ALD1_ARATH
ID ALD1_ARATH Reviewed; 456 AA.
AC Q9ZQI7; Q93ZH8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Aminotransferase ALD1, chloroplastic;
DE EC=2.6.1.- {ECO:0000305};
DE AltName: Full=AGD2-like defense response protein 1 {ECO:0000303|PubMed:14729919};
DE Flags: Precursor;
GN Name=ALD1 {ECO:0000303|PubMed:14729919};
GN OrderedLocusNames=At2g13810 {ECO:0000312|Araport:AT2G13810};
GN ORFNames=F13J11.16 {ECO:0000312|EMBL:AAM15253.1};
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], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14729919; DOI=10.1105/tpc.019372;
RA Song J.T., Lu H., Greenberg J.T.;
RT "Divergent roles in Arabidopsis thaliana development and defense of two
RT homologous genes, aberrant growth and death2 and AGD2-LIKE DEFENSE RESPONSE
RT PROTEIN1, encoding novel aminotransferases.";
RL Plant Cell 16:353-366(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15447647; DOI=10.1111/j.1365-313x.2004.02200.x;
RA Song J.T., Lu H., McDowell J.M., Greenberg J.T.;
RT "A key role for ALD1 in activation of local and systemic defenses in
RT Arabidopsis.";
RL Plant J. 40:200-212(2004).
RN [6]
RP FUNCTION.
RX PubMed=19825557; DOI=10.1093/mp/ssn011;
RA Zhang Z., Lenk A., Andersson M.X., Gjetting T., Pedersen C., Nielsen M.E.,
RA Newman M.A., Hou B.H., Somerville S.C., Thordal-Christensen H.;
RT "A lesion-mimic syntaxin double mutant in Arabidopsis reveals novel
RT complexity of pathogen defense signaling.";
RL Mol. Plant 1:510-527(2008).
RN [7]
RP FUNCTION.
RX PubMed=18266921; DOI=10.1111/j.1365-313x.2008.03439.x;
RA Lee M.W., Jelenska J., Greenberg J.T.;
RT "Arabidopsis proteins important for modulating defense responses to
RT Pseudomonas syringae that secrete HopW1-1.";
RL Plant J. 54:452-465(2008).
RN [8]
RP INDUCTION.
RX PubMed=19054359; DOI=10.1111/j.1365-313x.2008.03756.x;
RA Ahlfors R., Brosche M., Kollist H., Kangasjaervi J.;
RT "Nitric oxide modulates ozone-induced cell death, hormone biosynthesis and
RT gene expression in Arabidopsis thaliana.";
RL Plant J. 58:1-12(2009).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21530897; DOI=10.1016/j.jgg.2011.03.001;
RA Nie H., Wu Y., Yao C., Tang D.;
RT "Suppression of edr2-mediated powdery mildew resistance, cell death and
RT ethylene-induced senescence by mutations in ALD1 in Arabidopsis.";
RL J. Genet. Genomics 38:137-148(2011).
RN [10]
RP FUNCTION.
RX PubMed=23221596; DOI=10.1105/tpc.112.103564;
RA Navarova H., Bernsdorff F., Doering A.C., Zeier J.;
RT "Pipecolic acid, an endogenous mediator of defense amplification and
RT priming, is a critical regulator of inducible plant immunity.";
RL Plant Cell 24:5123-5141(2012).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25372120; DOI=10.1094/mpmi-06-14-0187-r;
RA Cecchini N.M., Jung H.W., Engle N.L., Tschaplinski T.J., Greenberg J.T.;
RT "ALD1 regulates basal immune components and early inducible defense
RT responses in Arabidopsis.";
RL Mol. Plant Microbe Interact. 28:455-466(2015).
RN [12]
RP FUNCTION.
