ID   GSA_HORVU               Reviewed;         469 AA.
AC   P18492;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 3.
DT   25-MAY-2022, entry version 133.
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   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Bonus; TISSUE=Seedling;
RX   PubMed=2349227; DOI=10.1073/pnas.87.11.4169;
RA   Grimm B.;
RT   "Primary structure of a key enzyme in plant tetrapyrrole synthesis:
RT   glutamate 1-semialdehyde aminotransferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4169-4173(1990).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2505791; DOI=10.1007/bf02907586;
RA   Grimm B., Bull A., Welinder K.G., Gough S.P., Kannangara C.G.;
RT   "Purification and partial amino acid sequence of the glutamate 1-
RT   semialdehyde aminotransferase of barley and synechococcus.";
RL   Carlsberg Res. Commun. 54:67-79(1989).
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.
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; M31545; AAB59330.1; -; mRNA.
DR   PIR; A35789; A35789.
DR   AlphaFoldDB; P18492; -.
DR   SMR; P18492; -.
DR   PRIDE; P18492; -.
DR   UniPathway; UPA00251; UER00317.
DR   UniPathway; UPA00668; -.
DR   ExpressionAtlas; P18492; baseline and differential.
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   1: Evidence at protein level;
KW   Chlorophyll biosynthesis; Chloroplast; Direct protein sequencing;
KW   Isomerase; Plastid; Porphyrin biosynthesis; Pyridoxal phosphate;
KW   Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Chloroplast"
FT   CHAIN           35..469
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase,
FT                   chloroplastic"
FT                   /id="PRO_0000001258"
FT   MOD_RES         309
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        309
FT                   /note="K -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   469 AA;  49494 MW;  78BF03C14A3C1448 CRC64;
     MAGAAAAVAS GISIRPVAAP KISRAPRSRS VVRAAVSIDE KAYTVQKSEE IFNAAKELMP
     GGVNSPVRAF KSVGGQPIVF DSVKGSHMWD VDGNEYIDYV GSWGPAIIGH ADDKVNAALI
     ETLKKGTSFG APCALENVLA QMVISAVPSI EMVRFVNSGT EACMGALRLV RAFTGREKIL
     KFEGCYHGHA DSFLVKAGSG VATLGLPDSP GVPKGATVGT LTAPYNDADA VKKLFEDNKG
     EIAAVFLEPV VGNAGFIPPQ PAFLNALREV TKQDGALLVF DEVMTGFRLA YGGAQEYFGI
     TPDVTTLGKI IGGGLPVGAY GGRKDIMEMV APAGPMYQAG TLSGNPLAMT AGIHTLKRLM
     EPGTYEYLDK VTGELVRGIL DVGAKTGHEM CGGHIRGMFG FFFAGGPVHN FDDAKKSDTA
     KFGRFHRGML GEGVYLAPSQ FEAGFTSLAH TTQDIEKTVE AAEKVLRWI