ID A0A0D3CTK3_BRAOL Unreviewed; 718 AA.
AC A0A0D3CTK3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0000256|ARBA:ARBA00012139, ECO:0000256|RuleBase:RU003955};
DE EC=4.3.1.24 {ECO:0000256|ARBA:ARBA00012139, ECO:0000256|RuleBase:RU003955};
GN Name=106300639 {ECO:0000313|EnsemblPlants:Bo6g067250.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo6g067250.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo6g067250.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo6g067250.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- FUNCTION: This is a key enzyme of plant metabolism catalyzing the first
CC reaction in the biosynthesis from L-phenylalanine of a wide variety of
CC natural products based on the phenylpropane skeleton.
CC {ECO:0000256|ARBA:ARBA00002235}.
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|ARBA:ARBA00023537,
CC 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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013592283.1; XM_013736829.1.
DR AlphaFoldDB; A0A0D3CTK3; -.
DR STRING; 109376.A0A0D3CTK3; -.
DR EnsemblPlants; Bo6g067250.1; Bo6g067250.1; Bo6g067250.
DR GeneID; 106300639; -.
DR Gramene; Bo6g067250.1; Bo6g067250.1; Bo6g067250.
DR KEGG; boe:106300639; -.
DR eggNOG; KOG0222; Eukaryota.
DR HOGENOM; CLU_014801_3_0_1; -.
DR OMA; VDIVSMM; -.
DR OrthoDB; 1030318at2759; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000032141; Chromosome C6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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:SF80; PHENYLALANINE AMMONIA-LYASE 2; 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 Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW Phenylpropanoid metabolism {ECO:0000256|ARBA:ARBA00023051,
KW ECO:0000256|RuleBase:RU003955};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141}.
SQ SEQUENCE 718 AA; 78069 MW; E84784BF1BB38D1E CRC64;
MDQTQNDNIE AMLCGGVEKT NVAVAADPLN WGAAAEQMKG SHLDEVKRMV EEYRRPVVNL
GGETLTIGQV AAISTVGNGV KVELAEASRD GVKASSDWVM ESMGKGTDSY GVTTGFGATS
HRRTKNGAAL QTELIRFLNA GIFGNTKETC HTLPESAPRA AMLVRVNTLL QGYSGIRFEI
LEAITSLLNH NISPSLPLRG TITASGDLVP LSYIAGLLTG RPNSKATGPN GESLTAEEAF
KQAGITSGFF DLQPKEGLAL VNGTAVGSGM ASMVLFEANV QSVLAEVLSA IFAEVMSGKP
EFTDHLTHRL KHHPGQIEAA AIMEHILDGS SYMKLAQKLH EMDPLQKPKQ DRYALRTSPQ
WLGPQIEVIR YATKSIEREI NSVNDNPLID VSRNKAIHGG NFQGTPIGVS MDNTRLAVAA
IGKLMFAQFS ELVNDFYNNG LPSNLTASNN PSLDYGFKGA EIAMASYCSE LQYLANPVTS
HVQSAEQHNQ DVNSLGLISS RKTSEAVDIL KLMSTTFLVA ICQAVDLRHL EENLRQAVKN
TVSQVAKKVL TTGVNGEMHP SRFCERDLLK VVDREQVFTY VDDPCSATYP LMQKLRQVIV
DQALANGETE KNVETSIFQK IGAFEEELKT VLPKEVDAAR EAYGNGNAAI PNRIKECRSY
PLYKFVREEL GTKLLTGEKV VSPGEEFDKV FTAMCEGKII DPLMDCLKEW NGAPIPIC
//