ID PAL2_POPKI Reviewed; 710 AA. AC Q43052; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 58. DE RecName: Full=Phenylalanine ammonia-lyase G2B; DE EC=4.3.1.24; GN Name=PALG2B; 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D43802; BAA07860.1; -; Genomic_DNA. DR HSSP; P21310; 1GKM. DR SMR; Q43052; 20-710. 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 1 710 Phenylalanine ammonia-lyase G2B. FT /FTId=PRO_0000215414. FT MOD_RES 198 198 2,3-didehydroalanine (Ser) (By FT similarity). FT CROSSLNK 197 199 5-imidazolinone (Ala-Gly) (By FT similarity). SQ SEQUENCE 710 AA; 77585 MW; B81ADAA0DF641080 CRC64; MEFCQDSRNG NGSPGFNTND PLNWGMAAES LKGSHLDEVK RMIEEYRNPV VKLGGETLTI GQVTAIASRD VGVMVELSEE ARAGVKASSD WVMDSMSKGT DSYGVTTGFG ATSHRRTKQG GELQKELIRF LNAGIFGNGT ESSHTLPRSA TRAAMLVRTN TLLQGYSGIR FEMLEAITKM INHNITPCLP LRGTITASGD LVPLSYIAGL LTGRPNSKAV GPNGEPLTPA EAFTQAGIDG GFFELQPKEG LALVNGTAVG SGLASMVLFE ANVLAILSEV LSAIFAEVMQ GKPEFTDHLT HKLKHHPGQI VAAAIMEHIL DGSAYVKEAQ KLHEIDPLQK PKQDRHALRT SPQWLGPLIE VIRTSTKMIE REINSVNDNP LIDVSRNKAL HGGNFQGTPI GVSMDNTRLA IASIGKLMFA QFSELVNDLY NNGLPSNLTG GRNPSLDYGF KGAEIAMASY CSELQFLDQS CTNHVQSAEQ HNQDVNSLGL ISSRKTAEAI DILKLMSTTF LVGLCHSVDL RHIEENLKNT VKISVSQLPR VLTMGFNGEL HPSRFCEKDL LKVVDREHVF SYIDDPCSAT YPLMQKLRQV LVEHALVNGE KVRNSTTSIF QKIGSFEEEL KTLLPKEVES ARLEVENGNP AIPNRIKECR SYPLYKFVRE ELGTSLLTGE KVKSPGEEFD KVFTAICAGK LIDPLLECLK EWDGAPLPIC //