CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003204
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 D-3-phosphoglycerate dehydrogenase 
Protein Synonyms/Alias
 PGDH 
Gene Name
 serA 
Gene Synonyms/Alias
 b2913; JW2880 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
8MAKVSLEKDKIKFLLacetylation[1]
10KVSLEKDKIKFLLVEacetylation[1]
12SLEKDKIKFLLVEGVacetylation[1]
22LVEGVHQKALESLRAacetylation[1]
39YTNIEFHKGALDDEQacetylation[1, 2, 3]
48ALDDEQLKESIRDAHacetylation[1]
141AHRGVWNKLAAGSFEacetylation[1]
218VPENPSTKNMMGAKEacetylation[1]
224TKNMMGAKEISLMKPacetylation[1]
230AKEISLMKPGSLLINacetylation[1]
314EVAGKLIKYSDNGSTacetylation[1]
398EKALQAMKAIPGTIRacetylation[1, 3]
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] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] 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
  
Sequence Annotation
 DOMAIN 339 410 ACT.
 NP_BIND 161 162 NAD (By similarity).
 NP_BIND 238 240 NAD (By similarity).
 NP_BIND 292 295 NAD (By similarity).
 ACT_SITE 240 240
 ACT_SITE 269 269
 ACT_SITE 292 292 Proton donor.
 BINDING 181 181 NAD (By similarity).
 BINDING 264 264 NAD (By similarity).  
Keyword
 3D-structure; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; NAD; Oxidoreductase; Reference proteome; Serine biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 410 AA 
Protein Sequence
MAKVSLEKDK IKFLLVEGVH QKALESLRAA GYTNIEFHKG ALDDEQLKES IRDAHFIGLR 60
SRTHLTEDVI NAAEKLVAIG CFCIGTNQVD LDAAAKRGIP VFNAPFSNTR SVAELVIGEL 120
LLLLRGVPEA NAKAHRGVWN KLAAGSFEAR GKKLGIIGYG HIGTQLGILA ESLGMYVYFY 180
DIENKLPLGN ATQVQHLSDL LNMSDVVSLH VPENPSTKNM MGAKEISLMK PGSLLINASR 240
GTVVDIPALC DALASKHLAG AAIDVFPTEP ATNSDPFTSP LCEFDNVLLT PHIGGSTQEA 300
QENIGLEVAG KLIKYSDNGS TLSAVNFPEV SLPLHGGRRL MHIHENRPGV LTALNKIFAE 360
QGVNIAAQYL QTSAQMGYVV IDIEADEDVA EKALQAMKAI PGTIRARLLY 410 
Gene Ontology
 GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; IDA:EcoCyc.
 GO:0016597; F:amino acid binding; IEA:InterPro.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0004617; F:phosphoglycerate dehydrogenase activity; IDA:EcoCyc.
 GO:0006564; P:L-serine biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR002912; ACT_dom.
 IPR006139; D-isomer_2_OHA_DH_cat_dom.
 IPR006140; D-isomer_2_OHA_DH_NAD-bd.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF00389; 2-Hacid_dh
 PF02826; 2-Hacid_dh_C
 PF01842; ACT 
SMART
  
PROSITE
 PS51671; ACT
 PS00065; D_2_HYDROXYACID_DH_1
 PS00670; D_2_HYDROXYACID_DH_2
 PS00671; D_2_HYDROXYACID_DH_3 
PRINTS