ID   GSA1_BACC2              Reviewed;         428 AA.
AC   B7IIX2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 1 {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT 1 {ECO:0000255|HAMAP-Rule:MF_00375};
GN   Name=hemL1 {ECO:0000255|HAMAP-Rule:MF_00375};
GN   OrderedLocusNames=BCG9842_B0655;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001186; ACK95760.1; -; Genomic_DNA.
DR   RefSeq; WP_000712938.1; NC_011772.1.
DR   AlphaFoldDB; B7IIX2; -.
DR   SMR; B7IIX2; -.
DR   KEGG; bcg:BCG9842_B0655; -.
DR   HOGENOM; CLU_016922_1_5_9; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000006744; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR   InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00713; hemL; 1.
DR   PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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_0000382271"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   428 AA;  45964 MW;  17F8325D6F0266AA CRC64;
     MKKFDKSIAA FEEAQDLMPG GVNSPVRAFK SVGMNPLFME RGKGSKVYDI DGNEYIDYVL
     SWGPLIHGHA NDRVVEALKS VAERGTSFGA PTEIENKLAK LVIERVPSIE IVRMVNSGTE
     ATMSALRLAR GYTGRNKILK FIGCYHGHGD SLLIKAGSGV ATLGLPDSPG VPEGVAKNTI
     TVAYNDLESV KYAFEQFGDD IACVIVEPVA GNMGVVPPQP GFLEGLREVT EQNGALLIFD
     EVMTGFRVAY NCGQGYYGVT PDLTCLGKVI GGGLPVGAYG GKAEIMRQIA PSGPIYQAGT
     LSGNPLAMAA GYETLVQLTP ESYVEFERKA EMLEAGLRKA AEKHGIPHHI NRAGSMIGIF
     FTDEPVINYD AAKSSNLEFF AAYYREMVEQ GVFLPPSQFE GLFLSTAHSD ADIEATIAAA
     EIAMSKLK
//