CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024631
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine hydroxymethyltransferase 
Protein Synonyms/Alias
 SHMT; Serine methylase 
Gene Name
 glyA 
Gene Synonyms/Alias
 ECDH10B_2718 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12 / DH10B) 
NCBI Taxa ID
 316385 
Lysine Modification
Position
Peptide
Type
References
62YAEGYPGKRYYGGCEsuccinylation[1]
242RGGLILAKGGSEELYsuccinylation[1]
250GGSEELYKKLNSAVFsuccinylation[1]
277AGKAVALKEAMEPEFsuccinylation[1]
293TYQQQVAKNAKAMVEsuccinylation[1]
331VDKNLTGKEADAALGsuccinylation[1]
346RANITVNKNSVPNDPsuccinylation[1]
354NSVPNDPKSPFVTSGsuccinylation[1]
Reference
 [1] Identification of lysine succinylation as a new post-translational modification.
 Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y.
 Nat Chem Biol. 2011 Jan;7(1):58-63. [PMID: 21151122
Functional Description
 Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF- independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity). 
Sequence Annotation
 REGION 125 127 Substrate binding (By similarity).
 REGION 355 357 Substrate binding (By similarity).
 BINDING 35 35 Pyridoxal phosphate (By similarity).
 BINDING 55 55 Pyridoxal phosphate (By similarity).
 BINDING 57 57 Substrate (By similarity).
 BINDING 64 64 Substrate (By similarity).
 BINDING 65 65 Pyridoxal phosphate (By similarity).
 BINDING 99 99 Pyridoxal phosphate (By similarity).
 BINDING 121 121 Substrate; via carbonyl oxygen (By
 BINDING 175 175 Pyridoxal phosphate (By similarity).
 BINDING 203 203 Pyridoxal phosphate (By similarity).
 BINDING 228 228 Pyridoxal phosphate (By similarity).
 BINDING 235 235 Pyridoxal phosphate (By similarity).
 BINDING 263 263 Pyridoxal phosphate; via amide nitrogen
 BINDING 363 363 Pyridoxal phosphate (By similarity).
 MOD_RES 54 54 N6-acetyllysine (By similarity).
 MOD_RES 229 229 N6-(pyridoxal phosphate)lysine (By
 MOD_RES 250 250 N6-acetyllysine (By similarity).
 MOD_RES 285 285 N6-acetyllysine (By similarity).
 MOD_RES 354 354 N6-acetyllysine (By similarity).
 MOD_RES 375 375 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Amino-acid biosynthesis; Complete proteome; Cytoplasm; One-carbon metabolism; Pyridoxal phosphate; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 417 AA 
Protein Sequence
MLKREMNIAD YDAELWQAME QEKVRQEEHI ELIASENYTS PRVMQAQGSQ LTNKYAEGYP 60
GKRYYGGCEY VDIVEQLAID RAKELFGADY ANVQPHSGSQ ANFAVYTALL EPGDTVLGMN 120
LAHGGHLTHG SPVNFSGKLY NIVPYGIDAT GHIDYADLEK QAKEHKPKMI IGGFSAYSGV 180
VDWAKMREIA DSIGAYLFVD MAHVAGLVAA GVYPNPVPHA HVVTTTTHKT LAGPRGGLIL 240
AKGGSEELYK KLNSAVFPGG QGGPLMHVIA GKAVALKEAM EPEFKTYQQQ VAKNAKAMVE 300
VFLERGYKVV SGGTDNHLFL VDLVDKNLTG KEADAALGRA NITVNKNSVP NDPKSPFVTS 360
GIRVGTPAIT RRGFKEAEAK ELAGWMCDVL DSINDEAVIE RIKGKVLDIC ARYPVYA 417 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:HAMAP.
 GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
 GO:0019264; P:glycine biosynthetic process from serine; IEA:HAMAP.
 GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. 
Interpro
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2.
 IPR001085; Ser_HO-MeTrfase.
 IPR019798; Ser_HO-MeTrfase_PLP_BS. 
Pfam
 PF00464; SHMT 
SMART
  
PROSITE
 PS00096; SHMT 
PRINTS