RX PubMed=27758894; DOI=10.1105/tpc.16.00486;
RA Ding P., Rekhter D., Ding Y., Feussner K., Busta L., Haroth S., Xu S.,
RA Li X., Jetter R., Feussner I., Zhang Y.;
RT "Characterization of a pipecolic acid biosynthesis pathway required for
RT systemic acquired resistance.";
RL Plant Cell 28:2603-2615(2016).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
RX PubMed=23385743; DOI=10.1107/s1744309112050270;
RA Sobolev V., Edelman M., Dym O., Unger T., Albeck S., Kirma M., Galili G.;
RT "Structure of ALD1, a plant-specific homologue of the universal
RT diaminopimelate aminotransferase enzyme of lysine biosynthesis.";
RL Acta Crystallogr. F 69:84-89(2013).
CC -!- FUNCTION: Aminotransferase involved in local and systemic acquired
CC resistance (SAR) to the bacterial pathogen P.syringae. Required for
CC salicylic acid (SA) and camalexin accumulation upon pathogen infection.
CC Possesses aminotransferase activity in vitro and may generate amino-
CC acid-derived defense signals in vivo. May be involved in ethylene-
CC induced senescence signaling. Involved in the biosynthesis of
CC pipecolate (Pip), a metabolite that orchestrates defense amplification,
CC positive regulation of SA biosynthesis, and priming to guarantee
CC effective local resistance induction and the establishment of SAR
CC (PubMed:23221596, PubMed:27758894). Converts lysine to alpha-keto-
CC epsilon-aminocaproate, which then can spontaneously cyclize to form
CC delta-(1)-piperideine-2-carboxylate (P2C). P2C is converted to Pip by
CC SARD4 (PubMed:27758894). May produce non-Pip metabolites that play
CC roles in immunity. Involved in the synthesis of distinct metabolite
CC signals that affect basal and early defenses, and later defense
CC responses (PubMed:25372120). {ECO:0000269|PubMed:14729919,
CC ECO:0000269|PubMed:15447647, ECO:0000269|PubMed:18266921,
CC ECO:0000269|PubMed:19825557, ECO:0000269|PubMed:21530897,
CC ECO:0000269|PubMed:23221596, ECO:0000269|PubMed:25372120,
CC ECO:0000269|PubMed:27758894}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:23385743};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:23385743};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:25372120}.
CC -!- TISSUE SPECIFICITY: Highly expressed in senescing leaves, flowers,
CC siliques and seeds. {ECO:0000269|PubMed:14729919,
CC ECO:0000269|PubMed:21530897}.
CC -!- INDUCTION: By ozone, benzothiadiazole (BTH) and infection with the
CC bacterial pathogen P.syringae pv. maculicola. Down-regulated by nitric
CC oxide. {ECO:0000269|PubMed:14729919, ECO:0000269|PubMed:15447647,
CC ECO:0000269|PubMed:19054359}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but during infection with virulent strain of P.syringae,
CC mutant plants have reduced levels of SA and camalexin, and show
CC increased susceptibility to pathogen. Leaves show decreased ethylene-
CC induced senescence. {ECO:0000269|PubMed:14729919,
CC ECO:0000269|PubMed:15447647, ECO:0000269|PubMed:21530897}.
CC -!- MISCELLANEOUS: Treatment with exogenous pipecolate (Pip) enhances
CC disease resistance to Pseudomonas syringae pv. maculicola
CC (PubMed:23221596). Plants over-expressing ALD1 exhibit resistance to
CC Pseudomonas syringae pv. maculicola (PubMed:25372120).
CC {ECO:0000269|PubMed:23221596, ECO:0000269|PubMed:25372120}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
CC {ECO:0000305}.
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DR EMBL; AY518702; AAR99910.1; -; mRNA.
DR EMBL; AC006218; AAD15433.2; -; Genomic_DNA.
DR EMBL; AC006436; AAM15253.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06261.1; -; Genomic_DNA.
DR EMBL; AY057526; AAL09766.1; -; mRNA.
DR EMBL; AY143898; AAN28837.1; -; mRNA.
DR PIR; A84511; A84511.
DR RefSeq; NP_565359.1; NM_126957.2.
DR PDB; 4FL0; X-ray; 2.30 A; A/B=1-456.
DR PDBsum; 4FL0; -.
