ID V4LN43_EUTSA Unreviewed; 725 AA.
AC V4LN43;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=EUTSA_v10010153mg {ECO:0000313|EMBL:ESQ45164.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ45164.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ45164.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(2013).
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|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; KI517435; ESQ45164.1; -; Genomic_DNA.
DR RefSeq; XP_006403711.1; XM_006403648.1.
DR AlphaFoldDB; V4LN43; -.
DR STRING; 72664.V4LN43; -.
DR EnsemblPlants; ESQ45164; ESQ45164; EUTSA_v10010153mg.
DR GeneID; 18021609; -.
DR Gramene; ESQ45164; ESQ45164; EUTSA_v10010153mg.
DR KEGG; eus:EUTSA_v10010153mg; -.
DR eggNOG; KOG0222; Eukaryota.
DR OMA; IYVLCQA; -.
DR OrthoDB; 1030318at2759; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000030689; Unassembled WGS sequence.
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:SF41; 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:UP000030689}.
SQ SEQUENCE 725 AA; 78555 MW; 9C8C88C5DF646EAD CRC64;
MDQINGLVHQ NGKIDAMLCG GVEKTKTAVT TVADPLNWGA AAEQMKGSHL DEVKRMVEEY
RRPVVNLGGE TLTIGQVAAI STVGGGVKVE LAEASRAGVK ASSDWVMESM GKGTDSYGVT
TGFGATSHRR TKNGTALQTE LIRFLNAGIF GNTKETCHTL PESATRAAML VRVNTLLQGF
SGIRFEILEA ITSFLNHNIS PSLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKATGPDGKP
LTAAEAFEKA GISSGFFDLQ PKEGLALVNG TAVGSGMASM VLFEANVQSV LAEVLSAIFA
EVMSGKPEFT DHLTHRLKHH PGQIEAAAIM EHILDGSSYM KLAQKLHEMD PLQKPKQDRY
ALRTSPQWLG PQIEVIRQAT KSIEREINSV NDNPLIDVSR NKAIHGGNFQ GTPIGVSMDN
TRLAIAAIGK LMFAQFSELV NDFYNNGLPS NLTASNNPSL DYGFKGAEIA MASYCSELQY
LANPVTSHVQ SAEQHNQDVN SLGLISSRKT SEAVDILKLM STTFLVAICQ AVDLRHLEEN
LRQTVKNTVS QVAKKVLTTG VNGELHPSRF CEKDLLKVVD REQVFTYVDD PCSATYPLMQ
KLRQVIVDHA LCNGETEKNV ATSIFQKIGA FEEELKATLP KEVEATRAAF GNGTAAIPNR
IKECRSYPLY KFVREELGTK LLTGEKVVSP GEEFDKVFTA MCEGKIIDPL MDCLKEWNGA
PIPIC
//