PALY_FLAVE
ID PALY_FLAVE Reviewed; 724 AA.
AC A0A0A7AAW9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0000303|PubMed:26539050};
DE EC=4.3.1.24 {ECO:0000250|UniProtKB:A0A4Y6HUI7};
DE AltName: Full=FvPAL {ECO:0000303|PubMed:26539050};
GN Name=PAL1 {ECO:0000312|EMBL:AHD25301.1};
OS Flammulina velutipes (Agaricus velutipes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Physalacriaceae; Flammulina.
OX NCBI_TaxID=38945 {ECO:0000312|EMBL:AHD25301.1};
RN [1] {ECO:0000312|EMBL:AHD25301.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=26539050; DOI=10.5941/myco.2015.43.3.327;
RA Yun Y.H., Koo J.S., Kim S.H., Kong W.S.;
RT "Cloning and Expression Analysis of Phenylalanine Ammonia-Lyase Gene in the
RT Mycelium and Fruit Body of the Edible Mushroom Flammulina velutipes.";
RL Mycobiology 43:327-332(2015).
CC -!- FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to
CC form trans-cinnamic acid and a free ammonium ion (By similarity).
CC Facilitates the commitment step in phenylpropanoid pathways that
CC produce secondary metabolites such as lignins, coumarins and flavonoids
CC (By similarity). {ECO:0000250|UniProtKB:A0A4Y6HUI7,
CC ECO:0000250|UniProtKB:P11544}.
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:A0A4Y6HUI7};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P11544}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expression is the highest in mycelia, and
CC decreases during fruiting body development (PubMed:26539050). In the
CC fruiting body, present in the stipe but not in the pileus
CC (PubMed:26539050). {ECO:0000269|PubMed:26539050}.
CC -!- INDUCTION: Induced when grown in presence of ammonium nitrate, L-
CC phenylalanine, L-tryptophan and L-tyrosine.
CC {ECO:0000269|PubMed:26539050}.
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; KF737393; AHD25301.1; -; Genomic_DNA.
DR SMR; A0A0A7AAW9; -.
DR UniPathway; UPA00713; UER00725.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045548; F:phenylalanine ammonia-lyase activity; ISS:UniProtKB.
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..724
FT /note="Phenylalanine ammonia-lyase"
FT /id="PRO_0000454790"
FT ACT_SITE 99
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 265
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 493
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 205
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT CROSSLNK 204..206
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 724 AA; 78095 MW; 8E6284281BEB424B CRC64;
MPSELFDLDN ARAARDTFLD ARRTATLLHK FLDSHRELKS YKNGRTINVD GHTLSLAAVT
AAARYNANVE LSQSAQVKEG VEKSRAVIAE KVEQGTSVYG VSTGFGGSAD TRTDQPLKLQ
QALLQHQHAG VLPSSSKTLG VLPLMDPMAA TSMPEAWVRG AMLIRMNSLI RGHSGVRWEL
IEKINDLLRA NITPVVPLRS SISASGDLSP LSYVAGTLTA NPSIRVFDGP SAFGARKMVS
SRDALAAHKI KPVTLASKEG LGILNGTAFS AAVASLALTE ATHLALLAQV CTALGTEALC
GTTGSYAPFI HVTARPHPGQ IEAANNMWNL LQGSKLASGH EEEVSINQDK YELRQDRYPL
RTSPQFLGPQ IEDILAALAS VTQECNSTTD NPLVDGNTGE VHHGGNFQAM AISNAMEKTR
LAVHHIGKLM FSQSTELVNP AMNHGLPPSL AASDPSLNYH GKGVDIATAA YVSELGYLAN
PVTTHIQSAE MHNQAVNSLA LISARATVTS LDVLTILMSS YLYLLCQAVD LRALRRDLDV
GVRAIIAEEV SKLFSNNLSS EEMDLLHSSL YSKYQHTMDK TTTMDAVDQM KEVTASFAPM
LVEVFTSTRV MPDALSAIPR FRSNISSRAT QLFDRLRASY LSGERGATPA SSLLGRTRSV
YEFIRVSLGI RMHGSENYSA FANGLGVDDP TIGQNISSIY EAIRDGKFHD VVADLFEALP
RSKL
