ID   GSA2_STAA8              Reviewed;         429 AA.
AC   Q2G283;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 2 {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA 2 {ECO:0000255|HAMAP-Rule:MF_00375};
DE            EC=5.4.3.8 {ECO:0000255|HAMAP-Rule:MF_00375};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT 2 {ECO:0000255|HAMAP-Rule:MF_00375};
GN   Name=hemL2 {ECO:0000255|HAMAP-Rule:MF_00375};
GN   OrderedLocusNames=SAOUHSC_02000;
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 [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; Evidence={ECO:0000255|HAMAP-Rule:MF_00375};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00375};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00375}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD31056.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000253; ABD31056.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001011598.1; NZ_LS483365.1.
DR   RefSeq; YP_500497.2; NC_007795.1.
DR   AlphaFoldDB; Q2G283; -.
DR   SMR; Q2G283; -.
DR   STRING; 1280.SAXN108_1893; -.
DR   EnsemblBacteria; ABD31056; ABD31056; SAOUHSC_02000.
DR   GeneID; 3921880; -.
DR   KEGG; sao:SAOUHSC_02000; -.
DR   PATRIC; fig|93061.5.peg.1817; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_9; -.
DR   UniPathway; UPA00251; UER00317.
DR   PRO; PR:Q2G283; -.
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..429
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase 2"
FT                   /id="PRO_0000382376"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   429 AA;  46756 MW;  9FD547B0DBD1FD3A CRC64;
     MNFSESERLQ QLSNEYILGG VNSPSRSYKA VGGGAPVVMK EGHGAYLYDV DGNKFIDYLQ
     AYGPIITGHA HPHITKAIQE QAAKGVLFGT PTELEIEFSK KLRDAIPSLE KIRFVNSGTE
     AVMTTIRVAR AYTKRNKIIK FAGSYHGHSD LVLVAAGSGP SQLGSPDSAG VPESVAREVI
     TVPFNDINAY KEAIEFWGDE IAAVLVEPIV GNFGMVMPQP GFLEEVNEIS HNNGTLVIYD
     EVITAFRFHY GAAQDLLGVI PDLTAFGKIV GGGLPIGGYG GRQDIMEQVA PLGPAYQAGT
     MAGNPLSMKA GIALLEVLEQ DGVYEKLDSL GQQLEEGLLK LIEKHNITAT INRIYGSLTL
     YFTDEKVTHY DQVEHSDGEA FGKFFKLMLN QGINLAPSKF EAWFLTTEHT EEDIKQTLKA
     ADYAFSQMK