GSA2_ARATH
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 03-AUG-2022, entry version 159.
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},
GN HEML2 {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}.
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; 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.AT3G48730.1; -.
DR MetOSite; Q42522; -.
DR PaxDb; Q42522; -.
DR PRIDE; Q42522; -.
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; locus:2114520; AT3G48730.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_016922_1_5_1; -.
DR InParanoid; Q42522; -.
DR OMA; YHGHANS; -.
DR OrthoDB; 1160614at2759; -.
DR PhylomeDB; Q42522; -.
DR BioCyc; ARA:AT3G48730-MON; -.
DR UniPathway; UPA00251; UER00317.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q42522; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42522; baseline and differential.
DR Genevisible; Q42522; AT.
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; 3.40.640.10; -; 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; 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
