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 25-OCT-2017, entry version 92. 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; Magnoliophyta; 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, RP TISSUE 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 RT 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., RA Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., RA Weng Q., Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., RA Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., RA Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., RA Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., RA Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., RA Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., RA Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., RA 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., RA McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., RA Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L., RA Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T., RA Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using RT next 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., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., RA 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- RT aminobutyrate transaminase gene, OsGABA-T, in rice (Oryza sativa) RT leaves infected with blast fungus."; RL J. Plant Res. 119:663-669(2006). CC -!- FUNCTION: Transaminase that degrades gamma-amino butyric acid CC (GABA) and uses pyruvate as amino-group acceptor, but not 2- CC oxoglutarate. Not involved in the interaction with blast fungus. CC {ECO:0000269|PubMed:16896530, ECO:0000269|Ref.1}. CC -!- CATALYTIC ACTIVITY: 4-aminobutanoate + pyruvate = succinate CC semialdehyde + L-alanine. CC -!- CATALYTIC ACTIVITY: 4-aminobutanoate + glyoxylate = succinate CC semialdehyde + glycine. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Os.14095; -. DR ProteinModelPortal; Q7XN11; -. DR SMR; Q7XN11; -. DR STRING; 39947.LOC_Os04g52450.1; -. 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; ENOG410IR3Y; Eukaryota. DR eggNOG; COG0161; LUCA. DR InParanoid; Q7XN11; -. DR KO; K16871; -. DR OMA; FRIAPPI; -. DR OrthoDB; EOG093606SH; -. DR BRENDA; 2.6.1.19; 4460. DR BRENDA; 2.6.1.96; 4460. 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:0034387; F:4-aminobutyrate:pyruvate transaminase activity; IEA:UniProtKB-EC. 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 CDD; cd00610; OAT_like; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2. 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; Complete proteome; Mitochondrion; KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. FT TRANSIT 1 47 Mitochondrion. {ECO:0000255}. FT CHAIN 48 516 Gamma-aminobutyrate transaminase 1, FT mitochondrial. FT /FTId=PRO_0000416848. FT REGION 171 172 Pyridoxal phosphate binding. FT {ECO:0000250}. FT BINDING 204 204 Substrate. {ECO:0000250}. FT BINDING 311 311 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 340 340 Substrate. {ECO:0000250}. FT MOD_RES 340 340 N6-(pyridoxal phosphate)lysine. FT {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 //