ALAT1_ARATH
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 03-AUG-2022, entry version 76.
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.AT1G17290.1; -.
DR iPTMnet; F4I7I0; -.
DR MetOSite; F4I7I0; -.
DR SwissPalm; F4I7I0; -.
DR PaxDb; F4I7I0; -.
DR PRIDE; F4I7I0; -.
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; locus:2195808; AT1G17290.
DR eggNOG; KOG0258; Eukaryota.
DR HOGENOM; CLU_014254_3_0_1; -.
DR InParanoid; F4I7I0; -.
DR OMA; FGFECPP; -.
DR OrthoDB; 477122at2759; -.
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 Genevisible; F4I7I0; AT.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11751; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
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
