ID   ALAT1_ARATH             Reviewed;         543 AA.
AC   F4I7I0; Q56Z96; Q94BP8; Q9LKJ4; Q9LN15;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Alanine aminotransferase 1, mitochondrial {ECO:0000303|PubMed:17319845};
DE            Short=AtAlaAT1 {ECO:0000303|PubMed:17319845};
DE            Short=AtAlaATc {ECO:0000305};
DE            EC=2.6.1.2 {ECO:0000269|PubMed:17319845};
DE   AltName: Full=Alanine-2-oxoglutarate aminotransferase 4 {ECO:0000303|PubMed:12631323};
DE            EC=2.6.1.- {ECO:0000269|PubMed:17319845};
DE   Flags: Precursor;
GN   Name=ALAAT1 {ECO:0000303|PubMed:17319845};
GN   Synonyms=AOAT4 {ECO:0000303|PubMed:12631323};
GN   OrderedLocusNames=At1g17290 {ECO:0000312|Araport:AT1G17290};
GN   ORFNames=T13M22.3 {ECO:0000312|EMBL:AAF79891.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. C24;
RA   Ismond K.P., Dennis E.S., Dolferus R.;
RT   "Cloning and characterization of Arabidopsis alanine aminotransferase
RT   genes.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 75-543.
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-543.
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-543.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12631323; DOI=10.1046/j.1365-313x.2003.01688.x;
RA   Igarashi D., Miwa T., Seki M., Kobayashi M., Kato T., Tabata S.,
RA   Shinozaki K., Ohsumi C.;
RT   "Identification of photorespiratory glutamate:glyoxylate aminotransferase
RT   (GGAT) gene in Arabidopsis.";
RL   Plant J. 33:975-987(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY HYPOXIC
RP   STRESS, AND DISRUPTION PHENOTYPE.
RX   PubMed=17319845; DOI=10.1111/j.1365-313x.2006.03023.x;
RA   Miyashita Y., Dolferus R., Ismond K.P., Good A.G.;
RT   "Alanine aminotransferase catalyses the breakdown of alanine after hypoxia
RT   in Arabidopsis thaliana.";
RL   Plant J. 49:1108-1121(2007).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-56, CLEAVAGE OF TRANSIT PEPTIDE
RP   [LARGE SCALE ANALYSIS] AFTER MET-55, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Is the major alanine aminotransferase in roots that catalyzes
CC       the conversion of alanine to pyruvate (PubMed:17319845). Involved in
CC       the rapid conversion of alanine to pyruvate during recovery from low-
CC       oxygen stress (PubMed:17319845). {ECO:0000269|PubMed:17319845}.
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         Evidence={ECO:0000269|PubMed:17319845};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19454;
CC         Evidence={ECO:0000269|PubMed:17319845};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q93ZN9};
CC   -!- PATHWAY: Photosynthesis; C4 acid pathway. {ECO:0000305}.
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q93ZN9}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots and shoots, mostly in
CC       vascular tissues, and, to a lower extent, in flowers and leaves.
CC       {ECO:0000269|PubMed:12631323, ECO:0000269|PubMed:17319845}.
CC   -!- INDUCTION: Rapidly induced upon low-oxygen stress in roots and shoots.
CC       {ECO:0000269|PubMed:17319845}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Strong overall decrease of alanine
CC       aminotransferase activity, especially in roots.
CC       {ECO:0000269|PubMed:17319845}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD94892.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF275372; AAF82782.1; -; mRNA.
DR   EMBL; AC026479; AAF79891.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29570.1; -; Genomic_DNA.
DR   EMBL; AY039970; AAK64147.2; -; mRNA.
DR   EMBL; AK221072; BAD94892.1; ALT_INIT; mRNA.
DR   PIR; D86309; D86309.
DR   RefSeq; NP_173173.3; NM_101591.6.
DR   AlphaFoldDB; F4I7I0; -.
DR   SMR; F4I7I0; -.
DR   BioGRID; 23541; 13.
DR   IntAct; F4I7I0; 1.
DR   STRING; 3702.F4I7I0; -.
DR   iPTMnet; F4I7I0; -.
DR   MetOSite; F4I7I0; -.
DR   SwissPalm; F4I7I0; -.
DR   PaxDb; 3702-AT1G17290-1; -.
DR   ProMEX; F4I7I0; -.
DR   ProteomicsDB; 244994; -.
DR   DNASU; 838301; -.
DR   EnsemblPlants; AT1G17290.1; AT1G17290.1; AT1G17290.
DR   GeneID; 838301; -.
DR   Gramene; AT1G17290.1; AT1G17290.1; AT1G17290.
DR   KEGG; ath:AT1G17290; -.
DR   Araport; AT1G17290; -.
DR   TAIR; AT1G17290; ALAAT1.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   InParanoid; F4I7I0; -.
DR   OMA; KARETSC; -.
DR   OrthoDB; 5472891at2759; -.
DR   BRENDA; 2.6.1.2; 399.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
DR   PRO; PR:F4I7I0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4I7I0; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR   GO; GO:0019481; P:L-alanine catabolic process, by transamination; IMP:TAIR.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR   GO; GO:0001666; P:response to hypoxia; IEP:TAIR.
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.
DR   Genevisible; F4I7I0; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Aminotransferase; Mitochondrion; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..55
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           56..543
FT                   /note="Alanine aminotransferase 1, mitochondrial"
FT                   /id="PRO_0000416042"
FT   REGION          43..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         209..210
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         235
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         291
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         322
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         354..356
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         369
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         397
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   MOD_RES         56
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         360
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   CONFLICT        307
FT                   /note="K -> N (in Ref. 1; AAF82782)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   543 AA;  59821 MW;  4ED08F2CA3414E4B CRC64;
     MRRFVIGQAK NLIDQSRRRQ LHHHKNLSFV SLIPPFSAPS DSSSRHLSSS SSSDMSASDS
     SSSLPVTLDT INPKVIKCEY AVRGEIVNIA QKLQEDLKTN KDAYPFDEII YCNIGNPQSL
     GQQPITFFRE VLALCSYTAL LDESATHGLF SSDSIERAWK ILDQIPGRAT GAYSHSQGIK
     GLRDAIADGI EARDGFPADP NDIFMTDGAS PGVHMMMQLL ITSEKDGILC PIPQYPLYSA
     SIALHGGTLV PYYLDEASGW GLEISELKKQ LEDARSKGIT VRALAVINPG NPTGQVLSEE
     NQRDVVKFCK QEGLVLLADE VYQENVYVPD KKFHSFKKVA RSMGYGEKDL ALVSFQSVSK
     GYYGECGKRG GYMEVTGFTS DVREQIYKMA SVNLCSNISG QILASLIMSP PKPGDDSYES
     YIAEKDGILS SLARRAKTLE EALNKLEGVT CNRAEGAMYL FPCLHLPQKA IAAAEAEKTA
     PDNFYCKRLL KATGIVVVPG SGFRQVPGTW HFRCTILPQE DKIPAIVDRL TAFHQSFMDE
     FRD
//