DAAA_ARATH
ID DAAA_ARATH Reviewed; 373 AA.
AC Q8L493; Q9FJM9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=D-amino-acid transaminase, chloroplastic {ECO:0000303|PubMed:18318836};
DE EC=2.6.1.21;
DE EC=4.1.3.38;
DE AltName: Full=Aminodeoxychorismate lyase {ECO:0000303|PubMed:15500462};
DE Short=AtADCL;
DE AltName: Full=Branched-chain-amino-acid aminotransferase-like protein 3;
DE Flags: Precursor;
GN Name=DAAT {ECO:0000303|PubMed:18318836}; Synonyms=BCAL3;
GN OrderedLocusNames=At5g57850 {ECO:0000312|Araport:AT5G57850};
GN ORFNames=MTI20.10 {ECO:0000303|PubMed:9734815};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=15500462; DOI=10.1111/j.1365-313x.2004.02231.x;
RA Basset G.J., Ravanel S., Quinlivan E.P., White R., Giovannoni J.J.,
RA Rebeille F., Nichols B.P., Shinozaki K., Seki M., Gregory J.F.,
RA Hanson A.D.;
RT "Folate synthesis in plants: the last step of the p-aminobenzoate branch is
RT catalyzed by a plastidial aminodeoxychorismate lyase.";
RL Plant J. 40:453-461(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=18318836; DOI=10.1111/j.1742-4658.2008.06279.x;
RA Funakoshi M., Sekine M., Katane M., Furuchi T., Yohda M., Yoshikawa T.,
RA Homma H.;
RT "Cloning and functional characterization of Arabidopsis thaliana D-amino
RT acid aminotransferase--D-aspartate behavior during germination.";
RL FEBS J. 275:1188-1200(2008).
CC -!- FUNCTION: Amino acid aminotransferase showing activity for D-Asp and D-
CC Ala as amino donors with 2-oxoglutarate as an amino acceptor. Can also
CC use D-Met, D-Tyr, D-Phe, D-Gln, D-Trp and D-Asn as substrates, but no
CC activity with L-Asp, L-Ala, L-Leu, L-Ile or L-Val. Catalyzes also the
CC reverse reaction where an amino group is transferred from D-Glu to
CC pyruvate or oxaloacetate to produce D-Ala or D-Asp, respectively. Also
CC involved in folate biosynthesis, acting as an aminodeoxychorismate
CC lyase converting 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate
CC (PABA)(PubMed:15500462). {ECO:0000269|PubMed:15500462,
CC ECO:0000269|PubMed:18318836}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + D-alanine = D-glutamate + pyruvate;
CC Xref=Rhea:RHEA:15869, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29986, ChEBI:CHEBI:57416; EC=2.6.1.21;
CC Evidence={ECO:0000269|PubMed:18318836};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate;
CC Xref=Rhea:RHEA:16201, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:58406; EC=4.1.3.38;
CC Evidence={ECO:0000269|PubMed:15500462};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:18318836};
CC -!- ACTIVITY REGULATION: Inhibited by hydroxylamine or amino-oxyacetic
CC acid. {ECO:0000269|PubMed:18318836}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for D-aspartate {ECO:0000269|PubMed:18318836};
CC KM=1.0 mM for D-alanine {ECO:0000269|PubMed:18318836};
CC KM=27 mM for 2-oxoglutarate {ECO:0000269|PubMed:18318836};
CC KM=4.0 mM for D-glutamate {ECO:0000269|PubMed:18318836};
CC Vmax=2.5 umol/min/mg enzyme with D-aspartate as substrate
CC {ECO:0000269|PubMed:18318836};
CC Vmax=5 umol/min/mg enzyme with D-alanine as substrate
CC {ECO:0000269|PubMed:18318836};
CC Vmax=3.3 umol/min/mg enzyme with D-glutamate as substrate
CC {ECO:0000269|PubMed:18318836};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000303|PubMed:15500462}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15500462}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08855.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB013396; BAB08855.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96959.1; -; Genomic_DNA.
DR EMBL; AY099783; AAM20634.1; -; mRNA.
DR EMBL; AY128874; AAM91274.1; -; mRNA.
DR RefSeq; NP_001330897.1; NM_001345276.1.
DR RefSeq; NP_200593.2; NM_125170.5.
DR AlphaFoldDB; Q8L493; -.
DR SMR; Q8L493; -.
DR STRING; 3702.AT5G57850.1; -.
DR PaxDb; Q8L493; -.
DR PRIDE; Q8L493; -.
DR ProteomicsDB; 224698; -.
DR EnsemblPlants; AT5G57850.1; AT5G57850.1; AT5G57850.
DR GeneID; 835895; -.
DR Gramene; AT5G57850.1; AT5G57850.1; AT5G57850.
DR KEGG; ath:AT5G57850; -.
DR Araport; AT5G57850; -.
DR TAIR; locus:2174433; AT5G57850.
DR eggNOG; KOG0975; Eukaryota.
DR HOGENOM; CLU_020844_0_0_1; -.
DR InParanoid; Q8L493; -.
DR OrthoDB; 853728at2759; -.
DR PhylomeDB; Q8L493; -.
DR BioCyc; ARA:AT5G57850-MON; -.
DR BioCyc; MetaCyc:AT5G57850-MON; -.
DR BRENDA; 2.6.1.21; 399.
DR SABIO-RK; Q8L493; -.
DR UniPathway; UPA00077; UER00150.
DR PRO; PR:Q8L493; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L493; baseline and differential.
DR Genevisible; Q8L493; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0047810; F:D-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
DR GO; GO:0008153; P:para-aminobenzoic acid biosynthetic process; IDA:TAIR.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Chloroplast; Lyase; Plastid; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..373
FT /note="D-amino-acid transaminase, chloroplastic"
FT /id="PRO_0000001279"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 128
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 255
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT MOD_RES 222
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P19938"
SQ SEQUENCE 373 AA; 41065 MW; A0A1076FFA6CAD7D CRC64;
MAGLSLEFTV NTWNLRSLSQ VPCPLRHGFR FPRRLTRRRT ILMCSDSSSQ SWNVPVLSSY
EVGERLKLAR GGQQFLAMYS SVVDGITTDP AAMVLPLDDH MVHRGHGVFD TALIINGYLY
ELDQHLDRIL RSASMAKIPL PFDRETIKRI LIQTVSVSGC RDGSLRYWLS AGPGDFLLSP
SQCLKPTLYA IVIKTNFAIN PIGVKVVTSS IPIKPPEFAT VKSVNYLPNV LSQMEAEAKG
AYAGIWVCKD GFIAEGPNMN VAFVVNGGKE LVMPRFDNVL SGCTAKRTLT LAEQLVSKGI
LKTVKVMDVT VEDGKKADEM MLIGSGIPIR PVIQWDEEFI GEGKEGPIAK ALLDLLLEDM
RSGPPSVRVL VPY
