GATP1_SOLLC
ID GATP1_SOLLC Reviewed; 515 AA.
AC Q84P54;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Gamma aminobutyrate transaminase 1, mitochondrial;
DE AltName: Full=Gamma-aminobutyrate transaminase isozyme 1;
DE Short=LeGABA-TP1;
DE Short=SlGABA-T1;
DE EC=2.6.1.96;
DE Flags: Precursor;
GN Name=GABA-TP1; Synonyms=GABA-T1;
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, TISSUE SPECIFICITY, 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. Acts
CC predominantly in vegetative tissues. {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: Mitochondrion {ECO:0000269|PubMed:19470656}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, flowers and
CC fruits. {ECO:0000269|PubMed:18713763, ECO:0000269|PubMed:19470656}.
CC -!- DEVELOPMENTAL STAGE: Continuous expression during the fruit
CC development. {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; AY240229; AAO92255.1; -; mRNA.
DR EMBL; AB359916; BAG16482.1; -; mRNA.
DR RefSeq; NP_001234336.2; NM_001247407.2.
DR AlphaFoldDB; Q84P54; -.
DR SMR; Q84P54; -.
DR STRING; 4081.Solyc07g043310.2.1; -.
DR PaxDb; Q84P54; -.
DR PRIDE; Q84P54; -.
DR ProMEX; Q84P54; -.
DR GeneID; 543873; -.
DR KEGG; sly:543873; -.
DR eggNOG; KOG1404; Eukaryota.
DR InParanoid; Q84P54; -.
DR OrthoDB; 145181at2759; -.
DR BioCyc; MetaCyc:MON-15561; -.
DR BRENDA; 2.6.1.19; 3101.
DR BRENDA; 2.6.1.96; 3101.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q84P54; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; 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; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..57
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 58..515
FT /note="Gamma aminobutyrate transaminase 1, mitochondrial"
FT /id="PRO_0000416855"
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 515 AA; 56749 MW; 6984D5B23F93D84C CRC64;
MAKISRLFGS TVKAAITAQA GFHGKRIPAV SSLQEHIVKS TPARYNSTQA CLENDISGTD
NKGFKGHDML APFTAGWQST DVDPLIIEKS EGSHVYDMQG RKYIDTLAGL WCTALGGNEP
RLVDAATKQL NTLPFYHSFW NRTTKPSLDL AKELLDMFTA KKMAKAFFTN SGSEANDTQV
KLVWYYNNAL GRPNKKKFIA RAKAYHGSTL ISASLTGLPA LHQNFDLPAP FVLHTDCPHY
WRYHLPGETE EEFSTRLAKN LEDLILKEGP ETIAAFIAEP VMGAGGVIPP PATYFDKIQA
VVKKYDILFI ADEVICAFGR LGTMFGSDMY NIKPDLVTLA KALSSAYMPI GAVLVSPEVS
DVIHSQSNKL GSFSHGFTYS GHPVACAVAL EAIKIYKERN MVERVNRISP KFQEGLKAFS
DSPIIGEIRG LGLILATEFA NNKSPNDHFP PEWGVGAYFG AQCQKNGMLV RVAGDTIMMS
PPFVVTPEEL DELIRIYGKA LRETEKRVEE LKSQK
