PAL2_TOBAC
ID PAL2_TOBAC Reviewed; 712 AA.
AC P35513; O22114;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Phenylalanine ammonia-lyase;
DE EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN Name=PALA;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8165251; DOI=10.1104/pp.104.3.1091;
RA Nagai N., Kitauchi H., Shimosaka M., Okazaki M.;
RT "Cloning and sequencing of a full-length cDNA coding for phenylalanine
RT ammonia-lyase from tobacco cell culture.";
RL Plant Physiol. 104:1091-1092(1994).
RN [2]
RP SEQUENCE REVISION.
RA Nagai N., Kitauchi H., Shimosaka M., Okazaki M.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Bright Yellow; TISSUE=Callus;
RA Taguchi G., Sharan M., Gonda K., Yanagisawa K., Shimosaka M., Hayashida N.,
RA Okazaki M.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
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; D17467; BAA22963.1; -; mRNA.
DR EMBL; AB008199; BAA22947.1; -; Genomic_DNA.
DR PIR; T01858; T01858.
DR RefSeq; NP_001312352.1; NM_001325423.1.
DR AlphaFoldDB; P35513; -.
DR SMR; P35513; -.
DR STRING; 4097.P35513; -.
DR GeneID; 107786762; -.
DR KEGG; nta:107786762; -.
DR BRENDA; 4.3.1.24; 3645.
DR SABIO-RK; P35513; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
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..712
FT /note="Phenylalanine ammonia-lyase"
FT /id="PRO_0000215424"
FT ACT_SITE 104
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 483
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 199
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 198..200
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 712 AA; 77345 MW; E65F8A867FEA2C41 CRC64;
MAGVAQNGHQ EMDFCMKVDP LNWEMAADSL KGSHLDEVKK MVAEFRKPVV KLGGETLTVA
QVAAIAAKDN VKTVKVELSE GARAGVKASS DWVMDSMGKG TDSYGVTTGF GATSHRRTKN
GGALQKELIR FLNAGVFGNG TESCHTLPQS GTRAAMLVRI NTLLQGYSGI RFEILEAITK
LLNHNVTPCL PLRGTITASG DLVPLSYIAG LLTGRPNSKA VGPNGETLNA EEAFRVAGVN
GGFFELQPKE GLALVNGTAV GSGLASMVLF DANVLAVFSE VLSAIFAEVM NGKPEFTDHL
THKLKHHPGQ IEAAAIMEHI LDGSSYVKAA QKLHETDPLQ KPKQDRYALR TSPQWLGPQI
EVIRSATKMI EREINSVNDN PLIDVSRNKA LHGGNFQGTP IGVSMDNARL ALASIGKLMF
GQFSELVNDY YNNGLPSNLT AGRNPSLDYG FKGSEIAMAS YCSELQFLAN PVTNHVQSAE
QHNQDVNSLD LISARKTAEA VDILKLMSST YLVALCQAID LRHLEENLRN AVKNTVSQVA
KRTLTMGTNG ELHPSRFCEK DLLRVVDREY VFAYADDACS ANYPLMQKLR QVLVDHALQN
GENEKNANSS IFQKILAFED ELKAVLPKEV ESARAALESG NPAIANRIKE CRSYPLYRFV
RGELGAELLT GEKVRSPGEE CDKVFTAMCN GQIIDSLLEC LKEWNGAPLP IC
