GATP4_ORYSJ
ID GATP4_ORYSJ Reviewed; 483 AA.
AC Q6ZH29; A0A0P0VDU8; B9F225; Q9AXI9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable gamma-aminobutyrate transaminase 4;
DE Short=OsGABA-T;
DE EC=2.6.1.96;
GN Name=GABA-T; OrderedLocusNames=Os02g0112900, LOC_Os02g02210;
GN ORFNames=OJ1399_H05.13, OsJ_05081;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16896530; DOI=10.1007/s10265-006-0018-3;
RA Wu C., Zhou S., Zhang Q., Zhao W., Peng Y.;
RT "Molecular cloning and differential expression of an gamma-aminobutyrate
RT transaminase gene, OsGABA-T, in rice (Oryza sativa) leaves infected with
RT blast fungus.";
RL J. Plant Res. 119:663-669(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Transaminase that degrades gamma-amino butyric acid (GABA).
CC {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Not detected in roots, stems, flowers or leaves of
CC healthy plants. {ECO:0000269|PubMed:16896530}.
CC -!- INDUCTION: Up-regulated by blast fungus, UV, mechanical wounding,
CC salicylic acid and abscisic acid, but not by methyl jasmonate.
CC {ECO:0000269|PubMed:16896530}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE56165.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF324485; AAK11219.1; -; mRNA.
DR EMBL; AP004090; BAD07632.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07574.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS76627.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE56165.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015624768.1; XM_015769282.1.
DR AlphaFoldDB; Q6ZH29; -.
DR SMR; Q6ZH29; -.
DR STRING; 4530.OS02T0112900-00; -.
DR PaxDb; Q6ZH29; -.
DR PRIDE; Q6ZH29; -.
DR EnsemblPlants; Os02t0112900-00; Os02t0112900-00; Os02g0112900.
DR GeneID; 4328053; -.
DR Gramene; Os02t0112900-00; Os02t0112900-00; Os02g0112900.
DR KEGG; osa:4328053; -.
DR eggNOG; KOG1404; Eukaryota.
DR HOGENOM; CLU_016922_4_1_1; -.
DR InParanoid; Q6ZH29; -.
DR OMA; YGVFIMG; -.
DR OrthoDB; 145181at2759; -.
DR BRENDA; 2.6.1.96; 4460.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6ZH29; OS.
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 PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..483
FT /note="Probable gamma-aminobutyrate transaminase 4"
FT /id="PRO_0000416854"
FT BINDING 138..139
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 307
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 273
FT /note="I -> N (in Ref. 1; AAK11219)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="G -> E (in Ref. 1; AAK11219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 53070 MW; FD987B510747F3A2 CRC64;
MTTPHGLLQY SSGAFSDQVP ADDSAEEHGV KDHAMLAPFT AAWQTAISPP LVIERSEGCY
VYDVNGTKYL DALAGLLSTA LGGSEPRLVK AATEQLNKLP FYHSFWNHTT RPSLDLAKEL
ISMFTAREMG KVFFTNSGSE ANDSQVKIVW YYNNALGRPK KKNIISRTQS YHGTTFISAS
LSGLPTLHQD FDLPGRFVLH TDCPHYWRFH LPGETEEEFA TRLADNLENL ILKQGPETIA
AFIAEPVIGA GGVILPPKTY FEKIQAVVKK YDILFIVDEV ITGFGRLGTM FGSDLYNIKP
DLVSLAKALS SAYAPIGAIL VSPEISDVIH SHSNKLGTFA HGFTYSGHPV SCAVALEALK
IYRERDIPGH VTHVAQRFQE GIKAFAAGSP IVGETRGVGL LIATEFTDNK SPYELFPFEW
GVGEIFGQEC KKRGMMVKVL GNLIAMSPPL IITREEIDKL VSIYGEALKA TEERVAELKS
KKN
