ID   GSA_SOLLC               Reviewed;         481 AA.
AC   Q40147;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 129.
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;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. VFNT Cherry; TISSUE=Fruit;
RA   Polking G.F., Hannapel D.J., Gladon R.J.;
RT   "A cDNA clone for glutamate 1-semialdehyde 2,1-aminomutase from tomato
RT   (Lycopersicon esculentum Mill.).";
RL   (er) Plant Gene Register PGR95-035(1995).
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; L39279; AAA81881.1; -; mRNA.
DR   PIR; T07034; T07034.
DR   AlphaFoldDB; Q40147; -.
DR   SMR; Q40147; -.
DR   STRING; 4081.Q40147; -.
DR   PaxDb; 4081-Solyc04g009200-2-1; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   InParanoid; Q40147; -.
DR   UniPathway; UPA00251; UER00317.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q40147; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR   InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00713; hemL; 1.
DR   PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT   CHAIN           ?..481
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase,
FT                   chloroplastic"
FT                   /id="PRO_0000001259"
FT   REGION          18..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         321
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   481 AA;  51413 MW;  4D7EFC0E32D64BBD CRC64;
     MAAVNGVGLS WPSKLTKNQT PKWGFSPSHR RCNPSSSSSA TIRMTASVDE KKKTFTLEKS
     EEAFSKAKEL MPGGVNSPVR AFKSVGGQPI IIDSVKGSRM RDIDGNEYID YVGSWGPAII
     GHADDEVLAA LAETMKKGTS FGAPCLLENT LAEMVISAVP SIEMVRFVNS GTEACMGVLR
     LARAFTCRPK IIKFEGCYHG HADPFLVKAG SGVATLGLPD SPGVPKAATI DTLTAPYNDI
     SAVESLFEEH KGEIAAVILE PVVGNAGFIP PKLEFLAAIR KITKENDALL IFDEVMTGFR
     LAYGGAQEYF GITPDLTTLG KIIGGGLPVG AYGGRRDIME MVAPAGPMYQ AGTLSGNPLA
     MTAGIHTLKR LQGQGTYEHL DKITAELTQG ILDAGKKTGH AMCGGSIRGM FGFFFADGPI
     YNFSDAKKSD TEKFGRFYRG MLEEGVYFAP SQFEAGFTSL AHTPEDIQRT VAAAEKVLKQ
     I
//