HAMAP annotation rule: MF_00051
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Accession MF_00051
Dates 1-JUN-2001 (Created)
5-DEC-2011 (Last updated, Version 41)
Data class Protein
Names SHMT



Identifier GLYA
Protein name
RecName: Full=Pyridoxal-phosphate-dependent serine hydroxymethyltransferase;
Short=SHMT;
Short=Serine methylase;
EC=2.1.2.1;
Gene name glyA
FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate serving as the one-carbon carrier (By similarity).
CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine.
COFACTOR: Pyridoxal phosphate (By similarity).
PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1.

case <OC:Bacteria>
SUBUNIT: Homodimer (By similarity).
end case

SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the SHMT family.
Pfam PF00464; SHMT; 1;
PROSITE PS00096; SHMT; 1;
PIRSF PIRSF000412; SHMT; 1;

case <FT:18> or <FT:19> or <FT:20> or <FT:21> or <FT:22>
end case

GO:0004372; Molecular function: glycine hydroxymethyltransferase activity.
GO:0006730; Biological process: one-carbon metabolic process.
GO:0009069; Biological process: serine family amino acid metabolic process.
GO:0005737; Cellular component: cytoplasm.
From: GLYA_ECOLI (P0A825)
Key     From     To       Description   Condition   FTGroup
REGION     125     127       Substrate binding (By similarity)   G-X-[IL]  
case <OC:Escherichia> or <OC:Shigella>
Key     From     To       Description   Condition   FTGroup
REGION     355     357       Substrate binding (By similarity)   S-X-F  
end case

Key     From     To       Description   Condition   FTGroup
BINDING (Optional)     35     35       Pyridoxal phosphate (By similarity)   S  
BINDING     55     55       Pyridoxal phosphate (By similarity)   Y  
BINDING     57     57       Substrate (By similarity)   E  
BINDING     64     64       Substrate binding (By similarity)   [FY]  
BINDING     65     65       Pyridoxal phosphate (By similarity)   Y  
BINDING (Optional)     99     99       Pyridoxal phosphate (By similarity)   S  
BINDING     121     121       Substrate (By similarity)   L  
BINDING     175     175       Pyridoxal phosphate (By similarity)   [ST]  
BINDING     203     203       Pyridoxal phosphate (By similarity)   H  
BINDING (Optional)     228     228       Pyridoxal phosphate (By similarity)   H  
BINDING (Optional)     235     235       Pyridoxal phosphate (By similarity)   R  
BINDING (Optional)     263     263       Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen (By similarity)   G  
BINDING     363     363       Pyridoxal phosphate (By similarity)   R  
MOD_RES     229     229       N6-(pyridoxal phosphate)lysine (By similarity)   K  
case <OC:Escherichia> or <OC:Shigella>
Key     From     To       Description   Condition   FTGroup
MOD_RES     54     54       N6-acetyllysine (By similarity)   K  
MOD_RES     250     250       N6-acetyllysine (By similarity)   K  
MOD_RES     285     285       N6-acetyllysine (By similarity)   K  
MOD_RES     354     354       N6-acetyllysine (By similarity)   K  
MOD_RES     375     375       N6-acetyllysine (By similarity)   K  
end case




Size range: 406-574 amino acids
Related UniRules: None
Template: P0A825 (GLYA_ECOLI)
Scope: Bacteria
Archaea
Fusion: Nter: None; Cter: None
Duplicate: in AGRT5, BORBR, BORPA, BURMA, BURP1, BURPS, BURS3, BURTA, COLP3, ERWCT, HAHCH, MYCBO, MYCTU, PHOPR, PSE14, PSEAE, PSEF5, PSEPF, PSEPK, PSESM, PSEU2, CUPPJ, RALSO, RHILO, RHIME, RHOPA, RHORT, SILPO, SULDN, VIBCH, VIBPA, VIBVU, VIBVY
Plasmid encoded: None
Comments: Possible wrong start in ARCFU. Possible C-terminal problem in TREPA.

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