ID   GSA2_LISMH              Reviewed;         429 AA.
AC   B8DHJ5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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}; OrderedLocusNames=LMHCC_1016;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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}.
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DR   EMBL; CP001175; ACK39364.1; -; Genomic_DNA.
DR   RefSeq; WP_003736696.1; NC_011660.1.
DR   AlphaFoldDB; B8DHJ5; -.
DR   SMR; B8DHJ5; -.
DR   KEGG; lmh:LMHCC_1016; -.
DR   HOGENOM; CLU_016922_1_5_9; -.
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..429
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase 2"
FT                   /id="PRO_0000382333"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   429 AA;  46561 MW;  02AD16E4E8FF2E30 CRC64;
     MQIYSKSEKA FKEAKKVLPG GVNSPVRAFN SVDASPVFMD HGKGAYITDI DGNEYIDYVL
     SWGPLILGHA NPSVVQAITN AAMKGTSFGT PTEIETELAK LVIERVPSIE IVRMVSSGTE
     ATMSAIRLAR GYTKREKILK FEGSYHGHGD SLLIKAGSGV ATLGLPDSPG VTKGLAADTI
     TVPYNDIEGA KLAFEKYGEE IAAVIVEPVA GNMGVVPPIE GFLEGLRELT TNYGSLLIFD
     EVMTGFRVDY YSAQGYYVVT PDLTCLGKVI GGGLPVGAYG GKKEIMEQIA PAGSIYQAGT
     LSGNPLAMNA GFETVRQLTP QDYDVFRTLI KRMEEGLTEI SARRQVPLSI NKAGSMFGFF
     FTDQKVTNFD TAKTSDLEFF RSYYREMLGQ GIFLPPSQFE GVFISTMHTE KEIDKTLDAF
     DTTCKILRG