ID   Q9S768_ORYSA            Unreviewed;       483 AA.
AC   Q9S768;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
OS   Oryza sativa (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4530 {ECO:0000313|EMBL:BAA77261.1};
RN   [1] {ECO:0000313|EMBL:BAA77261.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10080717; DOI=10.1023/A:1006156214716;
RA   Kikuchi H., Hirose S., Toki S., Akama K., Takaiwa F.;
RT   "Molecular characterization of a gene for alanine aminotransferase from
RT   rice (Oryza sativa).";
RL   Plant Mol. Biol. 39:149-159(1999).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00025708}.
CC   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC       {ECO:0000256|ARBA:ARBA00025709}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000256|ARBA:ARBA00025785}.
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DR   EMBL; AB007404; BAA77260.1; -; Genomic_DNA.
DR   EMBL; AB007405; BAA77261.1; -; mRNA.
DR   AlphaFoldDB; Q9S768; -.
DR   SMR; Q9S768; -.
DR   EnsemblPlants; Os10t0390500-01; Os10t0390500-01; Os10g0390500.
DR   Gramene; Os10t0390500-01; Os10t0390500-01; Os10g0390500.
DR   OMA; KARETSC; -.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
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:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR045088; ALAT1/2-like.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11751; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF479; ALANINE TRANSAMINASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase {ECO:0000313|EMBL:BAA77261.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAA77261.1}.
FT   DOMAIN          108..463
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   483 AA;  52593 MW;  CA78A2545E48F850 CRC64;
     MAAPSVAVDN LNPKVLNCEY AVRGEIVIHA QRLQQQLQTQ PGSLPFDEIL YCNIGNPQSL
     GQKPVTFFRE VIALCDHPCL LEKEETKSLF SADAISRATT ILASIPGRAT GAYSHSQGIK
     GLRDAIAAGI ASRDGYPANA DDIFLTDGAS PGVHMMMQLL IRNEKDGILC PIPQYPLYSA
     SIALHGGALV PYYLNESTGW GLEISDLKKQ LEDSRLKGID VRALVVINPG NPTGQVLAEE
     NQRDIVKFCK NEGLVLLADE VYQENIYVDN KKFNSFKKIA RSMGYNEDDL PLVSFQSVSK
     GYYGECGKRG GYMEITGFSA PVREQIYKVA SVNLCSNITG QILASLVMNP PKAGDASYAS
     YKAEKDGILQ SLARRAKALE NAFNSLEGIT CNKTEGAMYL FPQLSLPQKA IDAAKAANKA
     PDAFYALRLL EATGIVVVPG SGFGQVPGTW HIRCTILPQE EKIPAIISRF KAFHEGFMAA
     YRD
//