ID   GSA_PROFF               Reviewed;         441 AA.
AC   Q06774;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 107.
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;
OS   Propionibacterium freudenreichii subsp. freudenreichii.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Propionibacterium.
OX   NCBI_TaxID=66712;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6207 / DSM 20271 / LMG 16412 / NBRC 12424 / NCIMB 5959 / NCTC
RC   10470 / NRRL B-3523;
RX   PubMed=8439165; DOI=10.1128/aem.59.1.347-350.1993;
RA   Murakami K., Hashimoto Y., Murooka Y.;
RT   "Cloning and characterization of the gene encoding glutamate 1-semialdehyde
RT   2,1-aminomutase, which is involved in delta-aminolevulinic acid synthesis
RT   in Propionibacterium freudenreichii.";
RL   Appl. Environ. Microbiol. 59:347-350(1993).
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;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR   EMBL; D12643; BAA02164.1; -; Genomic_DNA.
DR   EMBL; D85417; BAA21914.1; -; Genomic_DNA.
DR   PIR; A48959; A48959.
DR   RefSeq; WP_044636331.1; NZ_CP010341.1.
DR   AlphaFoldDB; Q06774; -.
DR   SMR; Q06774; -.
DR   UniPathway; UPA00251; UER00317.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR   InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate.
FT   CHAIN           1..441
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000120432"
FT   MOD_RES         270
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   441 AA;  45932 MW;  0F07395A67CAE4D2 CRC64;
     MSVSDELFAE ALKVMPGGVS SPVRAYRSVG GTPRFVKRAL GSHIVDVDDK RYVDLVCSWG
     PMIAGHAHPE VVAAVLQAVA DSTSFGAPSE VELRLAQAVV ARMGGAIDKV RFTCSGTEAV
     MTAARLARGI TKRPLLVKFV GCYHGHSDSF LVSAGSGVAS LGLPDSPGVP KEVAGDTVAL
     PYGRIDMVEE LFAERGDQVA AIVTEGVPAN MGVIVPPEGF NRRLHDIAHA HGALLIQDEV
     LTGFRLSPTG AWGLQGAKEG WTPDLFTFGK VIGGGMPLAA VGGSAQLMDY LAPEGPVYQA
     GTLSGNPAAC AAGLATLALM DDAAYSRLDA TADRVSAMAD AALESAGVPH RINKVSNLFS
     VFLTDAPVTD FASASKQDTK AFSRFFHAAL DAGLWLAPSG FEAWFCSTAL DDDDLEVIDA
     GLHKAAQAAA QGLSSLEDVR R