UniProt Accession

 GLYA_ECOLI; P0A825; P00477 

Genbank Protein ID

 V00283; U00096; AP009048; J01620 

Genbank Nucleotide ID

 CAA23547.1; AAC75604.1; BAA16459.1; AAA23912.1 

Protein Name

 Serine hydroxymethyltransferase 

Protein Synonyms/Alias

 SHMT; Serine methylase 

Gene Name

 glyA 

Gene Synonyms/Alias

 b2551; JW2535 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
23	WQAMEQEKVRQEEHI	acetylation	[1]
54	QGSQLTNKYAEGYPG	acetylation	[1, 2]
62	YAEGYPGKRYYGGCE	acetylation	[1, 3]
160	IDYADLEKQAKEHKP	acetylation	[1]
185	SGVVDWAKMREIADS	acetylation	[1]
242	RGGLILAKGGSEELY	acetylation	[1, 3]
250	GGSEELYKKLNSAVF	acetylation	[1, 2, 3]
251	GSEELYKKLNSAVFP	acetylation	[1, 3]
277	AGKAVALKEAMEPEF	acetylation	[1, 3]
285	EAMEPEFKTYQQQVA	acetylation	[1, 2, 3]
293	TYQQQVAKNAKAMVE	acetylation	[1, 3]
308	VFLERGYKVVSGGTD	acetylation	[1]
326	FLVDLVDKNLTGKEA	acetylation	[1]
331	VDKNLTGKEADAALG	acetylation	[1]
346	RANITVNKNSVPNDP	acetylation	[1, 3]
354	NSVPNDPKSPFVTSG	acetylation	[1, 2, 3]
375	AITRRGFKEAEAKEL	acetylation	[1, 2, 3]
403	EAVIERIKGKVLDIC	acetylation	[1]
405	VIERIKGKVLDICAR	acetylation	[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] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [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

 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. Thus, is able to catalyze the cleavage of allothreonine and 3- phenylserine. Also catalyzes the irreversible conversion of 5,10- methenyltetrahydrofolate to 5-formyltetrahydrofolate. 

Sequence Annotation

 REGION 125 127 Substrate binding.
 REGION 355 357 Substrate binding.
 BINDING 35 35 Pyridoxal phosphate.
 BINDING 55 55 Pyridoxal phosphate.
 BINDING 57 57 Substrate.
 BINDING 64 64 Substrate.
 BINDING 65 65 Pyridoxal phosphate.
 BINDING 99 99 Pyridoxal phosphate.
 BINDING 121 121 Substrate; via carbonyl oxygen.
 BINDING 175 175 Pyridoxal phosphate.
 BINDING 203 203 Pyridoxal phosphate.
 BINDING 228 228 Pyridoxal phosphate.
 BINDING 235 235 Pyridoxal phosphate.
 BINDING 246 246 Substrate.
 BINDING 263 263 Pyridoxal phosphate; via amide nitrogen
 BINDING 363 363 Pyridoxal phosphate.
 MOD_RES 54 54 N6-acetyllysine.
 MOD_RES 62 62 N6-succinyllysine.
 MOD_RES 229 229 N6-(pyridoxal phosphate)lysine.
 MOD_RES 242 242 N6-succinyllysine.
 MOD_RES 250 250 N6-acetyllysine; alternate.
 MOD_RES 250 250 N6-succinyllysine; alternate.
 MOD_RES 277 277 N6-succinyllysine.
 MOD_RES 285 285 N6-acetyllysine.
 MOD_RES 293 293 N6-succinyllysine.
 MOD_RES 331 331 N6-succinyllysine.
 MOD_RES 346 346 N6-succinyllysine.
 MOD_RES 354 354 N6-acetyllysine; alternate.
 MOD_RES 354 354 N6-succinyllysine; alternate.
 MOD_RES 375 375 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Amino-acid biosynthesis; Complete proteome; Cytoplasm; Direct protein sequencing; One-carbon metabolism; Pyridoxal phosphate; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 417 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0004372; F:glycine hydroxymethyltransferase activity; IDA:EcoCyc.
 GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0019264; P:glycine biosynthetic process from serine; IDA:EcoCyc.
 GO:0006546; P:glycine catabolic process; IMP:EcoCyc.
 GO:0006565; P:L-serine catabolic process; IDA:EcoCyc.
 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