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Annotation rule MF_00051 |
General rule information
[?]
Accession |
MF_00051 |
Dates |
1-JUN-2001 (Created) 20-NOV-2019 (Last updated, Version 55) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Bacteria> or <OC:Methanomicrobia> or <OC:Halobacteria>
Protein name |
RecName:
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Full=Serine hydroxymethyltransferase;
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Short=SHMT;
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Short=Serine methylase;
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EC 2.1.2.1;
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else
Protein name |
RecName:
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Full=Serine hydroxymethyltransferase;
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Short=SHMT;
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Short=Serine methylase;
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EC 2.1.2.-;
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|
end case
case <OC:Bacteria>
Function |
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. |
Catalytic activity |
RHEA:15481: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
EC 2.1.2.1
|
else case <OC:Methanomicrobia> or <OC:Halobacteria>
Function |
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. |
Catalytic activity |
RHEA:15481: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
EC 2.1.2.1
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else case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanopyri> or <OC:Archaeoglobi>
Function |
Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. |
Catalytic activity |
RHEA:47104: 5,10-methylenetetrahydromethanopterin + glycine + H2O = 5,6,7,8-tetrahydromethanopterin + L-serine
|
else
Function |
Catalyzes the reversible interconversion of serine and glycine with a modified folate serving as the one-carbon carrier. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. |
end case
case <OC:Bacteria> or <OC:Methanomicrobia> or <OC:Halobacteria>
Pathway |
One-carbon metabolism; tetrahydrofolate interconversion. |
end case
Pathway |
Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. |
Subunit |
Homodimer. |
Subcellular location |
Cytoplasm. |
Similarity |
Belongs to the SHMT family. |
case <FTTag:acetylation>
end case
GO:0004372; Molecular function: glycine hydroxymethyltransferase activity.
GO:0030170; Molecular function: pyridoxal phosphate binding.
GO:0006730; Biological process: one-carbon metabolic process.
GO:0019264; Biological process: glycine biosynthetic process from serine.
GO:0005737; Cellular component: cytoplasm.
From: GLYA_ECOLI (P0A825) |
Key
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From
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To
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Description
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|
Tag
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|
Condition
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FTGroup
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REGION
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|
125
|
|
127
|
|
Substrate binding
|
|
|
|
G-x-[IL]
|
|
|
REGION (Optional)
|
|
355
|
|
357
|
|
Substrate binding
|
|
|
|
[ST]-x-F
|
|
|
BINDING (Optional)
|
|
35
|
|
35
|
|
Pyridoxal phosphate
|
|
|
|
S
|
|
|
BINDING
|
|
55
|
|
55
|
|
Pyridoxal phosphate
|
|
|
|
Y
|
|
|
BINDING
|
|
57
|
|
57
|
|
Substrate
|
|
|
|
E
|
|
|
BINDING
|
|
64
|
|
64
|
|
Substrate
|
|
|
|
[FY]
|
|
|
BINDING
|
|
65
|
|
65
|
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Pyridoxal phosphate
|
|
|
|
Y
|
|
|
BINDING (Optional)
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|
99
|
|
99
|
|
Pyridoxal phosphate
|
|
|
|
[ST]
|
|
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BINDING
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|
121
|
|
121
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Substrate; via carbonyl oxygen
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|
|
|
L
|
|
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BINDING
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|
175
|
|
175
|
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Pyridoxal phosphate
|
|
|
|
[ST]
|
|
|
BINDING
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|
203
|
|
203
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|
Pyridoxal phosphate
|
|
|
|
H
|
|
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BINDING (Optional)
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228
|
|
228
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|
Pyridoxal phosphate
|
|
|
|
H
|
|
|
BINDING (Optional)
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235
|
|
235
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Pyridoxal phosphate
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|
|
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R
|
|
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BINDING (Optional)
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263
|
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263
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Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen
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|
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G
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BINDING
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363
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363
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Pyridoxal phosphate
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R
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MOD_RES
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229
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229
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N6-(pyridoxal phosphate)lysine
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K
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case <OC:Escherichia> or <OC:Shigella>
MOD_RES
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54
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54
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N6-acetyllysine
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acetylation
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K
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MOD_RES
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250
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250
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N6-acetyllysine
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acetylation
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K
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MOD_RES
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285
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285
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N6-acetyllysine
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acetylation
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K
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MOD_RES
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354
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354
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N6-acetyllysine
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acetylation
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K
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MOD_RES
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375
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375
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N6-acetyllysine
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acetylation
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K
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end case
Additional information
[?]
Size range |
406-574 amino acids |
Related rules |
None |
Fusion |
None |
Comments |
The pteridine substrate used in this reaction by Archaea differs depending on the species. Methanomicrobia and Halobacteria appear to use tetrahydrofolate, whereas Methanobacteria and Methanococci use tetrahydromethanopterin, Sulfolobus solfataricus use tetrahydrosulfopterin, and hyperthermophiles use a modified folate (see PMID: 9783425 and references mentioned in template entries). M.tuberculosis possesses 2 SHMTs, one (O53441, Rv1093) binds 1 pyridoxal phosphate per homodimer whereas the other (O53615, Rv0070c) binds 1 pyridoxal phosphate per subunit like other characterized members of the SHMT family. Possible wrong start in ARCFU. Possible C-terminal problem in TREPA. |