ID   GSA2_BACMK              Reviewed;         429 AA.
AC   A9VIT5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=BcerKBAB4_4306;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY45465.1; -; Genomic_DNA.
DR   RefSeq; WP_002034163.1; NC_010184.1.
DR   AlphaFoldDB; A9VIT5; -.
DR   SMR; A9VIT5; -.
DR   STRING; 315730.BcerKBAB4_4306; -.
DR   EnsemblBacteria; ABY45465; ABY45465; BcerKBAB4_4306.
DR   GeneID; 66265972; -.
DR   KEGG; bwe:BcerKBAB4_4306; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_9; -.
DR   OMA; WGPLIFG; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000002154; 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.
FT   CHAIN           1..429
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase 2"
FT                   /id="PRO_0000382282"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   429 AA;  46108 MW;  566C7AC7B4D875DC CRC64;
     MKKFDKSIAA FEEAQNLMPG GVNSPVRAFK SVGMNPLFME RGKGSKVYDI DGNEYIDYVL
     SWGPLIHGHA NDRVVEALKA VAEKGTSFGA PTEIENKLAQ LVIERVPSIE IVRMVNSGTE
     ATMSALRLAR GYTGRNKILK FIGCYHGHGD SLLIKAGSGV ATLGLPDSPG VPEGVAKNTI
     TVAYNDLESV KYAFEQFGDD IACIIVEPVA GNMGVVPPQP GFLEGLREVT EQNGALLIFD
     EVMTGFRVAY NCGQGYYGVT PDLTCLGKVI GGGLPVGAYG GKAEIMRQVA PSGPIYQAGT
     LSGNPLAMTA GYETLVQLTP ESYVEFERKA EMLEAGLRKA AEKHNIPHHI NRAGSMIGIF
     FTDEQVINYD AAKSSNLEFF AAYYREMVEQ GVFLPPSQFE GLFLSTAHSD ADIEATIAAA
     EIAMSKLKA