PALY1_PLEOS
ID PALY1_PLEOS Reviewed; 743 AA.
AC A0A4Y6HUI7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Phenylalanine ammonia-lyase 1 {ECO:0000303|PubMed:31655558};
DE EC=4.3.1.24 {ECO:0000269|PubMed:31655558};
DE AltName: Full=PoPAL1 {ECO:0000303|PubMed:31655558};
GN Name=PAL1 {ECO:0000303|PubMed:31655558};
OS Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5322 {ECO:0000312|EMBL:QDF60494.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=CCMSSC00389 {ECO:0000303|PubMed:31655558};
RX PubMed=31655558; DOI=10.1186/s12866-019-1594-4;
RA Hou L., Wang L., Wu X., Gao W., Zhang J., Huang C.;
RT "Expression patterns of two pal genes of Pleurotus ostreatus across
RT developmental stages and under heat stress.";
RL BMC Microbiol. 19:231-231(2019).
CC -!- FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to
CC form trans-cinnamic acid and a free ammonium ion (PubMed:31655558).
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:P11544,
CC ECO:0000269|PubMed:31655558}.
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:0000269|PubMed:31655558};
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 higher in fruiting bodies and spores
CC than in primordia, and very low in mycelia (PubMed:31655558). In the
CC fruiting body, present in the cap, gill, pileipellis but not in the
CC stipe (PubMed:31655558). {ECO:0000269|PubMed:31655558}.
CC -!- INDUCTION: Induced by thermal stress. {ECO:0000269|PubMed:31655558}.
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 -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in delayed
CC primordium formation. {ECO:0000269|PubMed:31655558}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; MK207023; QDF60494.1; -; mRNA.
DR SMR; A0A4Y6HUI7; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1112899; -.
DR UniPathway; UPA00713; UER00725.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0009800; P:cinnamic acid biosynthetic process; IC:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT CHAIN 1..743
FT /note="Phenylalanine ammonia-lyase 1"
FT /id="PRO_0000454791"
FT ACT_SITE 120
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 225
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT CROSSLNK 224..226
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 743 AA; 79841 MW; 641A8C4561D59A4C CRC64;
MTILSADTLS ITRPYSNSLS TLKVIATPVT ESPPSPVASS ISPNATNLVE EFINAHKELQ
SYKSGRPVVL DGHTLSIAAV AAAARYDAGV ELDDSPLVKD RLLQSRQVVA DKVEQGTSIY
GVTTGFGGSA DTRTDQPILL GNALMQMQHS GILPSSSKPL DALPLQDPFG LAMPESWVRG
AMLIRMNSLI RGHSGVRWEL IEKMNDLLRA NITPVVPLRG SISASGDLQP LSYVAGALYG
NPSIRVFDGE RTSALGPRKI VSSVEALEAH SISPISLACK EHLGILNGTA FSASVAALAL
HDAVHLTLLT QVLTAMGAEA LAGTRGNFDP FIHAVARPHP GQIETADVIW NLLEGSKFAT
TEEEEMTIDE DKGHLRQDRY PLRTSPQFIG PQVEDLIASL ATITLECNST TDNPLVDGET
GKVHNGGNFQ AMAVTNAMEK TRLSLHHLGK LVFSQCAELI NPTMNRGLPP SLAATDPSLN
YHAKGIDIAS AAYVAELGYL ANPVSTHIQS AEMHNQAINS MALVSGRATI TSLEVLSLLI
SSYLYAICQA LDLRALQHEL YEGLDAIVKE EIIAAFSPFL DDYEITRFTA ISCHIVRDAM
DSTSTMDAKD RMTSVAASLT TPLVDFLTGE AFSDVVSAGQ ALTTIPAFRA RIAARGYELL
DELRRAYLSG GRGLAPASRF LNKTRPVYEF VRLTLGIKMH GAENYNDFEN GVGVDDVTTG
QNVSLIHEAI RDGKLQPIIV DLF
