PAL1_PEA
ID PAL1_PEA Reviewed; 723 AA.
AC Q01861;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Phenylalanine ammonia-lyase 1;
DE EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN Name=PAL1;
OS Pisum sativum (Garden pea).
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; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1515609; DOI=10.1007/bf00029163;
RA Kawamata S., Yamada T., Tanaka Y., Sriprasertsak P., Kato H., Ichinose Y.,
RA Kato H., Shiraishi T., Oku H.;
RT "Molecular cloning of phenylalanine ammonia-lyase cDNA from Pisum
RT sativum.";
RL Plant Mol. Biol. 20:167-170(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Midoriusui; TISSUE=Epicotyl;
RA Yamada T., Tanaka Y., Sriprasertsak P., Kato H., Hashimoto T., Kawamata S.,
RA Ichinose Y., Kato H., Shiraishi T., Oku H.;
RT "Phenylalanine ammonia-lyase genes from Pisum sativum: structure, organ-
RT specific expression and regulation by fungal elicitor and suppressor.";
RL Plant Cell Physiol. 33:715-725(1992).
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: Present at high levels in roots, with slightly
CC higher amounts in roots with nodules than those without, and at
CC moderate levels in stems. Low levels also present in lower leaves.
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; D10001; BAA00885.1; -; mRNA.
DR EMBL; D10002; BAA00886.1; -; Genomic_DNA.
DR PIR; S25303; S25303.
DR AlphaFoldDB; Q01861; -.
DR SMR; Q01861; -.
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 2: Evidence at transcript level;
KW Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT CHAIN 1..723
FT /note="Phenylalanine ammonia-lyase 1"
FT /id="PRO_0000215403"
FT ACT_SITE 116
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 494
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 210
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 209..211
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 723 AA; 78831 MW; 41E2A73F2B98BE7E CRC64;
METVAAAITK NNGYESFCVT NAKNNNMKVN SADPLNWGVA AEAMKGSHLD EVKRMVEEYR
KPVVRLGGET LTISQVAAIA AHDHGVKVEL SESARAGVKA SSDWVMESMN KGTDSYGVTT
GFGATSHRRT KQGGALQKEL IRFLNAGIFG NGTESSHTLP HTATRAAMLV RINTLLQGYS
GIRFEILEAI TKLINNNVTP CLLRGTITAS GDLVPLSYIA GLLTGRPNSK AHGTSGEILN
AKEAFQSAEI NDGFFELQPK EGLALVNGTA VGSGLASIVL FEANILAVLS EVLSAIFAEV
MQGKPEFTDH LTHKLKHHPG QIEAAAIMEH ILDGSAYVKA AKKLHEMDPL QKPKQDRYAL
RTSPQWLGPL IEVIRFSTKS IEREINSVND NPLIDVSRNK ALHGGNFQGT PIGVSMDNTR
LALASIGKLL FAQFSELVND FYNNGLPSNL SASRNPSLDY GFKGSEIAMA SYCSELQYLA
NPVTTHVQSA EQHNQDVNSL GLISSRKTYE AIEILQLMSS TFLIALCQAV DLRHLEENLK
NSVKNIVSQV AKRTLTTGVN GELHPSRFCE KDLLRVVDRE HVFAYIDDPC SATYPLMQKL
RQVLVDHALV NGESEKNLNT SIFQKIATFE DELKTLLPKE VESTRAAYES GNPTVPNKIN
GCRSYPLYRF VRQELGTGLL TGEKVISPGE ECDKLFTAIC QGKIIDPLLQ CLGDWNGAPL
PIS
