ID   PALY_CITLI              Reviewed;         722 AA.
AC   Q42667;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24;
GN   Name=PAL6;
OS   Citrus limon (Lemon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Sapindales; Rutaceae; Citrus.
OX   NCBI_TaxID=2708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seelenfreund D., Chiong M., Lobos S., Perez L.M.;
RT   "A full-length cDNA coding for phenylalanine ammonia-lyase from Citrus
RT   limon.";
RL   (er) Plant Gene Register PGR96-026.
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   -!- 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; U43338; AAB67733.1; -; mRNA.
DR   HSSP; P21310; 1GK2.
DR   SMR; Q42667; 29-720.
DR   BRENDA; 4.3.1.5; 66695.
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    722       Phenylalanine ammonia-lyase.
FT                                /FTId=PRO_0000215389.
FT   MOD_RES     207    207       2,3-didehydroalanine (Ser) (By
FT                                similarity).
FT   CROSSLNK    206    208       5-imidazolinone (Ala-Gly) (By
FT                                similarity).
SQ   SEQUENCE   722 AA;  78490 MW;  C96893196E30D9E5 CRC64;
     MELSHETCNG IKNDRNGGTS SLGLCTGTDP LNWTVAADSL KGSHLDEVKR MIDEYRRPVV
     KLGGESLTIG QVTAIAAHDS GVKVELAEAA RAGVKASSDW VMDSMMKGTD SYGVTTGFGA
     TSHRRTKQGG ALQKELIRFL NSGIFGNGTE SSHTLPHSAT RAAMLVRVNT LLQGYSGIRF
     EILETITKFL NHNITPCLPL RGTITASGDL VPLSYIAGLL TGRPNSKAVG SNGQVLNPTE
     AFNLAGVTSG FFELQPKEGL ALVNGTAVGS GLAATVLFEA NILAIMSEVL SAIFAEVMNG
     KPEFTDHLTH KLKHHPGQIE AAAIMEHILD GSSYVKAAQK LHETDPLQKP KQDRYALRTS
     PQWLGPQIEV IRAATKMIER EINSVNDNPL IDVSRNKALH GGNFQGTPIG VSMDNTRLAI
     ASIGKLMFAQ FSELVNDFYN NGLPSNLTGG RNPSLDYGFK GAEIAMASYC SELQFLANPV
     TNHVQSAEQH NQDVNSLGLN SSRKTAEAVD ILKLMSSTFL VALCQAIDLR HLEENLKNTV
     KNTVSQVAKR VLTMGVNGEL HPSRFCEKDL IKVVDREYVF AYIDDPCSAS SPLMQKLRQV
     LVDHALDNGD REKNSTTSIF QKIGAFEDEL KTLLPKEVEI ARTELESGNA AIPNRIKECR
     SYPLYKIVRE DIGTSLLTGE KVRSPGEEFD KVFTAMCEGK LIDPMLECLK EWNGAPLPIC
     QN
//