AROD4_ARATH
ID AROD4_ARATH Reviewed; 424 AA.
AC O22241;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Arogenate dehydratase 4, chloroplastic {ECO:0000303|PubMed:17726025};
DE Short=AtADT4 {ECO:0000303|PubMed:17726025};
DE EC=4.2.1.91 {ECO:0000269|PubMed:17726025};
DE Flags: Precursor;
GN Name=ADT4 {ECO:0000303|PubMed:17726025};
GN OrderedLocusNames=At3g44720 {ECO:0000312|Araport:AT3G44720};
GN ORFNames=T32N15.11 {ECO:0000312|EMBL:AAB70035.1};
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. Columbia;
RA Matringe M., Grisollet D., Rippert P.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=17726025; DOI=10.1074/jbc.m702662200;
RA Cho M.-H., Corea O.R.A., Yang H., Bedgar D.L., Laskar D.D., Anterola A.M.,
RA Moog-Anterola F.A., Hood R.L., Kohalmi S.E., Bernards M.A., Kang C.,
RA Davin L.B., Lewis N.G.;
RT "Phenylalanine biosynthesis in Arabidopsis thaliana. Identification and
RT characterization of arogenate dehydratases.";
RL J. Biol. Chem. 282:30827-30835(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19136569; DOI=10.1104/pp.108.130070;
RA Rippert P., Puyaubert J., Grisollet D., Derrier L., Matringe M.;
RT "Tyrosine and phenylalanine are synthesized within the plastids in
RT Arabidopsis.";
RL Plant Physiol. 149:1251-1260(2009).
CC -!- FUNCTION: Converts the prephenate produced from the shikimate-
CC chorismate pathway into phenylalanine. {ECO:0000269|PubMed:17726025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-arogenate = CO2 + H2O + L-phenylalanine;
CC Xref=Rhea:RHEA:12536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58095, ChEBI:CHEBI:58180; EC=4.2.1.91;
CC Evidence={ECO:0000269|PubMed:17726025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12537;
CC Evidence={ECO:0000269|PubMed:17726025};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.08 mM for arogenate {ECO:0000269|PubMed:17726025};
CC Vmax=52.32 pmol/sec/ug enzyme with arogenate as substrate
CC {ECO:0000269|PubMed:17726025};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC phenylalanine from L-arogenate: step 1/1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19136569}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. More abundant in stems and roots.
CC {ECO:0000269|PubMed:17726025}.
CC -!- MISCELLANEOUS: Has no detectable prehenate dehydratase activity.
CC {ECO:0000269|PubMed:17726025}.
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DR EMBL; DQ411467; ABD67753.1; -; mRNA.
DR EMBL; AC002534; AAB70035.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77939.1; -; Genomic_DNA.
DR EMBL; AY062692; AAL32770.1; -; mRNA.
DR EMBL; BT008862; AAP68301.1; -; mRNA.
DR RefSeq; NP_190058.1; NM_114340.4.
DR AlphaFoldDB; O22241; -.
DR SMR; O22241; -.
DR BioGRID; 8921; 10.
DR IntAct; O22241; 13.
DR STRING; 3702.AT3G44720.1; -.
DR PaxDb; O22241; -.
DR PRIDE; O22241; -.
DR ProteomicsDB; 246959; -.
DR EnsemblPlants; AT3G44720.1; AT3G44720.1; AT3G44720.
DR GeneID; 823601; -.
DR Gramene; AT3G44720.1; AT3G44720.1; AT3G44720.
DR KEGG; ath:AT3G44720; -.
DR Araport; AT3G44720; -.
DR TAIR; locus:2101630; AT3G44720.
DR eggNOG; KOG2797; Eukaryota.
DR HOGENOM; CLU_035008_4_1_1; -.
DR InParanoid; O22241; -.
DR OMA; SHAIPKR; -.
DR OrthoDB; 1090069at2759; -.
DR PhylomeDB; O22241; -.
DR BioCyc; ARA:AT3G44720-MON; -.
DR BRENDA; 4.2.1.91; 399.
DR SABIO-RK; O22241; -.
DR UniPathway; UPA00121; UER00344.
DR PRO; PR:O22241; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O22241; baseline and differential.
DR Genevisible; O22241; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047769; F:arogenate dehydratase activity; IDA:TAIR.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEP:TAIR.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR Pfam; PF00800; PDT; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Lyase; Phenylalanine biosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..424
FT /note="Arogenate dehydratase 4, chloroplastic"
FT /id="PRO_0000373793"
FT DOMAIN 126..303
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 319..410
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 424 AA; 45925 MW; B12A05BE6C0A0D24 CRC64;
MQAATSCDLK FRSTDPTSRN KCFSHAIPKR VAVTCGYRSE SFSFPNGVSV SRSDWQSSCA
ILSSKVASVE NTGGLADKIA AVNGHTNGSV NLGLVAVEST NGKLAPAQPL TITDLSPAPL
HGSSLRVAYQ GVPGAYSEAA AGKAYPNCDA IPCDQFDVAF QAVELWIADR AVLPVENSLG
GSIHRNYDLL LRHRLHIVGE VQIPVHHCLL ALPGVRTDCV SRVISHPQAL AQTEHSLDVL
TPHAAREAFH DTAAAAEYIS ANDLHDTAAV ASARAAELYN LQILADGIQD DPGNVTRFLM
LAREPIIPRT DRPFKTSIVF AAQEHKGTSV LFKVLSAFAF RDISLTKIES RPHHNRPLRV
VGDGSFGTSK NFEYMFYVDF EASMAEPRAQ NALAEVQEYT SFLRVLGSYP MDMTPWSMTS
TEEA
