A0A0I9TTF5 · A0A0I9TTF5_9MYCO

  • Protein
    Glycerol-3-phosphate dehydrogenase [NAD(P)+]
  • Gene
    gpsA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site15-20NAD+ (UniProtKB | ChEBI)
Binding site18NADPH (UniProtKB | ChEBI)
Binding site19NADPH (UniProtKB | ChEBI)
Binding site38NADPH (UniProtKB | ChEBI)
Binding site55NADPH (UniProtKB | ChEBI)
Binding site113NADPH (UniProtKB | ChEBI)
Binding site113sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site113substrate
Binding site141sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site145NAD+ (UniProtKB | ChEBI)
Binding site145NADPH (UniProtKB | ChEBI)
Active site196Proton acceptor
Binding site196sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site249sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site259sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site260NAD+ (UniProtKB | ChEBI)
Binding site260NADPH (UniProtKB | ChEBI)
Binding site260sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site260-261substrate
Binding site261sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site284NADPH (UniProtKB | ChEBI)
Binding site286NADPH (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionacyltransferase activity
Molecular Functionglycerol-3-phosphate dehydrogenase (NADP+) activity
Molecular Functionglycerol-3-phosphate dehydrogenase [NAD(P)+] activity
Molecular FunctionNAD binding
Biological Processcarbohydrate metabolic process
Biological Processglycerol-3-phosphate biosynthetic process
Biological Processglycerol-3-phosphate catabolic process
Biological Processglycerophospholipid metabolic process
Biological Processphospholipid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycerol-3-phosphate dehydrogenase [NAD(P)+]
  • EC number
  • Alternative names
    • NAD(P)(+)-dependent glycerol-3-phosphate dehydrogenase
    • NAD(P)H-dependent dihydroxyacetone-phosphate reductase

Gene names

    • Name
      gpsA
    • ORF names
      ABH38_05210

Organism names

  • Taxonomic identifier
  • Strain
    • UC1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium

Accessions

  • Primary accession
    A0A0I9TTF5

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-165Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal
Domain185-325Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    342
  • Mass (Da)
    36,362
  • Last updated
    2015-10-14 v1
  • Checksum
    A0206E8F76B8E83F
MPVAEQREPKVVVFGGGSWGTTVASICARRGPTLQWVRSEVTAKDINEQHRNSRYLGNDVVLSDTLRATTDFAEAARCADVVVMGVPSHGFRGVLTELAKELRPWVPVVSLVKGLEQGTNMRMSQIVEEVLPGHPAGILAGPNIAREVAEGYAAAAVLAMPDQHLATRLAALFRTRRFRVYTTDDVIGVEVAGALKNVFAIAVGMGYSLGIGENTRALVIARALREMTKLGVALGGRSETFPGLAGLGDLIVTCTSQRSRNRHVGEQLGAGKPIDEIIASMNQVAEGVKAASVVMEFATEFGLSMPIAREVDAVINHASTVEQAYSGLIAEIPGHEVHGSGF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LDPR01000003
EMBL· GenBank· DDBJ
KLO38001.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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