ID   GATP3_ORYSI             Reviewed;         510 AA.
AC   B8BBZ7;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Probable gamma-aminobutyrate transaminase 3, mitochondrial;
DE            EC=2.6.1.96;
DE   Flags: Precursor;
GN   ORFNames=OsI_28220;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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; CM000133; EEC83087.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8BBZ7; -.
DR   SMR; B8BBZ7; -.
DR   STRING; 39946.B8BBZ7; -.
DR   EnsemblPlants; BGIOSGA027464-TA; BGIOSGA027464-PA; BGIOSGA027464.
DR   Gramene; BGIOSGA027464-TA; BGIOSGA027464-PA; BGIOSGA027464.
DR   HOGENOM; CLU_016922_4_1_1; -.
DR   OMA; VYSSMDR; -.
DR   Proteomes; UP000007015; Chromosome 8.
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; -; 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_0000416853"
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;  55956 MW;  FED8B743930D91E9 CRC64;
     MICRSLLLLR SNAASKASSI VKHVAATGCL PEYSSEAPAR YFSSESSLQV 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
     PDEVEEIISK YGDALKATEE RIAELKAKRG