ID   GATP2_ORYSJ             Reviewed;         497 AA.
AC   Q7XN12; A0A0P0WF20;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Probable gamma-aminobutyrate transaminase 2, mitochondrial;
DE            EC=2.6.1.96;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os04g0614500, LOC_Os04g52440; ORFNames=OSJNBa0008M17.3;
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=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   [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 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).
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; AL662950; CAE04332.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF15776.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS90991.1; -; Genomic_DNA.
DR   EMBL; AK100259; BAG94519.1; -; mRNA.
DR   RefSeq; XP_015635718.1; XM_015780232.1.
DR   AlphaFoldDB; Q7XN12; -.
DR   SMR; Q7XN12; -.
DR   STRING; 4530.OS04T0614500-01; -.
DR   PaxDb; Q7XN12; -.
DR   PRIDE; Q7XN12; -.
DR   EnsemblPlants; Os04t0614500-01; Os04t0614500-01; Os04g0614500.
DR   GeneID; 4336982; -.
DR   Gramene; Os04t0614500-01; Os04t0614500-01; Os04g0614500.
DR   KEGG; osa:4336982; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   HOGENOM; CLU_016922_4_1_1; -.
DR   InParanoid; Q7XN12; -.
DR   OMA; ARRHVFE; -.
DR   OrthoDB; 145181at2759; -.
DR   BRENDA; 2.6.1.96; 4460.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   Genevisible; Q7XN12; 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   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; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..497
FT                   /note="Probable gamma-aminobutyrate transaminase 2,
FT                   mitochondrial"
FT                   /id="PRO_0000416850"
FT   BINDING         153..154
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         322
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  54019 MW;  DB24DB6F728F2CC4 CRC64;
     MNLIKHAAFA ASFQGETDCT SHASARKFST SGSSPLLDST EGNGFKGHSM LAPFTAGWHS
     TDLEPLIIER SEGSYVYDSK GNKYLDTLAG LWCTALGGSE PRLVKAATDQ LNKLPFYHSF
     WNSTAKPPLD LAEELISMFT AKEMGKVFFT NSGSEANDSQ VKLVWYYNNA LGRPNKKKII
     AQSQAYHGST LISASLSGLP AMHLKFDLPA PFVLHTDCPH YWRFGLPGEA EEEFATRLAD
     NLENLILKEG PETVAAFIAE PVIGAGGVIP PPKTYFEKIQ AVLQKYDVLF IADEVITGFG
     RLGTMFGSDL YNIKPDLVSL AKALSSAYVP IGATLVSPEI SDVVHSQSNK IGFFAHGFTY
     SGHPVSCAVA LEALKIYRER NIPAHVKQIS PRFQEGIKAF AGSSIIGETR GVGLLLATEF
     ANNKSPNDPF PVEWGVAQIF GAECKKRGML VKVVGDEIAM SPPLIMSQRE VDGLVSIYGE
     ALKATEERVA ELRSKKK