ID K3Y5M0_SETIT Unreviewed; 701 AA.
AC K3Y5M0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0000256|RuleBase:RU003955};
DE EC=4.3.1.24 {ECO:0000256|RuleBase:RU003955};
GN Name=101756300 {ECO:0000313|EnsemblPlants:KQK98115};
GN ORFNames=SETIT_7G168700v2 {ECO:0000313|EMBL:RCV34556.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV34556.1};
RN [1] {ECO:0000313|EMBL:RCV34556.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK98115,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV34556.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV34556.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV34556.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK98115}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK98115};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine = (E)-cinnamate + NH4(+);
CC Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58095; EC=4.3.1.24;
CC Evidence={ECO:0000256|RuleBase:RU003955};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005138, ECO:0000256|RuleBase:RU003955}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU003955}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family.
CC {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
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DR EMBL; AGNK02004429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003534; RCV34556.1; -; Genomic_DNA.
DR RefSeq; XP_004976240.1; XM_004976183.2.
DR AlphaFoldDB; K3Y5M0; -.
DR SMR; K3Y5M0; -.
DR STRING; 4555.K3Y5M0; -.
DR EnsemblPlants; KQK98115; KQK98115; SETIT_009509mg.
DR GeneID; 101756300; -.
DR Gramene; KQK98115; KQK98115; SETIT_009509mg.
DR KEGG; sita:101756300; -.
DR eggNOG; KOG0222; Eukaryota.
DR HOGENOM; CLU_014801_3_0_1; -.
DR InParanoid; K3Y5M0; -.
DR OMA; TMNPVGE; -.
DR OrthoDB; 355118at2759; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000004995; Chromosome VII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0009800; P:cinnamic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro.
DR CDD; cd00332; PAL-HAL; 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR InterPro; IPR001106; Aromatic_Lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR InterPro; IPR005922; Phe_NH3-lyase.
DR InterPro; IPR023144; Phe_NH3-lyase_shielding_dom_sf.
DR NCBIfam; TIGR01226; phe_am_lyase; 1.
DR PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR PANTHER; PTHR10362:SF11; PHENYLALANINE AMMONIA-LYASE; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU003954};
KW Phenylpropanoid metabolism {ECO:0000256|ARBA:ARBA00023051,
KW ECO:0000256|RuleBase:RU003955};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995}.
SQ SEQUENCE 701 AA; 75519 MW; DA7BE6B0CFABC837 CRC64;
MASNTAILES DPLNWGKAAA EMAGSHLDEV KRMVAQFREP LVKIEGSSLR VGQVAAVAAA
KDASGVAVEL DEDARPRVKA SSEWILDCIA HGGDIYGVTT GFGGTSHRRT KDGPALQVEL
LRHLNAGIFG NGSDGHTLPS EVSRAAMLVR INTLLQGYSG IRFEILEAIT KLINTGVSPC
LPLRGTITAS GDLVPLSYIA GLITGRPNAQ AVTVDGRKVD AAEAFKVAGI EGGFFKLNPK
EGLAIVNGTS VGSALGAMVC FDANVLAVLS EVLSAVFCEV MNGKPEYTDH LTHKLKHHPG
SIEAAAIMEH ILEGSSFMKH AKKVNELDPL LKPKQDRYAL RTSPQWLGPQ IEVIRAATKS
IEREVNSVND NPVIDVHRGK ALHGGNFQGT PIGVSMDNAR LAIANIGKLM FAQFSELVNE
FYNNGLTSNL AGSRNPSLDY GFKGTEIAMA SYCSELQYLG NPITNHVQSA EQHNQDVNSL
GLVSARKTAE AIDILKLMSS TYMVALCQAI DLRHLEENIK TSVKNTVTQV AKKVLTMNPV
GELSSARFSE KDIITAIDRE GVFTYAEDAA SASLPLMQKL RAVLVDHALS SGDAEREPSV
FSKITKFEEE LRAVLPREVE AARVAVAEGT APVANRIKDS RSFPVYRFVR EELGCVFLTG
EKLKSPGEEC NKVFIGISQG KLIDPMLECL KEWDGKPLPI C
//
