ID   GSA_BRANA               Reviewed;         473 AA.
AC   Q85WB7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase, chloroplastic;
DE            Short=GSA;
DE            EC=5.4.3.8;
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE            Short=GSA-AT;
DE   Flags: Precursor;
GN   Name=GSA;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12602878; DOI=10.1023/a:1021102118801;
RA   Tsang E.W.T., Yang J., Chang Q., Nowak G., Kolenovsky A., McGregor D.I.,
RA   Keller W.A.;
RT   "Chlorophyll reduction in the seed of Brassica napus with a glutamate 1-
RT   semialdehyde aminotransferase antisense gene.";
RL   Plant Mol. Biol. 51:191-201(2003).
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   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR   EMBL; AF364595; AAO63782.1; -; mRNA.
DR   AlphaFoldDB; Q85WB7; -.
DR   SMR; Q85WB7; -.
DR   PRIDE; Q85WB7; -.
DR   EnsemblPlants; CDY41519; CDY41519; GSBRNA2T00073140001.
DR   Gramene; CDY41519; CDY41519; GSBRNA2T00073140001.
DR   OMA; RCCASSV; -.
DR   UniPathway; UPA00251; UER00317.
DR   UniPathway; UPA00668; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; Isomerase; Plastid;
KW   Porphyrin biosynthesis; Pyridoxal phosphate; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           38..473
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase,
FT                   chloroplastic"
FT                   /id="PRO_0000041970"
FT   MOD_RES         313
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   473 AA;  50252 MW;  C9B978159C951DCB CRC64;
     MSATLTGSGT ALGFSCSSKI SKRVSSSPST RCSIKMSVSV DEKKKSFTLQ KSEEAFNAAK
     NLMPGGVNSP VRAFKSVGGQ PVLIDSVKGS KMWDIDGNEY IDYVGSWGPA IIGHADDEVL
     AALAETMKKG TSFGAPCLLE NVLAEMVISA VPSIEMVRFV NSGTEACMGV LRLARAFTNK
     EKFIKFEGCY HGHANAFLVK AGSGVATLGL PDSPGVPKAA TSDTLTAPYN DIEAVAKLFE
     AHKGEISAVI LEPVVGNSGF ITPTPEFING LRQLTKDNGA LLIFDEVMTG FRLAYGGAQE
     YFGITPDLTT LGKIIGGGLP VGAYGGRRDI MEMVAPAGPM YQAGTLSGNP LAMTAGIHTL
     KRLKQPGTYE YLDKITKELT NGILEAGKKT GHPMCGGYIS GMFGFFFAEG PVYNFADAKK
     SDTEKFGKFF RGMLEEGVYF APSQFEAGFT SLAHTSEDIQ FTISAAERVL GRI