ID   GSA1_MACCJ              Reviewed;         427 AA.
AC   B9E740;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 75.
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}; OrderedLocusNames=MCCL_1301;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH18008.1; -; Genomic_DNA.
DR   RefSeq; WP_012657206.1; NC_011999.1.
DR   AlphaFoldDB; B9E740; -.
DR   SMR; B9E740; -.
DR   STRING; 458233.MCCL_1301; -.
DR   EnsemblBacteria; BAH18008; BAH18008; MCCL_1301.
DR   GeneID; 61128799; -.
DR   KEGG; mcl:MCCL_1301; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_9; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 493793at2; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000001383; 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..427
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase 1"
FT                   /id="PRO_0000382340"
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   427 AA;  45893 MW;  6393B1BB9E748849 CRC64;
     MDYSKSKQAF KEAVNLMPGG VNSPVRAFKS VDMDPIFMER GKGSKIYDID GNEYIDYVLS
     WGPLILGHAN DTVTGALNKA VLNGTSFGAP TELENKMAEL VIERVPSIEM VRMVSSGTEA
     TLAALRLARG FTGKNKILKF IGCYHGHSDS LLIKAGSGVA TLGLPDSPGV PKGTAENTIT
     VHYNDLDAVK LAFEQFGDDI AGVIVEPVAG NMGVVPPVEG FLEGLREITT EHGALLIFDE
     VMTGFRVGYN CAQGYFGVIP DLTCLGKVIG GGLPVGAFGG RKDIMEHIAP SGPVYQAGTL
     SGNPLAMTGG YYTLSQLTPE SYEYFNHLGD MLEAGLTDVF AKHNVPITIN RAGSMIGFFL
     NEEKVTNFEI ASKSDLKLFA AMYKEMANNG VFLPPSQFEG MFLSTEHTEE DIQKTINAFD
     NSLTVIL