ID   PAL1_RUBID              Reviewed;         710 AA.
AC   Q9M568;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Phenylalanine ammonia-lyase 1;
DE            EC=4.3.1.24;
DE   AltName: Full=RiPAL1;
GN   Name=PAL1;
OS   Rubus idaeus (Raspberry).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Rosales; Rosaceae; Rosoideae; Rubus.
OX   NCBI_TaxID=32247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fruit;
RX   MEDLINE=21437948; PubMed=11553751; DOI=10.1104/pp.127.1.230;
RA   Kumar A., Ellis B.E.;
RT   "The phenylalanine ammonia-lyase gene family in raspberry. Structure,
RT   expression, and evolution.";
RL   Plant Physiol. 127:230-239(2001).
CC   -!- FUNCTION: This is a key enzyme of plant metabolism catalyzing the
CC       first reaction in the biosynthesis from L-phenylalanine of a wide
CC       variety of natural products based on the phenylpropane skeleton.
CC   -!- CATALYTIC ACTIVITY: L-phenylalanine = trans-cinnamate + ammonia.
CC   -!- PATHWAY: Phenylpropanoid metabolism; cinnamic acid biosynthesis;
CC       trans-cinnamic acid from L-phenylalanine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- DEVELOPMENTAL STAGE: Early fruit ripening.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO),
CC       which is formed autocatalytically by cyclization and dehydration
CC       of residues Ala-Ser-Gly (By similarity).
CC   -!- SIMILARITY: Belongs to the PAL/histidase family.
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DR   EMBL; AF237954; AAF40223.1; -; mRNA.
DR   HSSP; P21310; 1GKM.
DR   SMR; Q9M568; 19-709.
DR   BRENDA; 4.3.1.5; 81556.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016211; F:ammonia ligase activity; IEA:InterPro.
DR   GO; GO:0016841; F:ammonia-lyase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001106; Phe/His_NH3-lyase.
DR   InterPro; IPR005922; Phe_NH3-lyase.
DR   Pfam; PF00221; PAL; 1.
DR   TIGRFAMs; TIGR01226; phe_am_lyase; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Phenylpropanoid metabolism.
FT   CHAIN         1    710       Phenylalanine ammonia-lyase 1.
FT                                /FTId=PRO_0000215418.
FT   MOD_RES     197    197       2,3-didehydroalanine (Ser) (By
FT                                similarity).
FT   CROSSLNK    196    198       5-imidazolinone (Ala-Gly) (By
FT                                similarity).
SQ   SEQUENCE   710 AA;  77746 MW;  8ED569D63C0D5167 CRC64;
     MEFYKNGNGA VESFCEGHDP LNWNMAAESL KGSHVDELKR MVSDYRKPVV KLGGETLTIG
     QVAAIASHDG GVRVELSEEK RAGVKASSDW VMDSMGKGTD SYGVTTGFGA TSHRRTKNGG
     ALQRELIRFL NAGIFGSSLD STHKLPHTAT RAAMLVRFNT LLQGYSGIRF EILEAITKFL
     NGNITPCLPL RGTITASGDL VPLSYIAGLL IGRPNSKSVG PKGETLSPAE GFKLAGIDGG
     FFELQPKEGL ALVNGTAVGS GMASMVLFDA NTLAVLSEVM SAIFAEVMQG KPEFTDHLTH
     KLKHHPGQIE AAAIMEHILE GSSYVKEAKK VHEMDPLQKP KQDRYALRTS PQWLGPQIEV
     IRAATKMIER EINSVNDNPL IDVSRNKALH GGNFQELPIG VAMDNTRLAI ASIGKLIFAQ
     FSELVNDYYN NGLPSILTGS SNPSLDYGFK GAEIAMASYC SELQFLANPV TNHVQSAEQH
     NQDVNSLGLI SSRKTSEAVD ILKLMSSTFL VALCQAIDLR HLEENLKIVV KTTVSNVAKR
     TLTVSPNGEL HPSRFSEKDL LTVVDREYLF SYIDDPCLAT YPLMQKLRAE LVEHALKNGE
     RERSANTSIF HKIAAFEEEL KTILPKEVDN ARIEIENGKS EIPNRIKECR SYPLYRFVRE
     ELGTSLLTGE KIKSPGEECY KVFNAICAGK LVDPLLECLK EWNGAPLPIS
//