QAGDNLSCIM VTYPSTHGVY 660
EETIREVCEV VHQFGGQVYL DGANMNAQVG ITSPGFIGAD VSHLNLHKTF CIPHGGGGPG 720
MGPIGVKAHL APFVPGHSVV QIEGMLTRQG AVSAAPFGSA SILPISWMYI RMMGAEGLKK 780
ASQVAILNAN YIASRLQDAF PVLYTGRDGR VAHECILDIR PLKEETGISE LDIAKRLIDY 840
GFHAPTMSFP VAGTLMVEPT ESESKVELDR FIDAMLAIRA EIDQVKAGVW PLEDNPLVNA 900
PHIQSELVAE WAHPYSREVA VFPAGVADKY WPTVKRLDDV YGDRNLFCSC VPISEYQ 957 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IDA:EcoCyc.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:HAMAP. 
Interpro
 IPR020580; GDC-P_N.
 IPR020581; GDC_P.
 IPR003437; GDC_P_homo.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1. 
Pfam
 PF02347; GDC-P 
SMART
  
PROSITE
  
PRINTS