GATP3_SOLLC
ID GATP3_SOLLC Reviewed; 520 AA.
AC Q84P52;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Gamma aminobutyrate transaminase 3, chloroplastic;
DE AltName: Full=Gamma-aminobutyrate transaminase isozyme 3;
DE Short=LeGABA-TP3;
DE Short=SlGABA-T3;
DE EC=2.6.1.96;
DE Flags: Precursor;
GN Name=GABA-TP3; Synonyms=GABA-T3;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. MicroTom; TISSUE=Fruit;
RX PubMed=18713763; DOI=10.1093/pcp/pcn113;
RA Akihiro T., Koike S., Tani R., Tominaga T., Watanabe S., Iijima Y.,
RA Aoki K., Shibata D., Ashihara H., Matsukura C., Akama K., Fujimura T.,
RA Ezura H.;
RT "Biochemical mechanism on GABA accumulation during fruit development in
RT tomato.";
RL Plant Cell Physiol. 49:1378-1389(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. MicroTom;
RX PubMed=19470656; DOI=10.1093/jxb/erp161;
RA Clark S.M., Di Leo R., Van Cauwenberghe O.R., Mullen R.T., Shelp B.J.;
RT "Subcellular localization and expression of multiple tomato gamma-
RT aminobutyrate transaminases that utilize both pyruvate and glyoxylate.";
RL J. Exp. Bot. 60:3255-3267(2009).
CC -!- FUNCTION: Transaminase that degrades gamma-amino butyric acid (GABA)
CC and uses pyruvate or glyoxylate as amino-group acceptor. Cannot use
CC beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine,
CC glutamine, glutamate, valine, leucine, isoleucine, methionine,
CC phenylalanine, histidine, lysine, arginine, aspartate, threonine,
CC tyrosine, tryptophan, proline, or cysteine as amino donors.
CC {ECO:0000269|PubMed:19470656}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate + pyruvate = L-alanine + succinate
CC semialdehyde; Xref=Rhea:RHEA:32263, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57706, ChEBI:CHEBI:57972, ChEBI:CHEBI:59888; EC=2.6.1.96;
CC Evidence={ECO:0000269|PubMed:19470656};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate + glyoxylate = glycine + succinate
CC semialdehyde; Xref=Rhea:RHEA:32267, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.96;
CC Evidence={ECO:0000269|PubMed:19470656};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19470656}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, flowers and
CC fruits. {ECO:0000269|PubMed:18713763}.
CC -!- DEVELOPMENTAL STAGE: Decreased expression in the yellow and red fruits,
CC after the breaker stage. {ECO:0000269|PubMed:18713763,
CC ECO:0000269|PubMed:19470656}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AY240231; AAO92257.1; -; mRNA.
DR EMBL; AB359918; BAG16484.1; -; mRNA.
DR AlphaFoldDB; Q84P52; -.
DR SMR; Q84P52; -.
DR STRING; 4081.Solyc12g006450.1.1; -.
DR PaxDb; Q84P52; -.
DR PRIDE; Q84P52; -.
DR eggNOG; KOG1404; Eukaryota.
DR InParanoid; Q84P52; -.
DR BRENDA; 2.6.1.19; 3101.
DR BRENDA; 2.6.1.96; 3101.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q84P52; baseline.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central.
DR GO; GO:0034387; F:4-aminobutyrate:pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central.
DR GO; GO:0102351; F:gamma-aminobutyrate transaminase (glyoxylate dependent) activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IBA:GO_Central.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
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 PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Chloroplast; Plastid; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..520
FT /note="Gamma aminobutyrate transaminase 3, chloroplastic"
FT /id="PRO_0000416857"
FT BINDING 172..173
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 341
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 520 AA; 57239 MW; E4FCD1E922BD28F9 CRC64;
MAKITSLIGS GIVAATNQVG PHVKHIPAVG NLQKQIVSDQ IQVRWSSTET SLKNDISATD
VRGYKGHDML APFTAGWHST DLEPLVIQKS EGSYVYDVNG KKYLDALAGL WCTSLGGNEP
RLVAAATKQL NELAFYHSFW NRSTKPSLDL AKELLDLFTA NKMAKAFFTN SGSEANDTQV
KLVWYYNNAL GRPDKKKFIA RTKSYHGSTL ISASLSGLPA LHQQFDLPAP FVLHTDCPHF
WRFHQPGETE EEFSTRLANN LENLILKEGP ETIAAFIAEP VMGAGGVIPP PATYFEKVQA
ILKKYDILFI ADEVICGFGR LGTMFGCEKY NIKPDLVSVA KALSSGYMPI GAVLVSPEVS
DVIYSQSNKL GTFSHGFTYS GHPVSCAVAL ETLKIYKERN IIEQVNRISP KFQEGLKAFS
DSPIIGEIRG TGLLHGTEFT DNKSPNDPFP PEWGIGAYFG ARCEKHGVLV RVAGDNIMMS
PPYILSLEEI DELIIKYGKA LKDTENRVEE LKSQKKIKSS
