ID   D7KFD9_ARALL            Unreviewed;       542 AA.
AC   D7KFD9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=ARALYDRAFT_889133 {ECO:0000313|EMBL:EFH66476.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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; GL348713; EFH66476.1; -; Genomic_DNA.
DR   RefSeq; XP_002890217.1; XM_002890171.1.
DR   AlphaFoldDB; D7KFD9; -.
DR   STRING; 81972.D7KFD9; -.
DR   EnsemblPlants; scaffold_101927.1; scaffold_101927.1; scaffold_101927.1.
DR   GeneID; 9326279; -.
DR   Gramene; scaffold_101927.1; scaffold_101927.1; scaffold_101927.1.
DR   KEGG; aly:9326279; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0019481; P:L-alanine catabolic process, by transamination; IEA:EnsemblPlants.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants.
DR   GO; GO:0001666; P:response to hypoxia; IEA:EnsemblPlants.
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:SF29; ALANINE TRANSAMINASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EFH66476.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFH66476.1}.
FT   DOMAIN          166..528
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          43..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  59663 MW;  393C58B7B9C9014D CRC64;
     MRRFVIGQAK NLIDQSRRRQ HIHHKNLSFL SLLPPFSAPS DSSSRHLSSS SSEMSASDSS
     SSLPVTLDSI NPKVIKCEYA VRGEIVNIAQ RLQEDLKTNK DAYPFDEIIY CNIGNPQSLG
     QQPITFFREV LALCSHTALL DESATHGLFS SDSIERAWKI LDQIPGKATG AYSHSQGIKG
     LRDAIAAGIE ARDGFPADPN DIFMTDGASP GVHMMMQLLI TSEKDGILCP IPQYPLYSAS
     IALHGGTLVP YYLDEASGWG LEISELKKQL EDARSKGITV RALAVINPGN PTGQVLAEEN
     QRDIVDFCKQ EGLVLLADEV YQENVYVPDK KFHSFKKVAR SMGYGEKDLA LVSFQSVSKG
     YYGECGKRGG YMEVTGFTSD VREQIYKMAS VNLCSNISGQ ILASLIMSPP KPGDDSYESY
     IAEKDGILSS LARRAKTLEE ALNKLEGVTC NRAEGAMYLF PCLHLPQKAI AAAEAEKTAP
     DNFYCKRLLK ATGIVVVPGS GFRQVPGTWH FRCTILPQED KIPAIVDRLT AFHKSFMDEF
     RD
//