ID   GSA2_ARATH              Reviewed;         472 AA.
AC   Q42522; Q1JPM9; Q9SMM6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplastic {ECO:0000303|Ref.1};
DE            Short=GSA 2 {ECO:0000303|Ref.1};
DE            EC=5.4.3.8 {ECO:0000250|UniProtKB:P42799};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase 2 {ECO:0000303|Ref.1};
DE            Short=GSA-AT 2 {ECO:0000303|Ref.1};
DE   Flags: Precursor;
GN   Name=GSA2 {ECO:0000303|Ref.1};
GN   Synonyms=FNE1 {ECO:0000303|PubMed:25840087}, HEML2
GN   {ECO:0000303|PubMed:15951223};
GN   OrderedLocusNames=At3g48730 {ECO:0000312|Araport:AT3G48730};
GN   ORFNames=T8P19.240 {ECO:0000312|EMBL:CAB62362.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Wenzlau J.M., Berry-Lowe S.L.;
RT   "Nucleotide sequence of a gene encoding glutamate 1-semialdehyde
RT   aminotransferase from Arabidopsis thaliana 'Columbia'.";
RL   (er) Plant Gene Register PGR95-007(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   REVIEW.
RX   PubMed=15951223; DOI=10.1016/j.tplants.2005.05.005;
RA   Beale S.I.;
RT   "Green genes gleaned.";
RL   Trends Plant Sci. 10:309-312(2005).
RN   [7]
RP   DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-92 AND GLY-162, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=25840087; DOI=10.1093/pcp/pcv050;
RA   Toyokura K., Yamaguchi K., Shigenobu S., Fukaki H., Tatematsu K., Okada K.;
RT   "Mutations in plastidial 5-aminolevulinic acid biosynthesis genes suppress
RT   a pleiotropic defect in shoot development of a mitochondrial GABA shunt
RT   mutant in Arabidopsis.";
RL   Plant Cell Physiol. 56:1229-1238(2015).
CC   -!- FUNCTION: Transaminase converting glutamate 1-semialdehyde (GSA) to 5-
CC       aminolevulinate (ALA). Involved in the biosynthesis of tetrapyrroles.
CC       {ECO:0000250|UniProtKB:P42799}.
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; Evidence={ECO:0000250|UniProtKB:P42799};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P42799};
CC       Note=Can use both pyridoxamine 5'-phosphate (PMP) and pyridoxal 5'-
CC       phosphate (PLP) as cofactors. {ECO:0000250|UniProtKB:P42799};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC       {ECO:0000250|UniProtKB:P42799}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis. {ECO:0000250|UniProtKB:P42799}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P42799}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:25840087}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaf primordia and shoot apical
CC       meristems (SAM). {ECO:0000269|PubMed:25840087}.
CC   -!- DISRUPTION PHENOTYPE: Suppresses partially the ENF1 disruption
CC       pleiotropic developmental phenotypes, including the suppression of the
CC       abnormal patterning of the adaxial-abaxial-related gene expression in
CC       leaf primordia. {ECO:0000269|PubMed:25840087}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR   EMBL; U10278; AAA79123.1; -; Genomic_DNA.
DR   EMBL; AL133315; CAB62362.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78450.1; -; Genomic_DNA.
DR   EMBL; BT025324; ABF57280.1; -; mRNA.
DR   EMBL; AK229328; BAF01191.1; -; mRNA.
DR   PIR; T46217; T46217.
DR   RefSeq; NP_190442.1; NM_114732.5.
DR   AlphaFoldDB; Q42522; -.
DR   SMR; Q42522; -.
DR   BioGRID; 9352; 17.
DR   IntAct; Q42522; 1.
DR   STRING; 3702.Q42522; -.
DR   iPTMnet; Q42522; -.
DR   MetOSite; Q42522; -.
DR   PaxDb; 3702-AT3G48730-1; -.
DR   ProteomicsDB; 222313; -.
DR   EnsemblPlants; AT3G48730.1; AT3G48730.1; AT3G48730.
DR   GeneID; 824034; -.
DR   Gramene; AT3G48730.1; AT3G48730.1; AT3G48730.
DR   KEGG; ath:AT3G48730; -.
DR   Araport; AT3G48730; -.
DR   TAIR; AT3G48730; GSA2.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_016922_1_5_1; -.
DR   InParanoid; Q42522; -.
DR   OMA; RRCIKMS; -.
DR   OrthoDB; 1107811at2759; -.
DR   PhylomeDB; Q42522; -.
DR   BioCyc; ARA:AT3G48730-MONOMER; -.
DR   UniPathway; UPA00251; UER00317.
DR   UniPathway; UPA00668; -.
DR   PRO; PR:Q42522; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q42522; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
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; Q42522; AT.
PE   1: Evidence at protein level;
KW   Chlorophyll biosynthesis; Chloroplast; Isomerase; Plastid;
KW   Porphyrin biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..472
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000001256"
FT   MOD_RES         312
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42799"
FT   MUTAGEN         92
FT                   /note="R->K: In gsa2-1; suppression of enf1 mutant
FT                   pleiotropic developmental phenotypes; when associated with
FT                   S-162."
FT                   /evidence="ECO:0000269|PubMed:25840087"
FT   MUTAGEN         162
FT                   /note="G->S: In gsa2-1; suppression of enf1 mutant
FT                   pleiotropic developmental phenotypes; when associated with
FT                   K-92."
FT                   /evidence="ECO:0000269|PubMed:25840087"
FT   CONFLICT        16
FT                   /note="C -> S (in Ref. 1; AAA79123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="N -> K (in Ref. 1; AAA79123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        283
FT                   /note="F -> L (in Ref. 1; AAA79123)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  50142 MW;  E463699500B353FE CRC64;
     MAATLTGSGI ALGFSCSAKF SKRASSSSNR RCIKMSVSVE EKTKKFTLQK SEEAFNAAKN
     LMPGGVNSPV RAFKSVGGQP VVMDSAKGSR IRDIDGNEYI DYVGSWGPAI IGHADDEVLA
     ALAETMKKGT SFGAPCLLEN VLAEMVISAV PSIEMVRFVN SGTEACMGVL RLARAFTGKQ
     KFIKFEGCYH GHANSFLVKA GSGVATLGLP DSPGVPKAAT SDTLTAPYND IAAVEKLFEA
     NKGEIAAIIL EPVVGNSGFI TPKPEFIEGI RRITKDNGAL LIFDEVMTGF RLAYGGAQEY
     FGITPDLTTL GKIIGGGLPV GAYGGRRDIM EMVAPAGPMY QAGTLSGNPL AMTAGIHTLK
     RLSQPGTYEY LDKITKELTN GILEAGKKTG HAMCGGYISG MFGFFFTEGP VYDFSDAKKS
     DTEKFGKFFR GMLEEGVYLA PSQFEAGFTS LAHTSEDIQF TIAAAEKVLS RL
//