P37292

PR
Gene name
SHM1 (SHMT1, YBR263W, YBR1732)
Protein name
Serine hydroxymethyltransferase, mitochondrial
Names
SHMT, Glycine hydroxymethyltransferase, Serine methylase
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YBR263W
EC number
2.1.2.1: Hydroxymethyl-, formyl- and related transferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-57 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P37292

Entry ID Method Resolution Chain Position Source
AF-P37292-F1 Predicted AlphaFoldDB

5 variants for P37292

Variant ID(s) Position Change Description Diseaes Association Provenance
s02-736269 4 R>K No SGRP
s02-736421 55 I>V No SGRP
s02-736610 118 W>G No SGRP
s02-736871 205 V>L No SGRP
s02-736941 228 G>E No SGRP

No associated diseases with P37292

2 regional properties for P37292

Type Name Position InterPro Accession
binding_site Serine hydroxymethyltransferase, pyridoxal phosphate binding site 257 - 273 IPR019798
domain Serine hydroxymethyltransferase-like domain 34 - 432 IPR039429

Functions

Description
EC Number 2.1.2.1 Hydroxymethyl-, formyl- and related transferases
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

4 GO annotations of molecular function

Name Definition
glycine hydroxymethyltransferase activity Catalysis of the reaction: 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.
pyridoxal phosphate binding Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
serine binding Binding to 2-amino-3-hydroxypropanoic acid.
zinc ion binding Binding to a zinc ion (Zn).

6 GO annotations of biological process

Name Definition
folic acid metabolic process The chemical reactions and pathways involving folic acid, pteroylglutamic acid. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines.
glycine biosynthetic process from serine The chemical reactions and pathways resulting in the formation of glycine from other compounds, including serine.
L-serine catabolic process The chemical reactions and pathways resulting in the breakdown of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
one-carbon metabolic process The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
tetrahydrofolate interconversion The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesise other tetrahydrofolate molecules.
tetrahydrofolate metabolic process The chemical reactions and pathways involving tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3SZ20 SHMT2 Serine hydroxymethyltransferase, mitochondrial Bos taurus (Bovine) PR
P34897 SHMT2 Serine hydroxymethyltransferase, mitochondrial Homo sapiens (Human) PR
10 20 30 40 50 60
MFPRASALAK CMATVHRRGL LTSGAQSLVS KPVSEGDPEM FDILQQERHR QKHSITLIPS
70 80 90 100 110 120
ENFTSKAVMD LLGSELQNKY SEGYPGERYY GGNEIIDKSE SLCQARALEL YGLDPAKWGV
130 140 150 160 170 180
NVQPLSGAPA NLYVYSAIMN VGERLMGLDL PDGGHLSHGY QLKSGTPISF ISKYFQSMPY
190 200 210 220 230 240
HVDHTTGLID YDNLQVLAKA FRPKVIVAGT SAYSRLIDYA RFKEISQGCG AYLMSDMAHI
250 260 270 280 290 300
SGLVAANVVP SPFEHSDIVT TTTHKSLRGP RGAMIFFRKG IKSVTKKGKE IPYELEKKIN
310 320 330 340 350 360
FSVFPGHQGG PHNHTIGAMA VALKQAMSPE FKEYQQKIVD NSKWFAQELT KMGYKLVSGG
370 380 390 400 410 420
TDNHLIVIDL SGTQVDGARV ETILSALNIA ANKNTIPGDK SALFPSGLRI GTPAMTTRGF
430 440 450 460 470 480
GREEFSQVAK YIDSAVKLAE NLKTLEPTTK LDARSRLNEF KKLCNESSEV AALSGEISKW
VGQYPVPGDI