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   03-AUG-2022, entry version 103.
DE   RecName: Full=Phenylalanine ammonia-lyase G2B;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PALG2B;
OS   Populus kitakamiensis (Aspen) (Populus sieboldii x Populus grandidentata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=34292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   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 the
RT   phenylalanine ammonia-lyase gene family from Populus kitakamiensis.";
RL   Plant Mol. Biol. 28:1133-1141(1995).
CC   -!- FUNCTION: This is a key enzyme of plant metabolism catalyzing the first
CC       reaction in the biosynthesis from L-phenylalanine of a wide variety of
CC       natural products based on the phenylpropane skeleton.
CC       {ECO:0000250|UniProtKB:P24481}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-phenylalanine = (E)-cinnamate + NH4(+);
CC         Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58095; EC=4.3.1.24;
CC         Evidence={ECO:0000250|UniProtKB:P24481};
CC   -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC       trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P24481}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC       is formed autocatalytically by cyclization and dehydration of residues
CC       Ala-Ser-Gly. {ECO:0000250|UniProtKB:Q68G84}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR   EMBL; D43802; BAA07860.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q43052; -.
DR   SMR; Q43052; -.
DR   UniPathway; UPA00713; UER00725.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009800; P:cinnamic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00332; PAL-HAL; 1.
DR   Gene3D; 1.10.274.20; -; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   InterPro; IPR001106; Aromatic_Lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR   InterPro; IPR005922; Phe_NH3-lyase.
DR   InterPro; IPR023144; Phe_NH3-lyase_shielding_dom_sf.
DR   PANTHER; PTHR10362; PTHR10362; 1.
DR   Pfam; PF00221; Lyase_aromatic; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR01226; phe_am_lyase; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT   CHAIN           1..710
FT                   /note="Phenylalanine ammonia-lyase G2B"
FT                   /id="PRO_0000215414"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        103
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         482
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         198
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        197..199
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
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