ID   GSA_XANCH               Reviewed;         429 AA.
AC   Q06741;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
DE            Short=GSA;
DE            EC=5.4.3.8;
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE            Short=GSA-AT;
GN   Name=hemL;
OS   Xanthomonas campestris pv. phaseoli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=317013;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HUT 8925;
RX   PubMed=7763385; DOI=10.1007/bf00242945;
RA   Murakami K., Korbsrisate S., Asahara N., Hashimoto Y., Murooka Y.;
RT   "Cloning and characterization of the glutamate 1-semialdehyde aminomutase
RT   gene from Xanthomonas campestris pv. phaseoli.";
RL   Appl. Microbiol. Biotechnol. 38:502-506(1993).
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;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR   EMBL; D12642; BAA02163.1; -; Genomic_DNA.
DR   PIR; A48377; A48377.
DR   RefSeq; WP_022558547.1; NZ_LT960913.1.
DR   AlphaFoldDB; Q06741; -.
DR   SMR; Q06741; -.
DR   STRING; 317013.NY99_03250; -.
DR   eggNOG; COG0001; Bacteria.
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"
FT                   /id="PRO_0000120470"
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  45044 MW;  C134A4589BCDD700 CRC64;
     MNHSRSHALF AQAQTLLPGG VNSPVRAFKS VGGEPFFVAR ADGPYLFDVD DNRYIDYVGS
     WGPMIAGHNH PAVREAVEQS IRNGLSFGAP CAAEVTMAQT IARLVPSCEM VRMVNSGTEA
     TLSAVRLARG ATGRNRIIKF EGCYHGHGDS FLVKAGSGML TLGVPTSPGV PAGLSELTAT
     LSFNDFEGAT ALFDEIGAEV AAVIIEPVVG NANCIPPQAG YLQHLRTLCT RHGALLIFDE
     VMTGFRVALG GAQAHYGVTP DLTTFGKIIG GGMPVGAYGG RRDLMEQVAP AGPIYQAGTL
     SGNPVAMAAG LAMLELVQEP GFHTRLSEAT SMLCEGLEDA ARAAGIAVTT NQVGGMFGLF
     FTDDVVESYA QATACDITSF NRFFHAMLQR GVYLAPSAYE AGFMSSAHDE AVIEATLAAA
     REAFADVAR