ID   GSA1_STAAU              Reviewed;         428 AA.
AC   P0C1P8; O34092; Q9RL91;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 1;
DE            Short=GSA 1;
DE            EC=5.4.3.8;
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase 1;
DE            Short=GSA-AT 1;
GN   Name=hemL1; Synonyms=hemL;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RUSA233;
RX   PubMed=10566865; DOI=10.1089/mdr.1999.5.163;
RA   de Lencastre H., Wu S.-W., Pinho M.G., Ludovice A.M., Filipe S.,
RA   Gardete S., Sobral R., Gill S.R., Chung M., Tomasz A.;
RT   "Antibiotic resistance as a stress response: complete sequencing of a large
RT   number of chromosomal loci in Staphylococcus aureus strain COL that impact
RT   on the expression of resistance to methicillin.";
RL   Microb. Drug Resist. 5:163-175(1999).
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         Evidence={ECO:0000250};
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; Y18635; CAB60738.1; -; Genomic_DNA.
DR   RefSeq; WP_001270868.1; NZ_WSFM01000001.1.
DR   AlphaFoldDB; P0C1P8; -.
DR   SMR; P0C1P8; -.
DR   OMA; WGPLIFG; -.
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   TIGRFAMs; TIGR00713; hemL; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate.
FT   CHAIN           1..428
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase 1"
FT                   /id="PRO_0000120451"
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  46388 MW;  88F0566FC5A26D49 CRC64;
     MRYTKSEEAM KVAETLMPGG VNSPVRAFKS VDTPAIFMDH GKGSKIYDID GNEYIDYVLS
     WGPLILGHRD PQVISHLHEA IDKGTSFGAS TLLENKLAQL VIDRVPSIEK VRMVSSGTEA
     TLDTLRLARG YTGRNKIVKF EGCYHGHSDS LLIKAGSGVA TLGLPDSPGV PEGIAKNTIT
     VPYNDLDALK IAFEKFGNDI AGVIVEPVAG NMGVVPPIEG FLQGLRDITT EYGALLIFDE
     VMTGFRVGYH CAQGYFGVTP DLTCLGKVIG GGLPVGAFGG KKEIMDHIAP LGNIYQAGTL
     SGNPLAMTSG YETLSQLTPE TYEYFNMLGD ILEDGLKRVF AKHNVPITVN RAGSMIGYFL
     NEGPVTNFEQ ANKSDLKLFA EMYREMAKEG VFLPPSQFEG TFLSTAHTKE DIEKTIQAFD
     TALSRIVK