DR AlphaFoldDB; Q9ZQI7; -.
DR SMR; Q9ZQI7; -.
DR STRING; 3702.AT2G13810.1; -.
DR PaxDb; Q9ZQI7; -.
DR PRIDE; Q9ZQI7; -.
DR ProteomicsDB; 244949; -.
DR EnsemblPlants; AT2G13810.1; AT2G13810.1; AT2G13810.
DR GeneID; 815864; -.
DR Gramene; AT2G13810.1; AT2G13810.1; AT2G13810.
DR KEGG; ath:AT2G13810; -.
DR Araport; AT2G13810; -.
DR TAIR; locus:2040481; AT2G13810.
DR eggNOG; KOG0257; Eukaryota.
DR HOGENOM; CLU_051433_0_0_1; -.
DR InParanoid; Q9ZQI7; -.
DR OMA; NFFNTRT; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q9ZQI7; -.
DR BioCyc; ARA:AT2G13810-MON; -.
DR BioCyc; MetaCyc:AT2G13810-MON; -.
DR BRENDA; 2.6.1.83; 399.
DR SABIO-RK; Q9ZQI7; -.
DR PRO; PR:Q9ZQI7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQI7; baseline and differential.
DR Genevisible; Q9ZQI7; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0062045; F:L-lysine alpha-aminotransferase; IMP:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0062034; P:L-pipecolic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:UniProtKB.
DR GO; GO:0009627; P:systemic acquired resistance; IDA:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR019942; DapL/ALD1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43144; PTHR43144; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03542; DAPAT_plant; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Chloroplast; Plant defense; Plastid;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..456
FT /note="Aminotransferase ALD1, chloroplastic"
FT /id="PRO_0000416859"
FT BINDING 108
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:23385743,
FT ECO:0007744|PDB:4FL0"
FT BINDING 142..143
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:23385743,
FT ECO:0007744|PDB:4FL0"
FT BINDING 223
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:23385743,
FT ECO:0007744|PDB:4FL0"
FT BINDING 251
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:23385743,
FT ECO:0007744|PDB:4FL0"
FT BINDING 254
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:23385743,
FT ECO:0007744|PDB:4FL0"
FT BINDING 281
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:23385743,
FT ECO:0007744|PDB:4FL0"
FT BINDING 283
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:23385743,
FT ECO:0007744|PDB:4FL0"
FT BINDING 292
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:23385743,
FT ECO:0007744|PDB:4FL0"
FT BINDING 323
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:23385743,
FT ECO:0007744|PDB:4FL0"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:4FL0"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:4FL0"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:4FL0"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:4FL0"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 231..244
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:4FL0"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 339..365
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:4FL0"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:4FL0"
FT HELIX 425..439
FT /evidence="ECO:0007829|PDB:4FL0"
SQ SEQUENCE 456 AA; 50577 MW; CA50F2170634E87B CRC64;
MVSLMFFSSA SPLCSSPSKI PKASLDFEMK KLGGSTKLVR NVNLEKLKNN YLFPEINRRE
LEHIEKHPNV QLISLGTGDT TEPIPEQITS HMSNFAHGLS TVEGYRGYGL EQGNKTLRKA
IAETFYRDLH VKSNEVFVSD GAQSDISRLQ LLLGSNVTIA VQDPTFPAYI DSSVIIGQTG
HFHEKTKKYQ NVVYMPCGPN NSFFPDLAMT PRTDVIFFCS PNNPTGYVAS RKQLHQLVDF
AKTNGSIIIF DSAYAAFIED GSPRSIYEIP GAREVAIEVS SFSKFAGFTG VRLGWSIIPD
ELLYSNGFPI INDFHRIVTT SFNGASNIAQ AGGLACLSSG GLKEIRSVNN YYKENRKILM
DTLVSLGLKV YGGVNAPYLW VHFKGSKSWD VFNEILENTH IITVPGSGFG PGGEEYLRIS
GFGRRDHIVE ASKRLQNFFN TRTKHFTYLS STSNTN
