GATP1_ORYSJ
ID GATP1_ORYSJ Reviewed; 516 AA.
AC Q7XN11; A0A0P0WER1; Q71SH3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Gamma-aminobutyrate transaminase 1, mitochondrial;
DE EC=2.6.1.96;
DE Flags: Precursor;
GN Name=OSL2; OrderedLocusNames=Os04g0614600, LOC_Os04g52450;
GN ORFNames=OsJ_16145, OSJNBa0008M17.4;
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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Tainung 57; TISSUE=Leaf;
RX DOI=10.1111/j.1399-3054.2004.00430.x;
RA Ansari M.I., Lee R.H., Chen S.C.G.;
RT "A novel senescence-associated gene encoding -aminobutyric acid
RT (GABA):pyruvate transaminase is upregulated during rice leaf senescence.";
RL Physiol. Plantarum 123:1-8(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
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 [4]
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 [5]
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 [6]
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).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP FUNCTION.
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).
CC -!- FUNCTION: Transaminase that degrades gamma-amino butyric acid (GABA)
CC and uses pyruvate as amino-group acceptor, but not 2-oxoglutarate. Not
CC involved in the interaction with blast fungus.
CC {ECO:0000269|PubMed:16896530, ECO:0000269|Ref.1}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and panicles.
CC {ECO:0000269|Ref.1}.
CC -!- DEVELOPMENTAL STAGE: Strongly up-regulated during leaf senescence.
CC {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF297651; AAQ14479.1; -; mRNA.
DR EMBL; AL662950; CAE04333.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF15777.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90992.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE61676.1; -; Genomic_DNA.
DR EMBL; AK102306; BAG95492.1; -; mRNA.
DR RefSeq; XP_015636709.1; XM_015781223.1.
DR AlphaFoldDB; Q7XN11; -.
DR SMR; Q7XN11; -.
DR STRING; 4530.OS04T0614600-01; -.
DR PaxDb; Q7XN11; -.
DR PRIDE; Q7XN11; -.
DR EnsemblPlants; Os04t0614600-01; Os04t0614600-01; Os04g0614600.
DR GeneID; 4336983; -.
DR Gramene; Os04t0614600-01; Os04t0614600-01; Os04g0614600.
DR KEGG; osa:4336983; -.
DR eggNOG; KOG1404; Eukaryota.
DR HOGENOM; CLU_016922_4_1_1; -.
DR InParanoid; Q7XN11; -.
DR OMA; REGLNQH; -.
DR OrthoDB; 145181at2759; -.
DR BRENDA; 2.6.1.19; 4460.
DR BRENDA; 2.6.1.96; 4460.
DR PlantReactome; R-OSA-1119458; Glutamate degradation.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q7XN11; baseline and differential.
DR Genevisible; Q7XN11; OS.
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..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..516
FT /note="Gamma-aminobutyrate transaminase 1, mitochondrial"
FT /id="PRO_0000416848"
FT BINDING 171..172
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 340
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 516 AA; 56474 MW; DCC7AC57563C403B CRC64;
MVIARGLLRS NASSSSSQAI NLLKYVTSTG SLQGHTQNLC DASTRHFSSV PSPQYNSTEE
NGFKGHGMLA PFTAGWQSTD VHPLVIERSE GSYVYDIDGK KYLDSLAGLW CTALGGSEPR
LVKAATEQLH KLPFYHSFWN RTTKPSLDLA KELLSMFTAR EMGKVFFTNS GSEANDSQVK
LVWYYNNALG RPDKKKFIAR SKSYHGSTLI SASLSGLPAL HQKFDLPAPF VLHTDCPHYW
RFHLPGETEE EFATRLANNL EELILKEGPE TIAAFIAEPV MGAGGVIPPP KTYFEKVQAI
VKKYDILFIA DEVITAFGRL GTMFGSDMYN IKPDLVSMAK ALSSAYVPIG AIMVSPEISD
VIHSQSNKLG SFAHGFTYSG HPVACAVAIE ALKIYQERNI PDHVKQISPR FQEGVKAFAG
SPIVGEIRGV GLILGTEFAD NKSPNDPFPA EWGVGAIFGA ECQKRGMLVR VAGDNIMMSP
PLIMTPDEVE ELVSIYGDAL KATEERVAEL KSKKNN
