ID   GSA_TOBAC               Reviewed;         478 AA.
AC   P31593;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 112.
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   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. SR1;
RX   PubMed=8127872; DOI=10.1073/pnas.91.5.1726;
RA   Hoefgen R., Axelsen K.B., Kannangara C.G., Schuettke I., Pohlenz H.-D.,
RA   Willmitzer L., Grimm B., von Wettstein D.;
RT   "A visible marker for antisense mRNA expression in plants: inhibition of
RT   chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase
RT   antisense gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:1726-1730(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.
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; X65973; CAA46786.1; -; mRNA.
DR   EMBL; X65974; CAA46787.1; -; mRNA.
DR   PIR; S21454; S21454.
DR   PIR; S21455; S21455.
DR   RefSeq; NP_001311974.1; NM_001325045.1.
DR   AlphaFoldDB; P31593; -.
DR   SMR; P31593; -.
DR   STRING; 4097.P31593; -.
DR   PRIDE; P31593; -.
DR   ProMEX; P31593; -.
DR   GeneID; 107769957; -.
DR   KEGG; nta:107769957; -.
DR   UniPathway; UPA00251; UER00317.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000084051; Unplaced.
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; 3.40.640.10; -; 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; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT   CHAIN           ?..478
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase,
FT                   chloroplastic"
FT                   /id="PRO_0000001261"
FT   MOD_RES         318
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         18
FT                   /note="G -> S (in isozyme 2)"
FT   VARIANT         104
FT                   /note="E -> D (in isozyme 2)"
FT   VARIANT         221
FT                   /note="G -> V (in isozyme 2)"
FT   VARIANT         227
FT                   /note="S -> T (in isozyme 2)"
FT   VARIANT         245
FT                   /note="E -> K (in isozyme 2)"
FT   VARIANT         270
FT                   /note="L -> P (in isozyme 2)"
FT   VARIANT         375
FT                   /note="E -> D (in isozyme 2)"
FT   VARIANT         411
FT                   /note="L -> F (in isozyme 2)"
FT   VARIANT         413
FT                   /note="A -> V (in isozyme 2)"
FT   VARIANT         466
FT                   /note="K -> R (in isozyme 2)"
SQ   SEQUENCE   478 AA;  50877 MW;  459CBA43FE46E84A CRC64;
     MAAVNGVGIS WPSKLTQGQR PKLVFSPSPR RCTPSSSTIK MTASVDEKKK TFTLQKSEEA
     FSKAKELMPG GVNSPVRAFK SVGGQPIIID SVKGSRMRDI DGNEYIDYVG SWGPAIIGHA
     DDEVLAALAE TMKKGTSFGA PCLLENTLAE MVISAVPSIE MVRFVNSGTE ACMGVLRLAR
     AFTGRPKIIK FEGCYHGHAD PFLVKAGSGV ATLGLPDSPG GPKAATSDTL TAPYNDISAV
     ESLFEEHKGE VAAIILEPVV GNAGFIQPNL DFLAAIRKIT KENDALLIFD EVMTGFRLAY
     GGAQEYFGIT PDLTTLGKII GGGLPVGAYG GRRDIMEMVA PAGPMYQAGT LSGNPLAMTA
     GIHTLKRLQG PGTYEYLDKI TGELTQGILD AGKKTGHAMC GGYIRGMFGF LFAEGPVNNF
     SDAKKSDTEK FGRFYRGMLE EGVYFAPSQF EAGFTSLAHT SEDIQKTVAA AEKVLKQI