ALAT2_ARATH
ID ALAT2_ARATH Reviewed; 540 AA.
AC Q9LDV4; F4IDA2; F4IDA4; Q94C83; Q9C7S4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Alanine aminotransferase 2, mitochondrial;
DE Short=AtAlaAT2;
DE Short=AtAlaATm;
DE EC=2.6.1.2;
DE AltName: Full=Alanine-2-oxoglutarate aminotransferase 3;
DE EC=2.6.1.-;
DE Flags: Precursor;
GN Name=ALAAT2; Synonyms=AOAT3; OrderedLocusNames=At1g72330;
GN ORFNames=T10D10.20, T9N14.10;
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] (ISOFORM 1).
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].
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 9-540 (ISOFORM 1).
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 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 [6]
RP TISSUE SPECIFICITY, AND INDUCTION BY HYPOXIC STRESS.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-46.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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 Evidence={ECO:0000250};
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25732537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LDV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LDV4-2; Sequence=VSP_042467;
CC -!- TISSUE SPECIFICITY: Expressed in shoots, essentially in leaves and
CC flowers, mostly in vascular tissues. Also detected in stems and roots.
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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. Alanine aminotransferase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51787.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE35307.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF275371; AAF82781.1; -; mRNA.
DR EMBL; AC016529; AAG52580.1; -; Genomic_DNA.
DR EMBL; AC067754; AAG51787.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35305.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35306.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35307.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY035086; AAK59591.2; -; mRNA.
DR PIR; B96747; B96747.
DR RefSeq; NP_001077811.1; NM_001084342.1. [Q9LDV4-2]
DR RefSeq; NP_001185380.1; NM_001198451.1.
DR RefSeq; NP_565040.2; NM_105892.5. [Q9LDV4-1]
DR AlphaFoldDB; Q9LDV4; -.
DR SMR; Q9LDV4; -.
DR BioGRID; 28785; 13.
DR STRING; 3702.AT1G72330.3; -.
DR PaxDb; Q9LDV4; -.
DR PRIDE; Q9LDV4; -.
DR ProteomicsDB; 244868; -. [Q9LDV4-1]
DR EnsemblPlants; AT1G72330.1; AT1G72330.1; AT1G72330. [Q9LDV4-1]
DR EnsemblPlants; AT1G72330.2; AT1G72330.2; AT1G72330. [Q9LDV4-2]
DR GeneID; 843565; -.
DR Gramene; AT1G72330.1; AT1G72330.1; AT1G72330. [Q9LDV4-1]
DR Gramene; AT1G72330.2; AT1G72330.2; AT1G72330. [Q9LDV4-2]
DR KEGG; ath:AT1G72330; -.
DR Araport; AT1G72330; -.
DR eggNOG; KOG0258; Eukaryota.
DR InParanoid; Q9LDV4; -.
DR OMA; YGEKDVC; -.
DR OrthoDB; 477122at2759; -.
DR PhylomeDB; Q9LDV4; -.
DR BRENDA; 2.6.1.2; 399.
DR UniPathway; UPA00322; -.
DR UniPathway; UPA00528; UER00586.
DR PRO; PR:Q9LDV4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LDV4; baseline and differential.
DR Genevisible; Q9LDV4; AT.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
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 GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
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 Alternative splicing; Aminotransferase; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 47..540
FT /note="Alanine aminotransferase 2, mitochondrial"
FT /id="PRO_0000416043"
FT REGION 11..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 357
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 410..540
FT /note="PGDDSYDSYMAERDGILSSMAKRAKTLEDALNSLEGVTCNRAEGAMYLFPRI
FT NLPQKAIEAAEAEKTAPDAFYCKRLLNATGVVVVPGSGFGQVPGTWHFRCTILPQEDKI
FT PAIVNRLTEFHKSFMDEFRN -> KEMEFSHPWLNVQRLWKTLSTV (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042467"
FT CONFLICT 265
FT /note="K -> E (in Ref. 4; AAK59591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 59511 MW; 4D1D4D4102CBD661 CRC64;
MRRFLINQAK GLVDHSRRQH HHKSPSFLSP QPRPLASSPP ALSRFFSSTS EMSASDSTSS
LPVTLDSINP KVLKCEYAVR GEIVNIAQKL QEDLKTNKDA YPFDEIIYCN IGNPQSLGQL
PIKFFREVLA LCDHASLLDE SETHGLFSTD SIDRAWRILD HIPGRATGAY SHSQGIKGLR
DVIAAGIEAR DGFPADPNDI FLTDGASPAV HMMMQLLLSS EKDGILSPIP QYPLYSASIA
LHGGSLVPYY LDEATGWGLE ISDLKKQLEE ARSKGISVRA LVVINPGNPT GQVLAEENQR
DIVNFCKQEG LVLLADEVYQ ENVYVPDKKF HSFKKVARSL GYGEKDISLV SFQSVSKGYY
GECGKRGGYM EVTGFTSDVR EQIYKMASVN LCSNISGQIL ASLVMSPPKP GDDSYDSYMA
ERDGILSSMA KRAKTLEDAL NSLEGVTCNR AEGAMYLFPR INLPQKAIEA AEAEKTAPDA
FYCKRLLNAT GVVVVPGSGF GQVPGTWHFR CTILPQEDKI PAIVNRLTEF HKSFMDEFRN
