ID   GSA1_STAA8              Reviewed;         428 AA.
AC   Q2FXR4; O34092; Q9RL91;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 101.
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; OrderedLocusNames=SAOUHSC_01771;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9358061; DOI=10.1016/s0378-1119(97)00372-7;
RA   Kafala B., Sasarman A.;
RT   "Isolation of the Staphylococcus aureus hemCDBL gene cluster coding for
RT   early steps in heme biosynthesis.";
RL   Gene 199:231-239(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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; U89396; AAC45836.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30840.1; -; Genomic_DNA.
DR   RefSeq; WP_001270868.1; NZ_LS483365.1.
DR   RefSeq; YP_500276.1; NC_007795.1.
DR   AlphaFoldDB; Q2FXR4; -.
DR   SMR; Q2FXR4; -.
DR   STRING; 1280.SAXN108_1694; -.
DR   EnsemblBacteria; ABD30840; ABD30840; SAOUHSC_01771.
DR   GeneID; 3919689; -.
DR   KEGG; sao:SAOUHSC_01771; -.
DR   PATRIC; fig|93061.5.peg.1615; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_9; -.
DR   OMA; WGPLIFG; -.
DR   UniPathway; UPA00251; UER00317.
DR   PRO; PR:Q2FXR4; -.
DR   Proteomes; UP000008816; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..428
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase 1"
FT                   /id="PRO_0000247015"
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        370
FT                   /note="Q -> T (in Ref. 1; AAC45836)"
FT                   /evidence="ECO:0000305"
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