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Information on EC 2.6.1.83 - LL-diaminopimelate aminotransferase and Organism(s) Methanosphaera stadtmanae and UniProt Accession Q2NFU1

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.83 LL-diaminopimelate aminotransferase
IUBMB Comments
A pyridoxal-phosphate enzyme. In vivo, the reaction occurs in the opposite direction to that shown above. This is one of the final steps in the lysine-biosynthesis pathway of plants (ranging from mosses to flowering plants). meso-Diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. 2-Oxoglutarate cannot be replaced by oxaloacetate or pyruvate. It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate.
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Methanosphaera stadtmanae
UNIPROT: Q2NFU1
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The taxonomic range for the selected organisms is: Methanosphaera stadtmanae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ll-dap-at, atdap-at, l,l-diaminopimelate aminotransferase, ctdap-at, ll-diaminopimelate aminotransferase, diaminopimelate aminotransferase, vsdapl, ll-dap aminotransferase, ct390, sll0480, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LL-DAP aminotransferase
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SYSTEMATIC NAME
IUBMB Comments
LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate enzyme. In vivo, the reaction occurs in the opposite direction to that shown above. This is one of the final steps in the lysine-biosynthesis pathway of plants (ranging from mosses to flowering plants). meso-Diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. 2-Oxoglutarate cannot be replaced by oxaloacetate or pyruvate. It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hudson, A.O.; Gilvarg, C.; Leustek, T.
Biochemical and phylogenetic characterization of a novel diaminopimelate biosynthesis pathway in prokaryotes identifies a diverged form of LL-diaminopimelate aminotransferase
J. Bacteriol.
190
3256-3263
2008
Syntrophobacter fumaroxidans (A0LEA5), Methanothermobacter thermautotrophicus (O26158), Aquifex aeolicus (O66630), Chlamydia trachomatis (O84395), Desulfitobacterium hafniense (Q18T09), Methanosphaera stadtmanae (Q2NFU1), Moorella thermoacetica (Q2RK33), Trichormus variabilis (Q3MAL4), Trichormus variabilis (Q3MDN5), Synechocystis sp. (Q55828), Bacteroides fragilis (Q5LC03), Candidatus Protochlamydia amoebophila (Q6MDE0), Leptospira interrogans (Q72NJ3), Geobacter sulfurreducens (Q74GT3), Gloeobacter violaceus (Q7NDX4), Methanosarcina acetivorans (Q8TQ40)
Manually annotated by BRENDA team