GATP2_SOLLC
ID GATP2_SOLLC Reviewed; 458 AA.
AC Q84P53;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Gamma aminobutyrate transaminase 2;
DE AltName: Full=Gamma-aminobutyrate transaminase isozyme 2;
DE Short=LeGABA-TP2;
DE Short=SlGABA-T2;
DE EC=2.6.1.96;
GN Name=GABA-TP2; Synonyms=GABA-T2;
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. May be
CC responsible for establishing the GABA gradient in the carpel.
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: Cytoplasm {ECO:0000269|PubMed:19470656}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, flowers and
CC fruits. Expressed in carpels, but not in stamens.
CC {ECO:0000269|PubMed:18713763}.
CC -!- DEVELOPMENTAL STAGE: Loss of 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; AY240230; AAO92256.1; -; mRNA.
DR EMBL; AB359917; BAG16483.1; -; mRNA.
DR AlphaFoldDB; Q84P53; -.
DR SMR; Q84P53; -.
DR STRING; 4081.Solyc12g006470.1.1; -.
DR PaxDb; Q84P53; -.
DR PRIDE; Q84P53; -.
DR eggNOG; KOG1404; Eukaryota.
DR InParanoid; Q84P53; -.
DR BioCyc; MetaCyc:MON-15562; -.
DR BRENDA; 2.6.1.19; 3101.
DR BRENDA; 2.6.1.96; 3101.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q84P53; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; 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; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..458
FT /note="Gamma aminobutyrate transaminase 2"
FT /id="PRO_0000416856"
FT BINDING 114..115
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 283
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 458 AA; 50503 MW; 392338831521D37D CRC64;
MAKTNGFMGH DMLAPFTAAW MIDMGPLVID KAEGSYVYGV NGKKYLDSLS GLWCTVLGGS
EPRLIEAASK QLNKSAFYHS FWNRTTKPSL DLAKELINMF TANKMGKVFF TSSGSEANDT
QVKLVWYYNN AIGRPNKKKI ISRKNAYHGS TYMTAGLSGL PSLHLKFDLP PPYILHTDCP
HYWNYHLPGE TEEEYSTRLA NNLENLILKE GPETVAAFIA EPVMGGAGVI IPPATYFEKI
QAVLKKYDIL FIADEVICGF GRLGTMFGCD KYNIKPDLVS IAKALSGGYI PIGAVLVSEE
ISKVIMSQSN QLGVFCHGFT YSGHPVACAV ALEALKIYKE KNITEVVNKL SPKLQEGLKA
FIDSPIIGEI RGTGLVLSTE FVDNKSPNDP FPPEWGVGTY FGSQCQKHGM LVSFSGDHVN
MAPPFTLSLE ELDEMISIYG KALKDTEKRV EELKSQKK
