ID   PAL2_CICAR              Reviewed;         718 AA.
AC   Q9SMK9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Phenylalanine ammonia-lyase 2;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL2;
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. ILC 3279;
RA   Hein F., Overkamp S., Barz W.;
RT   "Cloning and characterization of a full length cDNA encoding phenylalanine
RT   ammonia-lyase (PAL) from chickpea (Cicer arietinum L.).";
RL   (er) Plant Gene Register PGR00-038(2000).
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; AJ250836; CAB60719.1; -; mRNA.
DR   RefSeq; NP_001266106.1; NM_001279177.1.
DR   RefSeq; XP_012570018.1; XM_012714564.1.
DR   AlphaFoldDB; Q9SMK9; -.
DR   SMR; Q9SMK9; -.
DR   STRING; 3827.XP_004496257.1; -.
DR   GeneID; 101509831; -.
DR   KEGG; cam:101509831; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   OrthoDB; 923557at2759; -.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000087171; Chromosome Ca4.
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   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism;
KW   Reference proteome.
FT   CHAIN           1..718
FT                   /note="Phenylalanine ammonia-lyase 2"
FT                   /id="PRO_0000215388"
FT   ACT_SITE        110
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         386
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         489
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         205
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        204..206
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   718 AA;  78301 MW;  0290D012C6E68B24 CRC64;
     MMELPNGNCN GSSLNVCNGN GNLSNNDSLN WGMAADSMRG SHLDEVKRMV EEYRKAVVPL
     GGKGLTISQV AAVATQNTGV AVELAEETRY AVKASSDWVV DSMNKGTDSY GVTTGFGATS
     HRRTKQGGAL QNELIRFLNA GIFGNGTEST QTLPHTATRA AMLVRINTLL QGYSGIRFEI
     MEAIAKFLNH NITPCLPLRG TITASGDLVP LSYVAGLLIG RPNSKSIGPN GQILNAKEAF
     QLAGIETGFF ELQPKEGLAL VNGTAVGSGL ASLALFETNL LVVLSEILSA IFAEVMQGKP
     EFTDHLTHKL KHHPGQIEAA AIMEHILDGS YYVKAAQKVH DIDPLQKPKQ DRYALRTSPQ
     WLGPQIEVIR NATKMIEREI NSVNDNPLID VSRNKALHGG NFQGTPIGVS MDNTRLAIAS
     IGKLMFAQFS ELVNDFYNNG LPSNLTGSRN PSLDYGFKGA EIAMASYCSE LQYLANPVTN
     HVQSAEQHNQ DVNSLGLISS RKTAEAVEIL KLMSSTFLVA LCQAIDLRHI EENLKSVVKN
     TVSQVAKRVL TVGVNGELHP SRFCEKDLLN VVEREYVFAY IDDPCSATYP LMQKLRHVLV
     DHALENGDRE GNSSTSIFQK IGAFEQELKT LLPKEVESVR VDVENGNPAV PNRIIECRSY
     PLYKFVRENL GTSLLTGEKI RSPGEECDKV FAALCDGRFI DPMLDCLKEW NGAPLPIC