ID   ALD1_ORYSJ              Reviewed;         440 AA.
AC   Q6VMN7; Q8H7W8;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Aminotransferase ALD1 homolog;
DE            EC=2.6.1.-;
GN   Name=ALD1; OrderedLocusNames=Os03g0195100, LOC_Os03g09910;
GN   ORFNames=OSJNBa0064E16.9;
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].
RX   PubMed=14729919; DOI=10.1105/tpc.019372;
RA   Song J.T., Lu H., Greenberg J.T.;
RT   "Divergent roles in Arabidopsis thaliana development and defense of two
RT   homologous genes, aberrant growth and death2 and AGD2-LIKE DEFENSE RESPONSE
RT   PROTEIN1, encoding novel aminotransferases.";
RL   Plant Cell 16:353-366(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
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).
CC   -!- FUNCTION: Probable aminotransferase that may generate amino-acid-
CC       derived defense signals and be involved in resistance to pathogens.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN59772.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY338236; AAR01226.1; -; mRNA.
DR   EMBL; AC105731; AAN59772.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000009; ABF94441.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF11169.1; -; Genomic_DNA.
DR   EMBL; AP014959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015630783.1; XM_015775297.1.
DR   AlphaFoldDB; Q6VMN7; -.
DR   SMR; Q6VMN7; -.
DR   STRING; 4530.OS03T0195100-00; -.
DR   PaxDb; Q6VMN7; -.
DR   PRIDE; Q6VMN7; -.
DR   EnsemblPlants; Os03t0195100-01; Os03t0195100-01; Os03g0195100.
DR   GeneID; 4331930; -.
DR   Gramene; Os03t0195100-01; Os03t0195100-01; Os03g0195100.
DR   KEGG; osa:4331930; -.
DR   eggNOG; KOG0257; Eukaryota.
DR   InParanoid; Q6VMN7; -.
DR   OrthoDB; 683031at2759; -.
DR   PlantReactome; R-OSA-1119419; Lysine biosynthesis VI.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01642; DapL_aminotrans_1; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR019942; DapL/ALD1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43144; PTHR43144; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03542; DAPAT_plant; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase; Plant defense; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..440
FT                   /note="Aminotransferase ALD1 homolog"
FT                   /id="PRO_0000416860"
FT   BINDING         104
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   440 AA;  47761 MW;  87DFD5D5F85441D5 CRC64;
     MPVNMISKLL EKAVLPALDV APPVKIGGPR RTSVLRNPNM EKLQKGYLFP EISIKREEHL
     KKYPDAKVIS LGIGDTTEPI PSIVTSAMAE YALALSTPEG YQGYGPEQGH KNLRKEIADK
     VYPDMGIKES EVFISDGAQC DIARLQTLFG PNVTIAVQDP TFPGYVDNGV IMGQTGKADD
     GGRYAGIEYM RCAPENAFFP DLSRVRRTDV IFFCSPNNPT GHAASREQLR QLVELARRNG
     SIIVFDSAYS SYISSSSSSS TPRSIYEIPG AREVAIEVSS FSKFAGFTGV RLGWAVVPDE
     LLYSDGVPVA RDFDRVVCTC FNGASGIAQA GGVACLSTEE GRGAVARVVG VYRENARVLV
     ETFRSLGKEV HGGGDAPYVW VRFPGRRSWD VFAEILEKTH VITVPGSGFG PGGEGFIRVS
     AFNSRDKVLE ACQRLKSFLA