ID   GSA_SOYBN               Reviewed;         466 AA.
AC   P45621;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 134.
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=GSA1; Synonyms=GSA;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root nodule;
RX   PubMed=8278535; DOI=10.1104/pp.102.3.829;
RA   Sangwan I., O'Brian M.R.;
RT   "Expression of the soybean (Glycine max) glutamate 1-semialdehyde
RT   aminotransferase gene in symbiotic root nodules.";
RL   Plant Physiol. 102:829-834(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Essex;
RX   PubMed=7706283; DOI=10.1074/jbc.270.13.7387;
RA   Frustaci J.M., Sangwan I., O'Brian M.R.;
RT   "gsa1 is a universal tetrapyrrole synthesis gene in soybean and is
RT   regulated by a GAGA element.";
RL   J. Biol. Chem. 270:7387-7393(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   -!- TISSUE SPECIFICITY: Strongly expressed in leaves of etiolated plantlets
CC       independently of light treatment and, to a much lesser extent, in
CC       leaves of mature plants.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L12453; AAA33968.1; -; mRNA.
DR   EMBL; U20260; AAC48996.1; -; Genomic_DNA.
DR   PIR; JQ2263; JQ2263.
DR   RefSeq; NP_001238043.1; NM_001251114.1.
DR   AlphaFoldDB; P45621; -.
DR   SMR; P45621; -.
DR   STRING; 3847.P45621; -.
DR   PaxDb; 3847-GLYMA06G00510-1; -.
DR   ProMEX; P45621; -.
DR   EnsemblPlants; KRH51376; KRH51376; GLYMA_06G002900.
DR   GeneID; 547795; -.
DR   Gramene; KRH51376; KRH51376; GLYMA_06G002900.
DR   KEGG; gmx:547795; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_016922_1_5_1; -.
DR   InParanoid; P45621; -.
DR   OMA; EVLMGFR; -.
DR   OrthoDB; 1107811at2759; -.
DR   UniPathway; UPA00251; UER00317.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000008827; Chromosome 6.
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.
DR   Genevisible; P45621; GM.
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..28
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..466
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase,
FT                   chloroplastic"
FT                   /id="PRO_0000001260"
FT   MOD_RES         306
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  49646 MW;  5523012AE808DE72 CRC64;
     MAVSAITGAR LTLGMSLSSS TRSRTVAMAV SIDPKTDNKL TLTKSEEAFA AAKELMPGGV
     NSPVRAFKSV GGQPIVIDSV KGSRMWDIDG NEYIDYVGSW GPAIIGHADD QVLAALGETM
     KKGTSFGAPC LLENTLAELV IDAVPSIEMV RFVNSGTEAC MGALRLARAY TGREKIIKFE
     GCYHGHADPF LVKAGSGVAT LGLPDSPGVP KAATFETLTA PYNDTEAIEK LFEANKGEIA
     AVFLEPVVGN AGFIVPKPDF HSFLRKITKE NNTLLVFDEV MTGFRLSYGG AQEYFGITPD
     ITTLGKIIGG GLPVGAYGGR RDIMEKVAPA GPMYQAGTLS GNPLAMTAGI ETLQRIKEPG
     TYEYLDKITG ELVEGIIEAG KRAGHAICGG HIRGMFGFFF TEGPVYNFAD AKKSDTAKFA
     RFFWGMLAEG VYLAPSQFEA GFTSLAHTSD DIKKTIAAAE KVFREI
//