PAL1_TOBAC
ID PAL1_TOBAC Reviewed; 715 AA.
AC P25872;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phenylalanine ammonia-lyase;
DE EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN Name=TPA1; Synonyms=PALB;
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 [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RX PubMed=8624404; DOI=10.1007/bf00019006;
RA Fukasawa-Akada T., Kung S.D., Watson J.C.;
RT "Phenylalanine ammonia-lyase gene structure, expression, and evolution in
RT Nicotiana.";
RL Plant Mol. Biol. 30:711-722(1996).
RN [2]
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 -!- TISSUE SPECIFICITY: Expressed in flowers, roots, leaves and stems.
CC {ECO:0000269|PubMed:8624404}.
CC -!- DEVELOPMENTAL STAGE: Expression declines during flower maturation but
CC increases during leaf maturation. {ECO:0000269|PubMed:8624404}.
CC -!- INDUCTION: Rapidly induced after wounding.
CC {ECO:0000269|PubMed:8624404}.
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; M84466; AAA34122.1; -; Genomic_DNA.
DR EMBL; AB008200; BAA22948.1; -; Genomic_DNA.
DR PIR; S66343; S66343.
DR RefSeq; XP_016435186.1; XM_016579700.1.
DR AlphaFoldDB; P25872; -.
DR SMR; P25872; -.
DR STRING; 4097.P25872; -.
DR GeneID; 107761482; -.
DR KEGG; nta:107761482; -.
DR OMA; MYVHSIP; -.
DR OrthoDB; 923557at2759; -.
DR PhylomeDB; P25872; -.
DR BRENDA; 4.3.1.24; 3645.
DR SABIO-RK; P25872; -.
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..715
FT /note="Phenylalanine ammonia-lyase"
FT /id="PRO_0000215423"
FT ACT_SITE 107
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 202
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 201..203
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 715 AA; 77781 MW; 03CB4E8527394C62 CRC64;
MASNGHVNGG ENFELCKKSA DPLNWEMAAE SLRGSHLDEV KKMVSEFRKP MVKLGGESLT
VAQVAAIAVR DKSANGVKVE LSEEARAGVK ASSDWVMDSM NKGTDSYGVT TGFGATSHRR
TKNGGALQKE LIRFLNAGVF GNGTETSHTL PHSATRAAML VRINTLLQGY SGIRFEILEA
ITKLINSNIT PCLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKAVGPNGET LNAEEAFRVA
GVNGGFFELQ PKEGLALVNG TAVGSGMASM VLFDSNILAV MSEVLSAIFA EVMNGKPEFT
DHLTHKLKHH PGQIEAAAIM EHILDGSSYV KAAQKLHEMD PLQKPKQDRY ALRTSPQWLG
PQIEVIRAAT KMIEREINSV NDNPLIDVSR NKALHGGNFQ GTPIGVSMDN ARLALASIGK
LMFAQFSELV NDYYNNGLPS NLTASRNPSL DYGFKGAEIA MASYCSELQF LANPVTNHVQ
SAEQHNQDVN SLGLISARKT AEAVDILKLM SSTYLVALCQ AIDLRHLEEN LKNAVKNTVS
QVAKRTLTMG ANGELHPARF CEKELLRIVD REYLFAYADD PCSCNYPLMQ KLRQVLVDHA
MNNGESEKNV NSSIFQKIGA FEDELKAVLP KEVESARAAL ESGNPAIPNR ITECRSYPLY
RFVRKELGTE LLTGEKVRSP GEECDKVFTA MCNGQIIDPM LECLKSWNGA PLPIC
