ID   PAL2_IPOBA              Reviewed;         708 AA.
AC   Q42858;
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;
DE            EC=4.3.1.24;
OS   Ipomoea batatas (Sweet potato) (Batate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Beniazuma; TISSUE=Root;
RA   Tanaka Y.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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; D78640; BAA11459.1; -; mRNA.
DR   PIR; T10909; T10909.
DR   HSSP; P21310; 1GKM.
DR   SMR; Q42858; 18-708.
DR   BRENDA; 4.3.1.5; 21210.
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    708       Phenylalanine ammonia-lyase.
FT                                /FTId=PRO_0000215394.
FT   MOD_RES     195    195       2,3-didehydroalanine (Ser) (By
FT                                similarity).
FT   CROSSLNK    194    196       5-imidazolinone (Ala-Gly) (By
FT                                similarity).
SQ   SEQUENCE   708 AA;  77383 MW;  C10F736C41F1BEC6 CRC64;
     MEGAIANGHT NDFCIKVDPL NWEMAADSLK GSHLDEVKRM VAEFRNPAVK IGGQTLTSLR
     SPPIAARDNA SKWSSPRLPA RRESSSDWVM NSMNNGTDSY GVTTGFGATS HRRTKNGHAL
     QQELIRFLNA GIFGTGTGAS HTLPHSATRA AMLVRINTLL QGYSGIRFEI LEAITKLLNH
     NITPCLPLRG TITASGDLVP LSYIAGLLTG RPNSKAVGPN GEALTAEEAF KLAGVQGGFF
     ELQPKEGLAL VNGTAVGSGM ASMVLFEANV LAVLSEVLSA IFAEVMNGKP EFTDHLTHKL
     KHHPGQIEAA AIMEHILDRS YYMKAAQKLH EMDPLQKPKQ DRYALRTSPQ WLGPQIEVIR
     QATKMIEREI NSVNDNPLID VSRNKALHGG NFQGTPIGVS MDNSRLALAS IGKLIFAQFS
     ELVNDYYNNG LPSNLTAGRN PSLDYGFKGV EIAMASYCSE LQFLANPVTN HVQSAEQHNQ
     DVNSLGLISA RKTAEAVDVL KLMSSTYLVA LCQAIDLRHL EENLKNAVRN TVNQVAKRTL
     TMGVNGELHP SRFCEKDLLR VVDREYVFAY ADDPCSANYP LFQKLRQVLV DHALQNGEHE
     KNVSTSIFQK IAAFEDELKA VLPKEVEGAR SAIENGNPAI PNRITECRSY PLYKFVREEL
     GTEMLTGEKV KSPGEVCDKV FTAVCDGGII DPLLECLKSW DGAPLPIC
//