ID   GSA_CHLRE               Reviewed;         463 AA.
AC   Q39566; Q39567;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 127.
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   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NO-;
RX   PubMed=8155881; DOI=10.1007/bf00023558;
RA   Matters G.L., Beale S.I.;
RT   "Structure and light-regulated expression of the gsa gene encoding the
RT   chlorophyll biosynthetic enzyme, glutamate 1-semialdehyde aminotransferase,
RT   in Chlamydomonas reinhardtii.";
RL   Plant Mol. Biol. 24:617-629(1994).
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; U03632; AAA18861.1; -; mRNA.
DR   EMBL; U03633; AAA18862.1; -; Unassigned_DNA.
DR   PIR; S43787; S43787.
DR   RefSeq; XP_001697519.1; XM_001697467.1.
DR   AlphaFoldDB; Q39566; -.
DR   SMR; Q39566; -.
DR   STRING; 3055.EDP00181; -.
DR   ProMEX; Q39566; -.
DR   EnsemblPlants; PNW84771; PNW84771; CHLRE_03g158000v5.
DR   GeneID; 5723033; -.
DR   Gramene; PNW84771; PNW84771; CHLRE_03g158000v5.
DR   KEGG; cre:CHLRE_03g158000v5; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_016922_1_5_1; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 1160614at2759; -.
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..30
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..463
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase,
FT                   chloroplastic"
FT                   /id="PRO_0000001257"
FT   MOD_RES         303
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   463 AA;  49228 MW;  9CB3BDF9A90C8010 CRC64;
     MQMQLNAKTV QGAFKAQRPR SVRGNVAVRA VAAPPKLVTK RSEEIFKEAQ ELLPGGVNSP
     VRAFRSVGGG PIVFDRVKGA YCWDVDGNKY IDYVGSWGPA ICGHGNDEVN NALKAQIDKG
     TSFGAPCELE NVLAKMVIDR VPSVEMVRFV SSGTEACLSV LRLMRAYTGR EKVLKFTGCY
     HGHADSFLVK AGSGVITLGL PDSPGVPKST AAATLTATYN NLDSVRELFA ANKGEIAGVI
     LEPVVGNSGF IVPTKEFLQG LREICTAEGA VLCFDEVMTG FRIAKGCAQE HFGITPDLTT
     MGKVIGGGMP VGAYGGKKEI MKMVAPAGPM YQAGTLSGNP MAMTAGIKTL EILGRPGAYE
     HLEKVTKRLI DGIMAAAKEH SHEITGGNIS GMFGFFFCKG PVTCFEDALA ADTAKFARFH
     RGMLEEGVYL APSQFEAGFT SLAHSEADVD ATIAAARRVF ARI