| Tag | Content |
|---|
| CPLM ID | CPLM-015040 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine hydroxymethyltransferase 1 |
Protein Synonyms/Alias | SHMT 1; Serine methylase 1 |
Gene Name | glyA1 |
Gene Synonyms/Alias | RPA2724 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 355 | RAGITCNKNGIPFDP | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
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 135 137 Substrate binding (By similarity).
BINDING 45 45 Pyridoxal phosphate (By similarity).
BINDING 65 65 Pyridoxal phosphate (By similarity).
BINDING 67 67 Substrate (By similarity).
BINDING 74 74 Substrate (By similarity).
BINDING 75 75 Pyridoxal phosphate (By similarity).
BINDING 109 109 Pyridoxal phosphate (By similarity).
BINDING 131 131 Substrate; via carbonyl oxygen (By
BINDING 186 186 Pyridoxal phosphate (By similarity).
BINDING 214 214 Pyridoxal phosphate (By similarity).
BINDING 239 239 Pyridoxal phosphate (By similarity).
BINDING 246 246 Pyridoxal phosphate (By similarity).
BINDING 272 272 Pyridoxal phosphate; via amide nitrogen
BINDING 372 372 Pyridoxal phosphate (By similarity).
MOD_RES 240 240 N6-(pyridoxal phosphate)lysine (By |
Keyword | Amino-acid biosynthesis; Complete proteome; Cytoplasm; One-carbon metabolism; Pyridoxal phosphate; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 432 AA |
Protein Sequence | MSTANPASAP DSFFSASLEQ ADPEIAAAIR GELGRQRHEV ELIASENIVS RAVLEAQGSV 60
MTNKYAEGYP GNRYYGGCEF VDVAENLAID RAKKLFGANF ANVQPNSGSQ MNQAVFLALL 120
QPGDTFMGLD LAAGGHLTHG APVNMSGKWF KPVHYTVRRE DQMIDMDAVA KLAEEAKPKL 180
IIAGGSAYPR AWDFKRFREI ADSVGAYFMV DMAHFAGLVA GGVHASPVPH AHVTTTTTHK 240
SLRGPRGGLI LTNDEALAKK FNSAIFPGLQ GGPLMHVIAA KAVAFKEALQ PDFKVYTKNV 300
VENAKALAET LRSAGFDLVS GGTDNHLMLV DLRPKGLKGN VSEKALVRAG ITCNKNGIPF 360
DPEKPFVTSG LRLGTPAATT RGFGVAEFQQ VGHLIAEVLN AIAQSSDGAA PLVEASVKQR 420
VKELTDRFPI YQ 432 |
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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |