Mp8g16970



Description

Annotation

Database ID Description
CDD cd04902 ACT_3PGDH-xct
CDD cd12173 PGDH_4
FunFam G3DSA:3.30.1330.90:FF:000003 D-3-phosphoglycerate dehydrogenase
FunFam G3DSA:3.30.70.260:FF:000008 D-3-phosphoglycerate dehydrogenase, chloroplastic
FunFam G3DSA:3.40.50.720:FF:000021 D-3-phosphoglycerate dehydrogenase
FunFam G3DSA:3.40.50.720:FF:000616 D-3-phosphoglycerate dehydrogenase 2 chloroplastic
Gene3D G3DSA:3.30.1330.90 -
Gene3D G3DSA:3.30.70.260 -
Gene3D G3DSA:3.40.50.720 -
KEGG K00058 D-3-phosphoglycerate dehydrogenase / 2-oxoglutarate reductase [EC:1.1.1.95 1.1.1.399]
KOG KOG0068 D-3-phosphoglycerate dehydrogenase, D-isomer-specific 2-hydroxy acid dehydrogenase superfamily; [E]
NCBIfam TIGR01327 phosphoglycerate dehydrogenase
PANTHER PTHR42938 FORMATE DEHYDROGENASE 1
Pfam PF00389 D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain
Pfam PF01842 ACT domain
Pfam PF02826 D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain
Pfam PF19304 D-3-phosphoglycerate dehydrogenase intervening domain
ProSitePatterns PS00065 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature.
ProSitePatterns PS00671 D-isomer specific 2-hydroxyacid dehydrogenases signature 3.
ProSiteProfiles PS51671 ACT domain profile.
SMART SM00997 AdoHcyase_NAD_2
SUPERFAMILY SSF143548 Serine metabolism enzymes domain
SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
SUPERFAMILY SSF52283 Formate/glycerate dehydrogenase catalytic domain-like
SUPERFAMILY SSF55021 ACT-like
GO GO:0004617 phosphoglycerate dehydrogenase activity
GO GO:0051287 NAD binding
GO GO:0006564 L-serine biosynthetic process
GO GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
MapolyID Mapoly0030s0029 -

Nomenclature

No gene symbols are registered for this gene.

Associated Literature (AI-based literature mining)

Single-copy Marchantia phosphoglycerate dehydrogenase functionally characterized as recombinant protein; forms a homotetramer in vitro and shows allosteric regulation, inhibited by L-serine and activated by L-alanine, L-valine, L-methionine, L-homoserine, and L-homocysteine (lowest EC50). Represents a conserved amino acid-sensitive ancestral PGDH form, with no amino acid-insensitive isozyme in M. polymorpha.

4 core 1 peripheral

Tabeta H, Uzaki M, Hirai MY. (2025) · Plant signaling & behavior  research experimental subject
Encodes 3-phosphoglycerate dehydrogenase, the key enzyme of the phosphorylated serine biosynthesis pathway. The Mppgdh knockout mutant, defective in sperm formation, was analyzed by spatial metabolomics, revealing local serine depletion in antheridial receptacles (cell-autonomous serine regulation) that whole-organ analysis had missed. MpPGDH is expressed in the middle area of antheridial receptacles.
Wang, M., et al. (2024a) · Communications Biology  research experimental subject
Main study gene; 3-phosphoglycerate dehydrogenase of the phosphorylated serine biosynthesis pathway. CRISPR/Cas9 knockouts show serine supply in the dark is crucial for thallus growth and that MpPGDH-mediated serine synthesis is essential for sperm, embryo, and sporophyte development. Recombinant protein (65.6 kDa) shows AtPGDH1-like cooperative inhibition by L-serine.
Okamura, E., et al. (2021) · Biochemical Journal  research experimental subject
Single-copy Marchantia phosphoglycerate dehydrogenase functionally characterized as recombinant protein; forms a homotetramer in vitro and shows allosteric regulation, inhibited by L-serine and activated by L-alanine, L-valine, L-methionine, L-homoserine, and L-homocysteine (lowest EC50). Represents a conserved amino acid-sensitive ancestral PGDH form, with no amino acid-insensitive isozyme in M. polymorpha.
Akashi, H., et al. (2018) · Frontiers in Plant Science  research experimental subject
Marchantia 3-phosphoglycerate dehydrogenase; cDNA cloned and expressed in serine-auxotrophic E. coli, restoring growth without Ser to confirm function. Biochemically characterized: forms a homotetramer, optimal pH 9.0, Km/Vmax determined, stabilized by phosphate, inhibited cooperatively by L-serine (to 40%) and activated by several amino acids. Acts as the committed serine-biosynthesis enzyme studied here.
Lindström Battle AL, Sweetlove LJ. (2025) · Current opinion in plant biology  review citation background
Reviewed as the M. polymorpha 3-phosphoglycerate dehydrogenase (MpPGDH), cited as crucial for metabolism and development in a review on bryophyte metabolic engineering.

Transcript models

Transcript ID Location Sequences Extract region
Mp8g16970.1 chr8:21753221..21757123 (-) Gene /  mRNA /  CDS /  Protein
FASTA / GenBank (with flanking bases)

Expression Level powered by MBEX

Link to the original image in MBEX

Single-cell expression scRNA-seq atlas from Wang et al., 2023

Expression of Mp8g16970 across the single-cell RNA-seq atlas. Cluster identities (right) annotate the same UMAP used for the feature plot (left).

Feature plot of Mp8g16970 on UMAP
Feature plot (Seurat scale expression level).
UMAP cluster annotation
Cell-type annotation of the UMAP clusters.
Violin plot by developmental stage
Violin plot by stage. Expression across developmental time points (D0–D31).
Violin plot by cell cluster
Violin plot by cluster. Expression across cell clusters (1–21).

Gene structure:

Sequences:

Gene UTR + CDS + intron

FASTA

mRNA UTR + CDS

FASTA

CDS

FASTA

Protein

FASTA


MarpolBase / Genome Informatics Lab. NIG.