 |
|
| HAMAP annotation rule: MF_00051 |
| Accession |
MF_00051 |
| Dates |
1-JUN-2001 (Created) 5-DEC-2011 (Last updated, Version 41) |
| Protein name |
| RecName: |
Full=Pyridoxal-phosphate-dependent serine hydroxymethyltransferase; Short=SHMT; Short=Serine methylase; EC=2.1.2.1; |
|
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.
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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