ID   ALA2_PANMI              Reviewed;         482 AA.
AC   P34106;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Alanine aminotransferase 2;
DE            Short=ALAAT-2;
DE            EC=2.6.1.2;
DE   AltName: Full=Glutamate pyruvate transaminase 2;
DE            Short=GPT;
DE   AltName: Full=Glutamic--alanine transaminase 2;
DE   AltName: Full=Glutamic--pyruvic transaminase 2;
OS   Panicum miliaceum (Proso millet) (Broomcorn millet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX   NCBI_TaxID=4540;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 197-206 AND 308-317.
RC   TISSUE=Leaf;
RX   PubMed=1450385; DOI=10.1007/bf00046455;
RA   Son D., Sugiyama T.;
RT   "Molecular cloning of an alanine aminotransferase from NAD-malic enzyme
RT   type C4 plant Panicum miliaceum.";
RL   Plant Mol. Biol. 20:705-713(1992).
CC   -!- FUNCTION: Transfer of C3 units between the cytosol of mesophyll and
CC       bundle sheath cells to maintain a nitrogen-carbon balance in the C4-
CC       dicarboxylic pathway.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mesophyll and bundle sheath cells.
CC   -!- INDUCTION: By light.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X69421; CAA49199.1; -; mRNA.
DR   PIR; S28429; S28429.
DR   AlphaFoldDB; P34106; -.
DR   SMR; P34106; -.
DR   BioCyc; MetaCyc:MONOMER-17674; -.
DR   SABIO-RK; P34106; -.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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   1: Evidence at protein level;
KW   Aminotransferase; Direct protein sequencing; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..482
FT                   /note="Alanine aminotransferase 2"
FT                   /id="PRO_0000123940"
FT   MOD_RES         299
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   482 AA;  52682 MW;  FB6562233A0D3E21 CRC64;
     MAATVAVENL NPKVLKCEYA VRGEIVIHAQ HLQQQLQTQP GSLPFDEILY CNIGNPQSLG
     QQPVTFFREV LALCDHPCLL EKEETKSLFS ADAISRAKQI LSTIPGRATG AYSHSQGIKG
     LRDAIAAGIA SRDGFPANAD DIFVTDGASP GVHMMMQLLI RNEKDGILCP IPQYPLYSAS
     IALHGGTLVP YYLDEKTGWG LEISDLKKQL EDARSKGIDV RALVVINPGN PTGQVLAEDN
     QCDIVRFCKN EGLVLLADEV YQENIYVDDK KFNSFKKIAR SVGYGEDDLP LVSFQSVSKG
     YYGECGKRGG YMEITGFSAP VREQIYKIAS VNLCSNITGQ ILASLVMNPP KVGDESYAAY
     KAEKDGILQS LARRAKALED AFNNLEGISC NKAEGAMYLF PQIHLPKKAI EAAKAANKAP
     DAFYALRLLE STGIVVVPGS GFGQVPGTWH IRCTILPQED KIPAVITRFK AFHEAFMAEY
     RD
//