| Tag | Content |
|---|
| CPLM ID | CPLM-035853 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine hydroxymethyltransferase |
Protein Synonyms/Alias | SHMT; Serine methylase |
Gene Name | glyA |
Gene Synonyms/Alias | EAM_2497 |
Created Date | July 27, 2013 |
Organism | Erwinia amylovora (strain ATCC 49946 / CCPPB 0273 / Ea273 / 27-3) |
NCBI Taxa ID | 716540 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 250 | GGDEDFYKKLNSAVF | acetylation | [1] | | 251 | GDEDFYKKLNSAVFP | acetylation | [1] |
|
Reference | [1] Differential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomics. Wu X, Vellaichamy A, Wang D, Zamdborg L, Kelleher NL, Huber SC, Zhao Y. J Proteomics. 2013 Feb 21;79:60-71. [ PMID: 23234799] |
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 229 229 N6-(pyridoxal phosphate)lysine (By |
Keyword | Amino-acid biosynthesis; Complete proteome; Cytoplasm; Methyltransferase; 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
GKRYYGGCEH VDIVEQLAID RAKELFGADY ANVQPHSGSQ ANFAVYTALL QPGDTILGMS 120
LAHGGHLTHG SPVNLSGKLY NVIAYGIDEN GKIDYNELAE LAKTHRPKMI VGGFSAYSGV 180
CDWAKMREIA DSVGAYLFVD MAHVAGLIAA DVYPNPVPYA HIVTTTTHKT LAGPRGGLIL 240
AKGGDEDFYK KLNSAVFPGS QGGPLMHVIA GKAVAFKEAM EPEFRTYQQQ VAKNAKAMVE 300
VFLQRGYNVV SGGTHNHLFL LDLVDKNLTG KEADAALGRA NITVNKNSVP NDPKSPFVTS 360
GIRIGSPSIT RRGFKEAEVR ELAGWISDIL DNINDEGVSE RVKKQVLDIC ARFPVYA 417 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:HAMAP. GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. 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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |