ID PALY_MEDSA Reviewed; 725 AA. AC P27990; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 16-JUN-2009, entry version 60. DE RecName: Full=Phenylalanine ammonia-lyase; DE EC=4.3.1.24; OS Medicago sativa (Alfalfa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Trifolieae; OC Medicago. OX NCBI_TaxID=3879; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Apollo; RX MEDLINE=91355933; PubMed=1715786; DOI=10.1007/BF00040636; RA Gowri G., Paiva N.L., Dixon R.A.; RT "Stress responses in alfalfa (Medicago sativa L.) 12. Sequence RT analysis of phenylalanine ammonia-lyase (PAL) cDNA clones and RT appearance of PAL transcripts in elicitor-treated cell cultures and RT developing plants."; RL Plant Mol. Biol. 17:415-429(1991). 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; X58180; CAA41169.1; -; mRNA. DR PIR; S17444; S17444. DR HSSP; P21310; 1GKM. DR SMR; P27990; 34-725. DR BRENDA; 4.3.1.5; 815. 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 1 725 Phenylalanine ammonia-lyase. FT /FTId=PRO_0000215400. FT COMPBIAS 24 27 Poly-Asn. FT MOD_RES 212 212 2,3-didehydroalanine (Ser) (By FT similarity). FT CROSSLNK 211 213 5-imidazolinone (Ala-Gly) (By FT similarity). SQ SEQUENCE 725 AA; 78866 MW; 19906A2575F64D7D CRC64; METISAAITK NNANESFCLI HAKNNNNMKV NEADPLNWGV AAEAMKGSHL DEVKRMVAEY RKPVVRLGGE TLTISQVAAI AAHDHGVQVD LSESARDGVK ASSEWVMESM NKGTDSYGVT TGFGATSHSR TKQGGALQKE LIRFLNAGIF GNGTESNHTL PKTATRAAML VRINTLLQGY SGIDFEILEA ITKPLNKTVT PCLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKAHGPSGEV LNAKEAFNLA GINAEFFELQ PKEGLALVNG TAVGSGLASI VLFEANILAV LSEVLSAIFA EVMQGKPEFT DHLTHKLKHH PGQIEAAAIM EHILDGSSYV KAAKKLHEID PLQKPKQDRY ALRTSPQWLG PLVEVIRFST KSIEREINSV NDNPLIDVSR NKALHGGNFQ GTPIGVSMDN TRLALASIGK LMFAQFSELV NDFYNNGLPS NLSASRNPSL DYGFKGAEIA MASYCSELQY LANPVTTHVQ SAEQHNQDVN SLGLISARKT NEAIEILQLM SSTFLIALCQ AIDLRHLEEN LKNSVKNTVS QVAKKTLTMG VNGELHPSRF CEKDLLKVVD REHVFAYIDD PCSATYPLSQ KLRQVLVDHA LVNGESEKNF NTSIFQKIAT FEEELKTLLP KEVESARTAY ESGNPTIPNK INGCRSYPLY KFVREELGTG LLTGENVISP GEECDKLFSA MCQGKIIDPL LECLGEWNGA PLPIC //