AC   MF_00375;
DC   Protein; auto
TR   HAMAP; MF_00375; -; 1; level=0
XX
Names: HemL_aminotrans_3
XX
ID   GSA
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
DE            Short=GSA;
DE            EC=5.4.3.8;
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE            Short=GSA-AT;
GN   Name=hemL;
XX
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate;
CC         Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416;
CC         EC=5.4.3.8;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
case not <Property:PHOTOSYN>
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
end case
case <Property:PHOTOSYN>
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
end case
case <OC:Bacteria>
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily.
XX
DR   Pfam; PF00202; Aminotran_3; 1; trigger=no
DR   NCBIfam; TIGR00713; HemL; 1; trigger=no
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1; trigger=no
XX
KW   Cytoplasm
KW   Porphyrin biosynthesis
case <Property:PHOTOSYN>
KW   Chlorophyll biosynthesis
end case
KW   Isomerase
KW   Pyridoxal phosphate
XX
GO   GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity
case <Property:PHOTOSYN>
GO   GO:0015995; P:chlorophyll biosynthetic process
end case
GO   GO:0006779; P:porphyrin-containing compound biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: GSA_ECOLI (P23893)
FT   MOD_RES         265
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
XX
Size: 412-466;
Related: None;
Template: P23893;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in ANOFW, BACVZ, BACAA, BACAC, BACAH, BACAN, BACC0, BACC1, BACC2,
 BACC3, BACC4, BACC7, BACCN, BACCQ, BACCR, BACCZ, HALH5, BACHK, BACLD, BACP2,
 SHOC1, BACSU, BACMK, BREBN, CENSY, LACP7, EXIS2, EXISA, GEOKA, GEOTN, LISIN,
 LISMC, LISMF, LISMH, LISMO, LISW6, LYSSC, MACCJ, OCEIH, STAA1, STAA2, STAA3,
 STAA8, STAA9, STAAB, STAAC, STAAE, STAAM, STAAN, STAAR, STAAS, STAAT, STAAW,
 STACT, STAEQ, STAES, STAHJ, STAS1
Plasmid: None
Comments: A third putative copy exists in HALH5.
 A second divergent copy exists in AERPE.
XX
# Revision 1.52 2023/11/28
//