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Annotation rule MF_00375
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General rule information [?]

Accession MF_00375
Dates 1-JUN-2001 (Created)
18-NOV-2019 (Last updated, Version 47)
Name HemL_aminotrans_3
Scope
Bacteria
Archaea
Template P23893 (GSA_ECOLI)

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
GSA
Protein name
RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
Short=GSA;
EC 5.4.3.8;
AltName: Full=Glutamate-1-semialdehyde aminotransferase;
Short=GSA-AT;
Gene name
hemL

Comments [?]

Catalytic activity RHEA:14265: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
EC 5.4.3.8
Cofactor pyridoxal 5'-phosphate
case not <Property:PHOTOSYN>
Pathway Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
end case
case <Property:PHOTOSYN>
Pathway Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
end case
case <OC:Bacteria>
Subunit Homodimer.
end case
Subcellular location Cytoplasm.
Similarity Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Keywords [?]

case <Property:PHOTOSYN>
end case

Gene Ontology [?]

GO:0042286; Molecular function: glutamate-1-semialdehyde 2,1-aminomutase activity.
case <Property:PHOTOSYN>
GO:0015995; Biological process: chlorophyll biosynthetic process.
end case
GO:0006779; Biological process: porphyrin-containing compound biosynthetic process.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF00202; Aminotran_3; 1;
TIGRFAMs TIGR00713; HemL; 1;
PROSITE PS00600; AA_TRANSFER_CLASS_3; 1;

Features [?]

From: GSA_ECOLI (P23893)
Key     From     To       Description   Tag   Condition   FTGroup
MOD_RES     265     265       N6-(pyridoxal phosphate)lysine     K  

Additional information [?]

Size range 412-466 amino acids
Related rules None
Fusion None
Comments A third putative copy exists in BACHD. A second divergent copy exists in AERPE.