ID   PAL4_POPKI              Reviewed;         571 AA.
AC   Q40910;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Phenylalanine ammonia-lyase G4;
DE            EC=4.3.1.24;
DE   Flags: Fragment;
GN   Name=PALG4;
OS   Populus kitakamiensis (Aspen) (Populus sieboldii x Populus
OS   grandidentata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=34292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96011759; PubMed=7548831; DOI=10.1007/BF00032674;
RA   Osakabe Y., Osakabe K., Kawai S., Katayama Y., Morohoshi N.;
RT   "Characterization of the structure and determination of mRNA levels of
RT   the phenylalanine ammonia-lyase gene family from Populus
RT   kitakamiensis.";
RL   Plant Mol. Biol. 28:1133-1141(1995).
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; D43803; BAA07861.1; -; Genomic_DNA.
DR   HSSP; P21310; 1GK2.
DR   SMR; Q40910; 1-571.
DR   BRENDA; 4.3.1.5; 280164.
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   3: Inferred from homology;
KW   Cytoplasm; Lyase; Phenylpropanoid metabolism.
FT   CHAIN        <1    571       Phenylalanine ammonia-lyase G4.
FT                                /FTId=PRO_0000215415.
FT   MOD_RES      57     57       2,3-didehydroalanine (Ser) (By
FT                                similarity).
FT   CROSSLNK     56     58       5-imidazolinone (Ala-Gly) (By
FT                                similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   571 AA;  62484 MW;  6B76CC92D2DB425F CRC64;
     STHTLPHSAS RAAMLVRINT LLQGYSGIRF EILEAITKLL NHNITPCLPL RGTITASGDL
     VPLSYIAGLL TGRPNSKAVG PNGETMAAAE AFTLAGINGG FFELQPKEGL ALVNGTAVGS
     GLASMVLFET NVLAILSEVL SAIFAEVMQG KPEFTDHLTH KLKHHPGQIE AAAVMEHILD
     GSSYVKAAQK LHEIDPLQKP KQDRYALRTS PQWLGPLIEV IRTSTKMIER EINSVNDNPL
     IDVSRNKALH GGNFPGSPIG VSMDNTLVLA IASIGKLMFA QFSELVNDYY NNGLPSNLTG
     GRNPSLDYGF KGAEIAMASY CSELQFLANP VTNHVQSAEQ HNQDVNSLGL ISARKTAEAV
     EILNVMSTTW LVALCQAIDL RHIEENLKNT VKNTVSQVAK RVLTMGFNGE LHPSRFCEKD
     LLKVVDREYV FTYIDDPCSA TYPLMQKLRQ VLVDHALMNG EKEQNSSTSI FQKIGAFEEE
     LKILLPKEVE SARLELENGN PAIPNRITDR RSYPLYKFVR EELGTVLLTG EKVGSPGEEF
     DKVFTAICAG KLIDPCWSVL KEWNGAPLPL C
//