hemL

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005737 cytoplasm	IEA GO_REF:0000120	ACCEPT	Summary: The soluble HemL enzyme is predicted to function in the bacterial cytoplasm. Reason: UniProt explicitly assigns cytoplasmic localization and no targeting or membrane feature. Supporting Evidence: file:PSEPK/hemL/hemL-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm
GO:0030170 pyridoxal phosphate binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: PLP is the established cofactor for HemL-family aminomutases. Reason: PLP binding is valid cofactor information, but the substrate-specific aminomutase activity is the core molecular function. Supporting Evidence: file:PSEPK/hemL/hemL-uniprot.txt Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
GO:0033014 tetrapyrrole biosynthetic process	IEA GO_REF:0000002	ACCEPT	Summary: HemL directly supplies 5-aminolevulinate for tetrapyrrole synthesis. Reason: HemL completes 5-aminolevulinate formation in the C5 route, which occurs in bacteria, archaea, and plastid-bearing eukaryotes and can feed multiple tetrapyrrole products. GO:0033014 accurately captures that direct role without relying on an obsolete route-specific term. Supporting Evidence: file:PSEPK/hemL/hemL-uniprot.txt biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. PMID:7883699 be used by Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas stutzeri,
GO:0042286 glutamate-1-semialdehyde 2,1-aminomutase activity	IEA GO_REF:0000120	ACCEPT	Summary: This term precisely identifies the HemL reaction. Reason: UniProt assigns EC 5.4.3.8 and the HemL family, supporting reversible rearrangement of glutamate 1-semialdehyde and ALA. Supporting Evidence: file:PSEPK/hemL/hemL-uniprot.txt RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase