ID   GSA1_BACC7              Reviewed;         434 AA.
AC   B7HU66;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=BCAH187_A0587;
OS   Bacillus cereus (strain AH187).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH187;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA   Okstad O.A., Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH187.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001177; ACJ78777.1; -; Genomic_DNA.
DR   RefSeq; WP_000260535.1; NC_011658.1.
DR   AlphaFoldDB; B7HU66; -.
DR   SMR; B7HU66; -.
DR   EnsemblBacteria; ACJ78777; ACJ78777; BCAH187_A0587.
DR   GeneID; 64202259; -.
DR   KEGG; bcr:BCAH187_A0587; -.
DR   HOGENOM; CLU_016922_1_5_9; -.
DR   OMA; NFGMVEP; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000002214; 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..434
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase 1"
FT                   /id="PRO_0000382265"
FT   MOD_RES         270
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   434 AA;  46489 MW;  B02A06345C49D46D CRC64;
     MVVKFTKSEA LHKEALEHIV GGVNSPSRSF KAVGGGAPVA MERGKGAYFW DVDGNKYIDY
     LAAYGPIITG HAHPHITKAI TTAAENGVLY GTPTALEVKF AKMLKEAMPA LDKVRFVNSG
     TEAVMTTIRV ARAYTGRTKI MKFAGCYHGH SDLVLVAAGS GPSTLGTPDS AGVPQSIAQE
     VITVPFNNVE TLKEALDKWG HEVAAILVEP IVGNFGIVEP KPGFLEKVNE LVHEAGALVI
     YDEVITAFRF MYGGAQDLLG VTPDLTALGK VIGGGLPIGA YGGKKEIMEQ VAPLGPAYQA
     GTMAGNPASM ASGIACLEVL QQEGLYEKLD ELGAMLEKGI LEQAEKHNID ITLNRLKGAL
     TVYFTTNTIE DYDAAQDTDG EMFGKFFKLM LQEGINLAPS KYEAWFLTTE HTKEDIEYTI
     EAVGRAFAAL ANNK