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Database: UniProt
Entry: G7JJ84_MEDTR
LinkDB: G7JJ84_MEDTR
Original site: G7JJ84_MEDTR 
ID   G7JJ84_MEDTR            Unreviewed;       393 AA.
AC   G7JJ84;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=arogenate dehydratase {ECO:0000256|ARBA:ARBA00013259};
DE            EC=4.2.1.91 {ECO:0000256|ARBA:ARBA00013259};
GN   Name=11438633 {ECO:0000313|EnsemblPlants:AES92641};
GN   OrderedLocusNames=MTR_4g132250 {ECO:0000313|EMBL:AES92641.1};
GN   ORFNames=MtrunA17_Chr4g0074991 {ECO:0000313|EMBL:RHN64980.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES92641.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES92641.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES92641.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES92641,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES92641.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES92641,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES92641}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES92641};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:RHN64980.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:RHN64980.1};
RA   Pecrix Y., Gamas P., Carrere S.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 0:0-0(2018).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC       phenylalanine from L-arogenate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004929}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000256|ARBA:ARBA00004470}.
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DR   EMBL; CM001220; AES92641.1; -; Genomic_DNA.
DR   EMBL; PSQE01000004; RHN64980.1; -; Genomic_DNA.
DR   RefSeq; XP_003610444.1; XM_003610396.2.
DR   AlphaFoldDB; G7JJ84; -.
DR   STRING; 3880.G7JJ84; -.
DR   PaxDb; 3880-AES92641; -.
DR   EnsemblPlants; AES92641; AES92641; MTR_4g132250.
DR   Gramene; AES92641; AES92641; MTR_4g132250.
DR   eggNOG; KOG2797; Eukaryota.
DR   HOGENOM; CLU_035008_4_0_1; -.
DR   OMA; CCTNQQH; -.
DR   OrthoDB; 2783975at2759; -.
DR   UniPathway; UPA00121; UER00344.
DR   Proteomes; UP000002051; Chromosome 4.
DR   Proteomes; UP000265566; Chromosome 4.
DR   ExpressionAtlas; G7JJ84; differential.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR   CDD; cd04905; ACT_CM-PDT; 1.
DR   CDD; cd13631; PBP2_Ct-PDT_like; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   PANTHER; PTHR21022:SF20; AROGENATE DEHYDRATASE_PREPHENATE DEHYDRATASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   Pfam; PF00800; PDT; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RHN64980.1};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT   DOMAIN          108..283
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          297..388
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   393 AA;  43235 MW;  38898BAB6C78E466 CRC64;
     MAFDLFLHKG AFIWGCSSKP HSQLDSHSGG LTDNLRYQLV HKCTILSVLA QKAAIPVEDE
     KPLVHSPPDD NALLHIHNKG FHKDINMLPK PLTSIDVSSS ASDGSKVRVA YQGLPGAYSE
     DAALKAYPKC ETVPCDEFEA AFKAVELWLV DKAVLPIENS IDGSIHRNYD LLLRHRLHIV
     GEVQLRVNHC LLGLPGVAKE ELKSVVSHPQ ALAQCEMVLN ELGVDKIGAH DTAAAAKTLA
     INCLRHNGAI ASSRAAKIYG LDILAEGIQD DDANVTRFLV LAREPIIPGT DRPYKTSIVF
     SIEEGPGVLF KALSVFSMRN INLAKIESRP LKQRPLRVVD DSNEGSAKYF DYLFYIDFEA
     SMAEPRAQNA LGQLQEIARF LRVLGCYPMD THV
//
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