ID   GATP3_ORYSJ             Reviewed;         510 AA.
AC   Q6ZCF0; A0A0P0XD35;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable gamma-aminobutyrate transaminase 3, mitochondrial;
DE            EC=2.6.1.96;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os08g0205900, LOC_Os08g10510;
GN   ORFNames=OJ1119_C05.10, OsJ_26408, P0486F07.39;
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 [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   [2]
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   [3]
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   [4]
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: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AP003875; BAD11549.1; -; Genomic_DNA.
DR   EMBL; AP004565; BAD05337.1; -; Genomic_DNA.
DR   EMBL; AP008214; BAF23151.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT04302.1; -; Genomic_DNA.
DR   EMBL; CM000145; EEE68226.1; -; Genomic_DNA.
DR   RefSeq; XP_015648304.1; XM_015792818.1.
DR   AlphaFoldDB; Q6ZCF0; -.
DR   SMR; Q6ZCF0; -.
DR   STRING; 4530.OS08T0205900-01; -.
DR   PaxDb; Q6ZCF0; -.
DR   PRIDE; Q6ZCF0; -.
DR   EnsemblPlants; Os08t0205900-01; Os08t0205900-01; Os08g0205900.
DR   GeneID; 4344928; -.
DR   Gramene; Os08t0205900-01; Os08t0205900-01; Os08g0205900.
DR   KEGG; osa:4344928; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   HOGENOM; CLU_016922_4_1_1; -.
DR   InParanoid; Q6ZCF0; -.
DR   OMA; VYSSMDR; -.
DR   OrthoDB; 145181at2759; -.
DR   PlantReactome; R-OSA-1119458; Glutamate degradation.
DR   PlantReactome; R-OSA-1119610; Biotin biosynthesis II.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000007752; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   Genevisible; Q6ZCF0; 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   3: Inferred from homology;
KW   Aminotransferase; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..510
FT                   /note="Probable gamma-aminobutyrate transaminase 3,
FT                   mitochondrial"
FT                   /id="PRO_0000416852"
FT   BINDING         166..167
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         335
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   510 AA;  56008 MW;  EF9DD0B9F3781A41 CRC64;
     MICRSLLLLR SNAASKASNI VKHVAATGCL PKYSSEAPAR YFSSEPSLQV DSTEENGFKG
     HGMLAPFTAG WQSTDLHPLV IDRSEGSYVY DINGKKYIDA LAGLWSTALG GNEPRLIKAA
     TDQLNKLPFY HSFWNRTTKP SLDLANEILS MFTAREMGKI FFTNSGSEAN DSQVKLVWYY
     NNALGRPNKK KFIARSKSYH GSTLVSASLS GLPALHQKFD LPAPFVLHTD CPHYWRFHLP
     DETEEEFATR LATNLENLIL KEGPETIAAF IAEPVMGAGG VIPPPKTYFE KIQAVLKKYD
     ILLIADEVIT AFGRLGTMFG CDMYDIKPDL VSIAKALSSA YMPIGAILVS PEITDVIYSQ
     SNKLGSFAHG FTYSGHPVSC AVAIEALKIY KERNIIEHVQ KIAPRFQEGI KAFSGSPIVG
     EIRGLGLILG TEFVDNKSPN DPFPAEWGVG SLFGAECEKR GMLIRVAGDN IMLSPPLIMT
     PDEVEEIICK YGDALKATEE RIAELKAKRG