Mp8g16970



Description

Annotation

Database ID Description
Gene3D G3DSA:3.40.50.720 -
FunFam G3DSA:3.40.50.720:FF:000021 D-3-phosphoglycerate dehydrogenase
Gene3D G3DSA:3.30.1330.90 -
PANTHER PTHR42938 FORMATE DEHYDROGENASE 1
SUPERFAMILY SSF52283 Formate/glycerate dehydrogenase catalytic domain-like
ProSitePatterns PS00671 D-isomer specific 2-hydroxyacid dehydrogenases signature 3.
SMART SM00997 AdoHcyase_NAD_2
Pfam PF00389 D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain
Gene3D G3DSA:3.30.70.260 -
ProSiteProfiles PS51671 ACT domain profile.
Pfam PF01842 ACT domain
SUPERFAMILY SSF143548 Serine metabolism enzymes domain
FunFam G3DSA:3.30.1330.90:FF:000003 D-3-phosphoglycerate dehydrogenase
NCBIfam TIGR01327 phosphoglycerate dehydrogenase
SUPERFAMILY SSF55021 ACT-like
ProSitePatterns PS00065 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature.
FunFam G3DSA:3.30.70.260:FF:000008 D-3-phosphoglycerate dehydrogenase, chloroplastic
Pfam PF02826 D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain
Pfam PF19304 D-3-phosphoglycerate dehydrogenase intervening domain
CDD cd12173 PGDH_4
CDD cd04902 ACT_3PGDH-xct
FunFam G3DSA:3.40.50.720:FF:000616 D-3-phosphoglycerate dehydrogenase 2 chloroplastic
SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
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]
MapolyID Mapoly0030s0029 -
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

Nomenclature

No gene symbols are registered for this gene.

Associated Literature (AI-based literature mining, Beta-version)

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.

Expression Level powered by MBEX

Link to the original image in MBEX

Transcript models

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

Gene structure:

Sequences:

Gene UTR + CDS + intron

FASTA

mRNA UTR + CDS

FASTA

CDS

FASTA

Protein

FASTA

MarpolBase / Genome Informatics Lab. NIG.