HAMAP rule MF_02084
General rule information
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Accession | MF_02084 |
Dates | 5-JAN-2017 (Created)
1-JUN-2023 (Last updated, Version 12) |
Name | LysJ_aminotrans_3 |
Scope(s) |
Archaea Bacteria Chloroflexota Deinococcota |
Template(s) | Q4JAP8 (LYSJ_SULAC); Q93R93 (LYSJ_THET2); Q5SHH5 (LYSJ_THET8); [ Recover all ] |
Triggered by |
HAMAP; MF_02084 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | LYSJ |
case <OC:Sulfolobales> | |
Protein name | RecName: Full=[LysW]-aminoadipate semialdehyde/glutamate semialdehyde transaminase; EC=2.6.1.118; EC=2.6.1.124; |
else case <OC:Archaea> and not <OC:Sulfolobales> | |
Protein name | RecName: Full=Putative [LysW]-aminoadipate semialdehyde/glutamate semialdehyde transaminase; EC=2.6.1.118; EC=2.6.1.124; |
else case <OC:Deinococcota> | |
Protein name | RecName: Full=[LysW]-aminoadipate semialdehyde transaminase; EC=2.6.1.118; |
else case <OC:Chloroflexota> | |
Protein name | RecName: Full=Putative [LysW]-aminoadipate semialdehyde transaminase; EC=2.6.1.118; |
end case | |
Gene name | Name=lysJ; |
Comments
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case <OC:Archaea> | |
FUNCTION | Involved in both the arginine and lysine biosynthetic pathways. |
else case <OC:Bacteria> | |
FUNCTION | Catalyzes the transfer of the amino group of L-glutamate to [LysW]-aminoadipate 6-semialdehyde, generating [LysW]-gamma-L-lysine. |
end case | |
CATALYTIC ACTIVITY | Reaction=2-oxoglutarate + [amino-group carrier protein]-C-terminal- gamma-(L-lysyl)-L-glutamate = [amino-group carrier protein]-C- terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate; Xref=Rhea:RHEA:41952, Rhea:RHEA-COMP:9714, Rhea:RHEA-COMP:9715, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:78501, ChEBI:CHEBI:78526; EC=2.6.1.118; |
case <OC:Archaea> | |
CATALYTIC ACTIVITY | Reaction=2-oxoglutarate + [amino-group carrier protein]-C-terminal- gamma-(L-ornithyl)-L-glutamate = [amino-group carrier protein]-C- terminal-gamma-(L-glutamyl-5-semialdehyde)-L-glutamate + L-glutamate; Xref=Rhea:RHEA:52672, Rhea:RHEA-COMP:13327, Rhea:RHEA-COMP:13328, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:136761, ChEBI:CHEBI:136763; EC=2.6.1.124; |
end case | |
COFACTOR | Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Note=Binds 1 pyridoxal phosphate per subunit |
PATHWAY | Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5. |
case <OC:Archaea> | |
PATHWAY | Amino-acid biosynthesis; L-arginine biosynthesis. |
end case | |
SUBUNIT | Homodimer. |
SUBCELLULAR LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. LysJ subfamily. |
Keywords
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Amino-acid biosynthesis | |
Aminotransferase | |
case <OC:Archaea> | |
Arginine biosynthesis | |
end case | |
Cytoplasm | |
Lysine biosynthesis | |
Pyridoxal phosphate | |
Transferase |
Gene Ontology
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GO:0008483; Molecular function:transaminase activity | |
case <OCellular component:Archaea> | |
GO:0042450; Biological process:arginine biosynthetic process via ornithine | |
end case | |
GO:0019878; Biological process:lysine biosynthetic process via aminoadipic acid | |
GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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From: LYSJ_THET8 (Q5SHH5) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 113 | 114 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
G-[TA] | ||||||||
BINDING | 225 | 228 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
D-E-[IV]-Q | ||||||||
BINDING | 140 | 140 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
F | ||||||||
BINDING | 143 | 143 | /ligand="substrate" | R | ||||||||
BINDING | 282 | 282 | /ligand="substrate" | [ST] | ||||||||
BINDING | 283 | 283 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
T | ||||||||
MOD_RES | 254 | 254 | /note="N6-(pyridoxal phosphate)lysine" | K |
Additional information
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Size range | 360-450 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |